Dictionary of Protein Secondary Structure Pattern Recognition

Dictionary of Protein Secondary Structure:
Pattern Recognition of Hydrogen-Bondedand

Geometrical Features
WOLFGANG KABSCH and CHRISTIAN SANDER, Biophysics

Department, Max Planck Institute of Medical Research, 6900
Heidelberg, Federal Republic of Germany
Synopsis
For a successful analysis of the relation between amino acid sequence and protein structure,
an unambiguous and physically meaningful definition of secondary structure is essential. We
have developed a set of simple and physically motivated criteria for secondary structure,
programmed as a pattern-recognition process of hydrogen-bonded and geometrical features
extracted from x-ray coordinates. Cooperative secondary structure is recognized as repeats
of the elementary hydrogen-bonding patterns turn and bridge. Repeating turns are
helices, repeating bridges are ladders, connected ladders are sheets. Geometric
structure is defined in terms of the concepts torsion and curvature of differential geometry.
Local chain chirality is the torsional handedness of four consecutive Ca positions and is
positive for right-handed helices and negative for ideal twisted @-sheets. Curved pieces are
defined as bends. Solvent exposure is given as the number of water molecules in possible
contact with a residue. The end result is a compilation of the primary structure, including
SS bonds, secondary structure, and solvent exposure of 62 different globular proteins. Th e
presentation is in linear form: strip graphs for an overall view and strip tables for the details
of each of 10,925 residues. The dictionary is also available in computer-readable form for
protein structure prediction work.
INTRODUCTION
Background
a-Helices and pleated @-sheetswere predicted in 1951 by Linus Pauling
and Robert Corey on the basis of hydrogen-bonding and cooperativity
criteria. They were seen later, and beautifully, in the first structures shown
in atomic detail by x-ray crystallography. Since then, the number of known
protein structures has risen to over 100 and comprehensive analysis of
secondary structure requires a computerized compilation of structure as-
signments, especially in the context of structure prediction methods.
Existing compilations have various shortcomings. The crystallographers
assignments of secondary structure in the Brookhaven Protein Data Bank2
are often subjective and sometimes incomplete. Objective algorithms exist,
e.g., for defining turn^^-^ (reviewed in Refs. 7, 8), P-sheets? and solvent
accessibility,1 but only Levitt and Greerll have published an extensive
compilation of automatic assignments of helices and sheets. Their ap-
Biopolymers, Vol. 22,2577-2637 (1983)

0 1983 John Wiley & Sons, Inc. CCC 0006-3525/83/122577-61$07.10
2578 KABSCH AND SANDER
proach has the advantage of giving assignments when only backbone Ca

coordinates are known; the price paid is loss of accuracy when all-atom
coordinates are known. Solvent exposure has been published for no more
than a few proteins, and chirality only on microfiche.12 We are thus mo-
tivated to make available an accurate?exhaustive, and up-to-date compi-
lation.
The Main Ideas

Our goal is to approximate the intuitive notion of secondary structure
by an objective algorithm. An algorithm for extracting structural features
from the atomic coordinates is obviously a pattern-recognition process.
The elementary patterns on which this process is based should be as simple
as possible yet capable of discriminating among the main types of secondary
structure. To discriminate whether a pattern is present or not in a con-
tinuum ofpossible atomic configurations, continuous decision parameters
must be fixed. Using backbone p,+ angles or Ca positions requires the
adjustment of several parameters, e.g., four angles for a rectangle in the p,$
plane for each type of secondary structure. In contrast, the presence or
absence of an H bond can be characterized by a single decision parameter,
a cutoff in the bond energy. Therefore, we base our secondary structure
recognition algorithm mainly on H-bonding patterns: n-turns with an
+
H-bond between the CO of residue i and the NH of residue i n , where n
= 3,4,5, and bridges with H bonds between residues not near each other
in sequence. These two types of pattern essentially exhaust all back-
bone-backbone H bonds. Repeating 4-turns define a-helices, and re-
peating bridges define 0-structure, in good agreement with intuitive as-
signments. All other occurrences of the basic patterns provide an inter-
esting survey of 3lo-helices, rhelices, single turns, and single &bridges.
The results are presented in short form as strip maps of secondary
structure (Fig. A l ) , and in long form, together with the amino acid sequence
as an easy-to-use dictionary (Table AIII). The computer program DSSP
(Define Secondary Structure of Proteins) written in standard PASCAL will
be available from the Protein Data Bank, Chemistry Dept., Brookhaven
National Laboratory, Upton, N.Y. 11973. Publication of an update of this
compilation is planned as more protein structures are solved.
DEFINITIONS
The definitions of H-bonded features form a hierarchy: first H bonds
are defined; based on them, turns and bridges; and, based on them, a-helices
and @-ladders,including common imperfections such as helical kinks and
@-bulges. Features defined geometrically are bends, chirality, SS bonds,
and solvent exposure. Each structural feature is defined independently
of the others and structural overlaps are resolved by defining a secondary
structure summary that assigns a single state to each residue. For brevity
we express the pattern definitions in the form of equations. For example,
DICTIONARY OF PROTEIN SECONDARY STRUCTURE 2579
I
:40 -
120 -
0-c
hF;\
100 -
e
40
20 \\ \
\ \ \
\ I \ \
0
2.5 3.0 3.5 4.0 4.5 5.0 5.5
Fig. 1. H bond between peptide units is described here by the dominant electrostatic part
E (see text) of the H-bond energy, drawn in contours of constant E a t 0.5 kcal/mol intervals
as a function of the distance, d , and the alignment angle 0. Dotted lines, E positive or zero;
broken lines, E negative. An ideal H bond has d = 2.9 A, 19 = 0, and E = -3.0 kcal/mol. We
assume an H bond for E up to - 0.5 kcal/mol (solid line). Thus, misalignment of up to 63
is allowed a t the ideal length; an N - 0 distance of up to d = 5.2 8, is allowed for perfect align-
ment. This definition of H bonds is particularly simple and physically meaningful. It is more
general than the historical definition of hydrogen bond and could be called polar interac-
tion.
Hbond(ij)=: [E < -0.5kcal/mole] means: there is an H bond (ij)if

E is less than -0.5 kcal/mol.
Hydrogen-Bonded Structure
Hydrogen Bonds
Hydrogen bonds in proteins have little wave-function overlap and are
well described by an electrostatic m0de1.l~ We calculate the electrostatic
interaction energy between two H-bonding groups by placing partial
charges on the C,O (+q1, - q1) and N,H (-q2, q 2 ) atoms, i.e., +
E = qlq2(1/r(0N) + l/r(CH) - l/r(OH) - l/r(CN))*f
with q1 = 0.42e and q 2 = 0.20e, e being the unit electron charge and r(AB)
the interatomic distance from A to B. In chemical units, r is in angstroms,
the dimensional factor f = 332, and E is in kcal/mol. A good H bond has
about -3 kcal/mol binding energy. We choose a generous cutoff to allow
for bifurcated H bonds and errors in coordinates and assign an H bond
between C=O of residue i and N-H of residue j if E is less than the cutoff,
i.e., Hbond(ij)=: [E < -0.5kcal/mole].
Figure 1illustrates the relation of this one-parameter definition to the
3-turn
> 3 3 < no t a t i o n
residues
H-bond
4-turn
notation
residues
H-bond
5-turn
notation
residues
H-bond
p a r a l l e l bridge
not a t ion
residues
H-bonds
( \ and / , or .)
residues
notation
a n t i p a r a l l e l bridge
notation
residues
H-bonds
( ! o r .)
residues
notation
bend
-
notation
re s f due s
d i r e c t i o n change
more t h a n 70
degrees
chirality
f o u r C(a1pha) atoms
define t h e dihedral
angle alpha
Fig. 2. Elementary patterns used in structure definition

more complicated description of H bonds in terms of one distance and one

angle. There is no generally correct H-bond definition, as there is no sharp
border between the quantum-mechanical (wave-function overlap domi-
nates a t short distances) and electrostatic (electrostatic interaction dom-
inates a t larger distances) regimes and no discontinuity of the interaction
energy as a function of distance or alignment. Thus, any H-bond definition
is empirically tailored to a particular purpose. Our definition, well tested
by trial and error, reflects a compromise suitable for the purpose of sec-
ondary structure definition. The cutoff chosen, which allows for an N - 0
distance up to 2.2 A larger than the optimal value a t perfect alignment or
a misalignment of maximally 60 is similar to the tolerances used by Levitt
and Greerl (1.8 A excess and 60) and was found to be sufficient to average
over coordinate errors without leading to spurious secondary structure
assignments. Were it not for historical reasons, we would use the term
polar interaction rather than hydrogen bond.
Elementary H-Bond Pattern: n-Turn

The basic turn pattern (Fig. 2) is a single H bond of type (i,i + n). We
assign an n-turn a t residue i if there is an H bond from CO(i) to NH(Z + n ) ,
+
i.e., n-turn(i)=: Hbond(i,i n), n = 3,4,5.
When the pattern is found, the ends of the H bond are indicated by using
) a t i and ( a t i 4-n in line %TURN, 4-TURN, or 5-TURN of Table AIII;
the residues bracketed by the H bond are noted 3, 4, or 5 unless they
are also the end points of other H bonds. Coincidence of ) and ( a t
one residue is indicated by X. In line SUMMARY of Table AIII, residues
bracketed by the hydrogen bond of an n- turn are marked T,unless they
are part of an n-helix (defined below).
Elementary H-Bond Pattern: Bridge

Two nonoverlapping stretches of three residues each, i - 1,i,i + 1 and
+
j - l j j 1, form either a parallel or antiparallel bridge, depending on
which of two basic patterns (Fig. 2) is matched. We assign a bridge between
residues i and j if there are two H bonds characteristic of P-structure; in
particular,
Parallel Bridge(i,j)=: [Hbond(i - 1,j) and HbondCj,i + I)]or
[HbondG - 1,i) and Hbond(i,j + I)]
Antiparallel Bridge(i,j) =: [Hbond(i,j) and HbondCj,i)]or
[Hbond(i - 1,j + 1)and Hbondfi - 1,i + l)]
Parallel bridges are marked at i and j by lower-case letters, antiparallel ones
by upper-case letters.
Cooperative H-Bond Pattern: Helices

A minimal helix is defined by two consecutive n-turns. For example,
+
a 4-helix, of minimal length 4 from residues i to i 3, requires 4-turns at
residues i - 1and i ,
4-helix(i,i + 3)=: [4-turn(i - 1)and 4-turn(i)]
+
i.e., an H bond (i - 1,i +3) and an H bond (i,i 4). Note that nothing is
+ +
required about the H-bond state of residues i 1and i 2. Similarly, two
consecutive turns are required and a 3-helix of minimal length 3 from res-
idue i to i + 2 and a 5-helix of minimal length 5 from residue i to i 5: +
3-helix(i,i + a)=: [3-turn(i - 1)and 3-turn(i)]
5-helix(i,i + 5)=: [5-turn(i - 1)and 5-turn(i)]
Longer helices are defined as overlaps of minimal helices. Conventionally,
these structures are called a-helix, 3,10-helix,and 7r-helix. In Table AIII,
a 3-helix can be recognized by the pattern ) ) 3 ( (, a 4-helix by ) )44( (, and
a 5-helix by ) ) 555 ( (. In the line SUMMARY, the residues bracketed by H
bonds are labeled G, H, I, e.g.,
5-TURN ) )555( (
4-TURN ))44((
3-TURN ))3((
SUMMARY GGG HHHH 11111
These helices are one residue shorter at each end than they would be ac-
cording to rule 6.3 of IUPAC-IUB.14 Examples of a 3-helix and a 5-helix
are shown in Fig. 3.
Couperatiue H-Bond Patterns: /%Ladders and /3-Sheets
We coin the term ladder and define
ladder=: set of one or more consecutive bridges of identical type
sheet=: set of one or more ladders connected by shared residues
Ladders are given letter names, where a,b,c, . . . is for parallel, A,B,C . . .
for antiparallel arrangement. Along the sequence, the first ladder is named
a or A, the second b or B, etc. Sheets are also given letter names
A,B,C . . . When the alphabet is exhausted, names restart at a or A.
In Table AIII, each residue is labeled in line SHEET by the sheet name and
in lines BRIDGE by the names of the ladders in which it participates (at most
two, one on each side). In line SUMMARY, residues in single bridges (lad-
ders of length 1)are marked 3, all other ladder residues E (extended).
Thus, continuous stretches of E are /%strands. The P-sheet notation
is illustrated in Fig. 4.
Secondary Structure Irregularities
Long helices can deviate from regularity in that not all possible H bonds
(b)
Fig. 3. Stereoviews of secondary structure: (a) 3-helix (3lo-helix) and (b) 5-helix (*-helix).
(a) 3-Helix Gly232-Lys237 from triose phosphate isomerase (ITIM). In Table AIII, it appears
as the H-bond pattern
S-TURN
SUMMARY
SEQUENCE
3-Helices are not uncommon, but have only two or three weak H bonds with E about -1
kcal/mol and the C=O direction tilted away from the helix axis typically by 30". (b) 5-Helix
Gly181-Lys188 from alcohol dehydrogenase (4ADH), a t the C-terminal end of a 4-helix. In
Table AIII, it appears as the H-bond pattern
.!-TURN
SEQUENCE
5-Helices are extremely rare; the longest one, shown here, has three H bonds. All stereoviews
are by PLUTO (Sam Motherwell, unpublished). In Figs. 3 and 5, the larger atoms are backbone
atoms with 1/4 their hard-sphere radius (C-, 0.47; C of CO, 0.44; 0,0.35; N, 0.41 A) and in Fig.
4 with twice these values; side-chain atoms are small, with 0.20-A radius.
(b)
Fig. 4. Stereoviews of secondary structure: (a) antiparallel and parallel P-sheets with two
ladders (three strands) each. (a) Two connected antiparallel P-ladders from trypsin (IPTN).
The three participating strands are Va116(31)-Ser20(37), Ile46(63)-Gly51(69), and
Glue62(80)-Ala67(85), where the first number is the sequential residue number from Table
A111 and the number in parentheses the authors residue identifier. The corresponding H-
bond notation (Table AIII) is
SHEET.. ................. CCC.. .............. C C C C ........... . C C C C . . ..
BRIDGEZ.. ................................... NNNN... ..................
BRIDGE1 ................. KKK ............... K K K . . ............NNNN.. ..
SEQUENCE .............. VSLNS.. ............ IQVRLG.. ........ E Q F I S A ..
The middle strand participates in two ladders. Both ladders belong to sheet C. (b) Two
connected parallel P-ladders, Arg172(189)-Gly177(194), Thrl96(213)-Ile200(217),
Asp266(283)-Ala271(288) from glutathione reductase (BGRS). The corresponding H-bond
notation (Table AIII) is
SHEET .................EEEE ................ E E E ............. E E E E ....
BRIDGEZ..... ............ 1 1 I ...........................................
BRIDGE1 ................ k k k k ................ I 1 I ............. k k k k .....
SEQUENCE.. .......... . R S V I V G . . ............ T S L M I . . ......... DCLLWA ...
The first strand has two ladder partners. The three strands are part of sheet E.
are formed. This possibility is implicit in the above helix definition, e.g.,
two overlapping minimal helices offset by two or three residues are joined
into one helix:
))44( ( ))44((
+ ))44(( + ) )44((
= ) ) 4 )x ( 4( ( irregular = ) ) 4 4 ~ x 44( ( irregular
= HHHHHHH = HHHHHHHH
)) ) )x( ( ( ( perfect > > ) > X X ( ( ( ( perfect
even though the third and/or fourth H bond is missing, compared to a
perfect seven- or eight-residue helix. Such imperfections are often asso-
ciated with a kink in the helix, e.g., due to a proline residue.
For 6-structure, we define explicitly: a bulge-linked ladder consists of
two (perfect) ladders or bridges of the same type connected by at most one
extra residue on one strand and at most four extra residues on the other
strand. This definition follows Richardson's* observation of 6-bulges, a
frequent lattice fault in ,&sheets, but. includes more general bulges than
her main types. In naming ladders, a bulge-linked ladder is treated as one
ladder (lines BRIDGE). In line SUMMARY, all residues in bulge-linked
ladders are marked "E," including the extra residues.
Geometrical Structure
Bend
Bends are regions with high curvature. We quantify chain curvature
at the central residue i of five residues as the angle between the backbone
direction of the first three and the last three residues. This definition of
curvature is identical to that of Rose and Seltzer5 but slightly different from
that of Rackovsky and Scheraga.I5 For a bend at i, we require a curvature
of a t least 70". The cutoff value was chosen by visual inspection of three-
dimensional traces. With C" the position vector of C", we define
Bend(i) =: [angle ( ( C W - Ca(i - 2)),(C"(i + 2) - C"(i))) > 70"]
and assign "S" for a bend at residue i.
Chirality
We define chirality at each residue (except at the ends of the chain) as
(Fig. 2)
a(i) = dihedral angle(C"(i - l),C"(i),C"(i + l),C"(i + 2))
but report only the sign of a in Table AIII: "+"
if 0" < a < 180" and "-"
if -180" < a < 0". Note that most helices have positive, most twisted
,&ladders negative, chirality. We have found only one left-handed helix,
in thermolysin. This rare specimen is shown in Fig. 5.
Fig. 5. Stereoviews of secondary structure: illustration of chirality. This short left-handed

a-helix, Gln225-Val230 from thermolysin (2TLN)is the only one known to us. In Table A111
(note that chirality is entered a t the second residue of each quartet) it appears as:
CHIRALITY _--
4-TURN ))44( (
SUMMARY HHHH
SEQUENCE QDNGGV
SS Bonds
SS bonds, i.e., covalent links between the S Y atoms of two Cys residues,
are taken directly from the Data Bank SSBOND records, as they can be
considered part of the amino acid sequence (primary structure). For the
coordinate data sets used here, an S-S distance of less than 3.0 8, can also
serve as a definition. The SS bonds are given names a,b,c . . . , and the
participating residues noted by this name in the line SEQUENCE in Table
AIII. Thus, Cys appears in the amino sequence either as C or as a lower-
case letter.
Chain Breaks
Chain breaks are assumed if the peptide bond length (distance C-N)
exceeds 2.5 A. They are labeled ! and counted as a break residue. Thus,
! may reflect the absence of a chemical peptide bond, missing density in
the crystallography map, or coordinate errors. The residues for which there
are coordinates in the data set are numbered sequentially, including break
residues. The resulting residue numbers often agree with the authors
except for proteins numbered according to sequence homology or those with
missing density or chain breaks. In any case, inspection of the amino acid
sequence in Table A111 always allows unambiguous identification of a
residue.
Structure Summary
To make contact with the usual notation of secondary structure and to
facilitate comparison with intuitive assignments, we summarize secondary
structure in a single line (SUMMARY in Table AIII). Structural overlaps
are eliminated in this line by giving priority to H,B,E,G,I,T,S in this order,
i.e., when several symbols coincide, the first one in this list is written. For
example, a helix is also a series of bends, but the state helix is given higher
priority. Pieces of 3- or 5-helix, reduced to less than minimal size due to
overlaps, are labeled T. A blank, by implication, means a piece of low
curvature not in H-bonded structure.
Static Solvent Exposure

Physically, we are interested in the number of water molecules in direct
contact with the protein or with a particular part of the protein.
Geometrically, a very useful representation of a monomolecular layer
of water is the surface described by all possible positions of a water molecule
in touching contact with protein atoms. That was the idea of Lee and
Richardslo water sphere rolling around the protein surface. Note that the
surface associated with holes in the protein interior is very small, e.g., a hole
that accommodates just one water molecule has zero area. For most of the
protein exterior, however, the surface is proportional to the number of water
molecules in the first hydration shell.
Mathematically, one calculates the surface by integrating a step function
+
f over all points x on the surface of a sphere of radius r(atom) r(water)
around atom i. f = 1if a water sphere centered a t x (by definition in con-
tact with atom i ) does not intersect with any other protein atom; otherwise,
f = 0.
Algorithmically, we integrate by summing over a polyhedron made of
20,80,320, or more approximately equal triangles. The integration points
are the triangle centers, the weights are the triangle area. The polyhedron
is generated starting from an icosahedron; a recursive procedure then di-
vides each triangle into four by connecting the midpoints of the sides and
projects the three new vertices onto the surface of the sphere, ready for the
next level of recursion. The final polyhedron is reminiscent of the shells
of certain viruses and of Buckminster Fullers architecture of geodesic
domes. Hence, we call the algorithm geodesic sphere integration. It
is similar to the algorithm of Shrake and RupleyI6and conceptually simpler
than z-layer integration.
With 320 integration points, the surface area of a residue is accurate to
within 1Az;with 80 points, to within 4 A2. For myoglobin, the numerical
values agree with those of Lee and Richards,lo using their parameters. The
numbers given here are based on slightly different values of atomic radii:
1.40 for 0,1.65 for N, 1.87 for Ca,1.76 for C of CO in the backbone, 1.80 for
2588 KABSCH A N D SANDER
all side-chain atoms,17 and 1.40 for a water molecule following observed
water-protein distances (Ref. 18 as cited in Ref. 19).
In Table AIII, we report the average number, W ,of water molecules in
contact with each residue. W can be estimated from the surface area by
Area
W= =-Area
V(water molecule)2/3 10
since the surface is proportional to the volume of the monolayer, which,
in turn, is proportional to the average number of molecules in the mono-
layer. For a water molecule volume of 30 A3 and area in A2, the conversion
factor is 9.65 N 10. Note that solvent exposure differs for a monomer and
a dimer: here, it is calculated in the presence of all monomers in the data
set (Table AI) but omitting HETATOMs (substrates, ligands, heme, etc.).
The sum over all residues is the total solvent exposure of the protein.
RESULTS AND DISCUSSION
Choice of Proteins
Of the more than 100 coordinate data sets in the Protein Data Bank,2
about 75 have complete backbone coordinates and a known amino acid
sequence. When two protein data sets had more than a 50% sequence
homology, i.e., identical amino acids in equivalent positions, the one with
higher resolution, better refinement, or more secondary structure was
chosen as representative, e.g., the first one was chosen of these pairs: serine
proteinase lSGA=lSGB by 61%;lactate dehydrogenases 4LHD=lLDX
by 63%; carbonic anhydrase lCAC=lCAB by 60%; chymotrypsin
2GCH=2CHA by 98%. Both were chosen of the following pairs: sulfhy-
dry1 proteinases actinidin/papain 2ACT=8PAP by 47%; immunoglobulins
lFAB=lREI by 47%; cytochrome c550/c2 155C=lC2C by 43%; chymo-
trypsin/trypsin 2GHA=lPTN by 42%; elastase/trypsin lEST=lPTN by
38%; acid protease/penicillopepsin lAPR=lAPP by 43%;a l p subunit of
hemoglobin 2MHB(a)=2MHB(P) by 44%. The final 62 data sets thus
cover essentially all known different protein structures, except those not
deposited with the protein data bank (Table AI).
H-Bonded Structure
Backbone-backbone H bonds can be simply classified by the number
+
of residues they bracket or, in our notation, by n of (i,i n ) = (CO(i),NH(i
+ n ) ) . Let us discuss the structural role of H bonds for each n.
H bonds n = 0 and n = 1are sterically disallowed. A hydrogen bond (i,i
+ 2) can be formed between two consecutive peptide units for certain 4,$
+
values of residue i 1. This local conformation is known as C7 and leads
to an extended strand roughly similar to a P-strand if it repeats. When
it occurs as part of a tight turn, that turn is sometimes called a y-turn.
30K
30
ia 5 10
Length of &leltx
15 20 25 10 5 10 15
Ladders per sheet
30 lb)
5 10 15 20 25
Length of p-Ladder lparollell
Hydrogen Bond Type
:L Length of R-Ladder tontiporallel I
Fig. 6. The common feature of the size distribution of secondary structure segments is the
gradual fall-off: larger sizes are less probable than smaller ones. Note that we give (b,c) the
length of 8-ladders (strand pairs) rather than the length of 6-strands. A strand is often longer
than the ladders in which it participates, since sheets tend to be trapezoidal rather than rec-
tangular in shape. The number of bulge-linked ladders per sheet (d) is given as an indication
of the width of the sheet. The width of a ladder is about 5 p\. In an ideal sheet, center strands
take part in two ladders, edge strands in one: the number of ladders is equal to the number
of strands minus one. In general, however, one strand can participate in more than one ladder
on each side and the width of the sheet less than the number of ladders times 5 A. Note:
sheets consisting of a single bridge are not included in the histogram of ladders per sheet. (e)
+
Number of H-bonds of type (CO(i),NH(i n ) ) . Due to the nature of L-amino acids, positive
n are heavily favored. The dominant peak a t n = 4 represents a-helices and 4-turns. We
+ +
find that H bonds (i,i 2) and (i,i 3) are surprisingly common, though generally weak.
Using our H bond definition, we find that many P-strands have, in addition
+
to the main interstrand H bonds, minor (i,i 2) intrastrand H bonds [see
peak in Fig. 6(e)]. These reflect part of the electrostatic stabilization of
extended conformations due to the polar interaction of the C - 0 and N-H
groups of adjacent peptide units, first shown by Florys group20to be es-
sential in stabilizing the C7 conformation in solution. We speculate that
P-strands originate as extended C7 strands as the protein folds up. Outside
of @strands, we typically find one or two weak ( E < -1.0 kcal/mol) (i,i +
2) H bonds per 100 residues, but most of them are neither repeating nor
part of a tight turn.
H bonds with n = +3,+4,+5 are reported as turns or helices. Most (i,i

+ n ) hydrogen bonds for n > 5 or n < -5 are part of a bridge or ladder.
Interestingly, H bonds (i,i - a), (i,i - 3) . . . (i,i 5) are also rare. There
-
is steric hindrance, e g , in an (i,i - 4) helix between the backbone oxygen

and the first side-chain atom CB.
3-Helices are more frequent than previously believed, although they are
usually short and have mediocre hydrogen bonds. a-Helices are rarely
+
entirely pure: numerous H bonds in them are bifurcated, i.e., (i,i 4) and
+
(i,i 3) or sometimes (i,i + 5). The ends of a-helices often are overwound,
ending in a 3-turn or 3-helix, or underwound, ending in a 5-turn. Some
of these cases were already noted and generalized by Schellman21 and
Richardson.8 We even find a few 5-helices (r-helices)-see Fig. 3.
Tabulation of the relative number of H bonds in Table A1 may be useful
in calibrating spectroscopic determination (CD, laser Raman) of the per-
centage of secondary structure (e.g., by the algorithm of Provencher and
Gloeckner22). In particular, we suggest that the distinction between par-
allel and antiparallel & ~ t r u c t u r e in
~ ~the
* ~reference
~ spectra will improve
the overall accuracy of these experiments.
Accuracy of H-Bond and Secondary Structure Assignments

At best, secondary structure assignments can only be as accurate as the
coordinates on which they are based. In using this dictionary, it is therefore
very important to be aware of the state of resolution and refinement of each
structure indicated in Table AI. The coordinate data sets range from re-
fined structures at better than 1.5-A resolution, where individual side chains
can clearly be seen, to unrefined structures a t a resolution just sufficient
to trace the protein chain. As a test, we compare our assignments with
those of the crystallographers and of Levitt and Greerl' for three proteins
of 1.5,2.5, and 3.0 A resolution (Table I).
For the higher-resolution structure of trypsin inhibitor (3PTI),
Deisenhofer and Steigemann25assign an H bond when the N - 0 distance
d is no greater than 3.1 A and list 18 backbone-backbone H bonds. Of
these, we find all except Tyr35(CO)-AlalG(NH),which has d = 3.1; instead,
we have Gly36(CO)-Ala16(NH),which has E = -2.2. In addition, we as-
sign 11others, due to the rather generous energy cutoff in our definition.
One, Tyr35(CO)-Ile18(NH) is quite strong, with E = -2.0, consistent with
the slow hydrogen-exchange rate of 2.6 X lop5min-' measured by nmr.26
+
Three others of type (i,i 3), with E = -1.3, -1.7, -0.9, form the well-
+
knowns 3-helix Asp3-Leu6. One (i,i 5) H bond, Asn24(CO)-Leu29(NH),
+
is part of the &hairpin. Six are of type (i,i 2), characteristic of the C7
configuration: five weak ones and one stronger one ( E = -1.8) in a y-turn
at Asn43. The additional H bonds assigned by us lead to identification
of two unambiguous segments of secondary structure not cited by the au-
thors but also assigned by Levitt and Greer.ll
For the medium-resolution structure of cytochrome c550, Timkovich
and DickersonZ7use a conservative interpretation of hydrogen bonds and
TABLE I
Comparison of Secondary Structure Assignments for Three Proteins of Higher, Medium,
and Lower Resolution
Original Levitt
Authors & Greer This Work
Structurea (AU) (LG) (KS)
3PTI
G1 -h 2-7 ?-6 Clearly 310; LG have N
El 16-25 14-25 18-24
E2 28-36 28-37 29-35
E3 -b 43-46 45-45 @-Bridge,2 H bonds
H1 47-56 47-55 48-55
155C
H1 6-11 4-16'' 6-12 4-Turn 13-16
G1 11-13 - 11-13 Overlaps with H1
El - 17-23h 19-20 AU have 2 H bonds; KS, 4
E2 - 26-3 1 - Discontinuity a t Asp28-He29
E3 - 33-39 35-37 AU have 2 H bonds; KS have 4
H1 - 40-44h - KS have 3-Turn
H2 56-63 55-65 56-64
H3 73-79 7 1-80 73-80
H4 - 81-9Ob - Pro a t 82,84; possible helix
H5 107-118 106-118 107-117
2ADK
H1 1-8 1-7 2-7
El 10-14 8-15 10-14
H2 23-30 21-31 23-31
E2 35-38 34-38 35-38
H3 41-48 39-49 39-48
H4 53-62 52-61 52-62
H5 69-84 68-83 69-83
E3 90-94 88-95 90-93
H6 100- 107 100-109 101-108
E4 114-1 I8 113-120 114-118
Hi I 23- 133 12 1- 136" 122-132 <?-Helixends in 3-turn
H8 144-158 141-1<57'] 143-157 N o (i,i + 4) H bond a t Asp 141
H9 160-164 159-166 160-167h Two weak H bonds a t 167,168
E.5 169-1 73 169-175 170-1 7 3
HI0 179-194 179-192 179-193
a H = n-helix, G = 31,)-helix,E = @-strand. 3PTI = pancreatic trypsin inhibitor, 1.5-A
resolution, Diamond real-space refinement (Re!. 25). 155C = cytochrome c550,2.5-A reso-
lution, Diamond model building to guide coordinates, assignments derived from the H-bonding
diagram of Ref'. 27. 2ADK = adenylate kinase, :LO-.& resolution, unrefined (Ref. 28).
Serious discrepancy (segment missing or boundary different by three or more resi-
dues).
give a minimal set of 41 backbone-backbone H bonds. We assign all of

these, except Alall5(CO)-Glnll9(NH),a t the end of an a-helix; instead,
+
we see the helix end with the (i,i 3) H bond Alall5(CO)-Aspll8(NH>.
We assign an additional 24 H bonds, of which 7 are the secondary partners
of a bifurcated H bond, which is common in helices, and 8 others are mar-
ginal, with E > -1.0 kcal/mol. Of the remaining 9, four are of type (i,i +
2) in approximate y-turns a t Glu2, Gly40, Lys 53, and Lys88; two are (i,i
+ 4) H bonds at the end of a-helices; two are (i,i - 3) and (i,i - 6) in the
loop region Gln22-Asp28; and one is involved in forming the heme pocket
by a tertiary contact between Thr80(CO) at a helix end and MetlOS(NH)
in an extended strand. All of these have a meaningful structural inter-
pretation. The resulting secondary structure assignments are consistent
with the authors H-bond list, except for the additional short parallel bulged
&strand pair, 19-20135-37, which is due to two additional weak H bonds.
Levitt and Greer assign considerably more secondary structure (Table
I), including a much longer parallel 0-sheet 17-23/33-39 (probably too
long), a 0-strand 26-31 (roughly antiparallel to 17-23), a helix 40-44 (we
assign a 3-turn), and a longer helix 81-90 (which has only two of the seven
possible H bonds but looks very much like a helix in a C* chain tracing and
therefore may be seen to be a helix a t higher resolution).
For the unrefined, lower-resolution structure of adenylate kinase
( 2ADK28),all secondary structure assignments (ours, the original authors,28
and Levitt and Greersl) are similar. Other lower-resolution coordinate
data sets show more discrepancies, depending on the quality of the H
bonds.
This detailed comparison shows that our H-bond energy cutoff, chosen
out of necessity to allow for coordinate errors in lower-resolution data,
typically leads to 50% more H bonds than conservative assignments in
higher-resolution data (example, 3PTI). All these have a physical meaning
in terms of electrostatic interaction energy and nearly all have an inter-
pretation in terms of canonical secondary structure; and, most importantly,
the increased number of H bonds does not give rise to spurious secondary
structure assignments.
H-bond assignments become less certain for some lower-resolution data.
For example, in the data sets lAPR, 3PGM, and lABP, Richardson8 sees
a number of 0-strands, which, in Table AIII, do appear as uncurved (non-
S) strands but with relatively few H-bonded bridges between them. A t
least for lAPR, only partially refined at 2.5-A resolution with tentative
amino acid sequence, one may expect that more H bonds will form in the
,f3-sheetson further refinement.
We conclude that our criteria for H-bonded secondary structure are
relatively strict, in spite of a generous cutoff in the H-bonding energy. For
higher-resolution data sets, our assignments are more accurate than those
of Levitt and Greer,l and for lower-resolution data, they are conservative
compared with both Levitt and Greers program and Richardons8 visual
processing.
Secondary Structure Size

What is the extent of secondary structure cooperativity? Are there any
preferred lengths of secondary structure segments? The length distribu-
tions [Fig. 6(a-c)] fall off almost monotonically with increasing length up
to a maximum segment length of about 30 A, with parallel &ladders slightly

shorter. There appear to be no statistically significant peaks, either for
an integral number of helical repeats or for typical domain sizes, with the
possible exception of four-residue parallel @-ladderscharacteristic of the
al@lafolding unit and, perhaps, 13- and 18-residue a-helices. We spec-
ulate that protein folding, although cooperative, follows random polymer
statistics approximately in that long segments are statistically less likely
than short ones. The apparent maximum size of 30 A perhaps reflects the
maximum size of globular domains.
OUTLOOK
The structure of influenza virus h e m a g g l ~ t i n i nwith
, ~ ~ its 50-residue
helix, shows that our data base certainly does not exhaust all possible
variations in protein architecture. In spite of this limitation, this compi-
lation will be used in the ongoing development of protein structure pre-
diction methods.
APPENDIX DICTIONARY OF PROTEIN SECONDARY

STRUCTURE
Notes to Table A1
Proteins are ordered by function and can be found in the strip tables (Table AIII) and strip
maps (Fig. AI) by their running number. Yo a-helix, YOP-antiparallel, YO&parallel = number
of H bonds per 100 residues of type 4-turn, parallel and antiparallel bridge; these percentages
can be compared with results from spectroscopy (CD, Raman, ir). Exposure = estimated
number of water molecules in contact with protein surface (first hydration shell); it can also
be read as the static exposed surface area in units of 10 A?. Exposure is calculated for the
entire data set and then divided by the multiplicity of sequence-unique molecules, e.g., the
data set lINS has two copies each of the insulin A- and B-chain (multiplicity 2). Exposure
given is that of the A- and B-chain in the tetramer. Number of residues is also for the se-
quence-unique molecule. Crystallographic resolution (A) and refinement give some indication
of the quality of the coordinates; both are taken from the Data Bank without further checking.
In case of doubt, consult the original papers. Refinement code: D1 = Diamond model
building to guide coordinates (Ref. 30); D2 = Diamond real-space refinement (Ref. 31); HK
= Hendrickson-Konnert (Ref. 32); DO = Dodson, Isaacs, and Rollett (Ref. 33); J L = Jack
and Levitt (Ref. 34); DS = Deisenhofer and Steigemann (Ref. 25); DF = difference Fourier;
DC = difference Fourier with constraints; FD = difference Fourier and D1; LS = least squares;
R L = restrained least squares; CL = constrained least squares; S D = steepest descent; LL
= energy minimization of Levitt and Lifson (Ref. 35); H H = D2 and Hermans REFINE2 and
HK; DD = DS and D2; DL = D F and LS; DJ = D2 and JL; AD = Agarwal least squares (Ref.
36) and DO; DH = D2 and HK; DE = D2 and LL; MD = energy minimization of McQueen
and D O CS = constrained difference Fourier of Chambers and Stroud (Ref. 37); RE = real
space and energy minimization; CC = constrained crystallographic refinement; CD = D2 and
CORELS (Ref. 38).
TABLE A1
List of 62 Different Globular Proteins
........... I A L P H A H E L I C A L AND 4-TURN HYDROGEN BONDS
I B E T A ANTIPARALLEL HYDROGEN BONDS
. . % BETA PARALLEL HYDROGEN BONDS
.. .. . . . . ... . . . . . . . . . . . . . .
WATER E X P O S U R E
.. . X U L T I P L I C I T Y OF D A T A S E T
. .. .................
.. . . . ... . . .... . . ..
N U 3 B E R O F RESIDUES
. . RESOLUTION
.. .. .. . .. . . .. . .. . .. REFINEHENT
ZAH XBA %BP EXPO M LEN RES RF . PROTEIN I D E N T I F I E R , N A X E
hlnding proceins
38 4 0 610 I08 1.9 D F I ) lCPV CALCIUM-BINDING P4RV4LBUXIN B
31 1 6 1423 306 2.4 - - 2) 1ABP L-ARABIUOSE-BINDING P R O T E I X
eleccio" transfer
7 I3 2 690 85 2.0 DF ?) I'iIP O X I D I Z E D H I G H P O T E N T I A L I R O N PROTEIN (HIPIPI.
election Lrd"SP0rt
19 15 7 566 85 CY T V C H R O N E
57 0 0 665 103 CYTOCHROXE
34 2 0 620 2 I03 CYTOCHROlE
23 2 2 642 112 CYTOCHROXE
23 0 3 781 I34 CYTOCHRUXE
38 2 0 482 a2 CYTOCHROXE
9 9 0 316 54 FERREDOXIN (PEPTOCOCCUS AEROGENES)
0 0 0 623 98 FERREDOXIN (SPIRULINA PLATENSIS)
30 I 18 715 I38 F L A V O D O X I N IOKIDILED)
I7 0 376 54 RUBREDOXIN
I7 7 645 125 A211
~. R IN
~
21 10 513 99 PLASTOCYANI
hormones
44 0 3430 36 1.4 RL 16) IPPT AVIAN P A N C R E A T I C P O L Y P E P T I D E
38 0 3540 29 3.0 R E 17) ICCN G L U C A G O N ( P H 6-7)
29 0 12
301 2 51 1.5 D L 18) L l N S INSULIN (A AND B CHAIN)
hydrolase, phospharlde acyl
37 7 0 712 123 1.7 AD 19) IBPZ P H O S P H O L I P A S E A2
hydrolases, 0-glycolsyl
38 7 0 918 164 2.6 C L 2d) I L Z M L Y S O Z Y X E (BACTERIOPHAGE T4)
24 8 2 665 129 2.5 CD 21) 7 L Y Z L Y S O Z Y M E (HEN EGG W H I C E , TRICLINIC)
hydrolaser, phosphoric d i e i t e r
I9 20 3 842 142 (6 - - 22) IS35 STAPHYLOCOCCAL NUCLEASE (COMPLEX)
I4 28 2 709 124 2.0 S D 23) I R X S RIBONUCLE4SE-S
hydrolJses, protelnases
23 5 9 1209 303 2.0 -- 24) LCPA C A R B O X Y P E P T I D A S E A
3 I3 3 1333 324 2.5 HK 2 5 ) LAPR ACID P R O T E A S E (RHIZOPUS CHINENSIS)
7 32 6 1272 323 2.8 D2 2 6 ) I A P P ACID P R O T E I N A S E (PENICILLOPEPSIN. FUNGUS)
27 9 6 1266 316 2.3 D2 27) 2 T L N T I I E R X O L Y S I N
6 31 I 1093 236 1.9 HH 28) 2GCH G A M X A CHYXOTRYPSIN A
3 37 3 821 198 2.8 DL 29) M L P ALPHA L Y T I C P R J T E A S E
7 31 I 929 223 1.5 02 30) lPTN BETA-TRYPSIN ( N A T I V E AT P H 8 )
6 34 2 145 131 2.8 DI 311 I S G A P R O T E I N A S E A FROM S T R E P T O M Y C E S G K I S E U S (SGPAI
23 5 I2 I 0 5 8 275 2.5 FU 3 2 ) iiaT SUHTILISIH BPN'
4 35 0 LO89 240 2.5 -- 3 3 ) i E s r TOSYLkELAST4SE
21 19 1 923 218 1.7 LS 34) 2 A C T ACTINIDIN
19 I5 I 968 212 2.8 D1 35) 8 Y A P Y A P A I N
immunoglobulins
I 34 2 2101 428 2.0 - - 3 6 ) IFAR L A X B D A IXMUHOGLOBULIN F A B
1 37 5 492 2 107 2.0 C C ?7) I R E 1 BENCE-JONES IXMUNOGLORVLIN (VARIABLE P O R T I O N )
IEOlerdSeS
23 2 5 12211 2 3 1) 2 . 8 HK 3 8 ) 3PGY PdOSPl{OCLYCERATE H U T A S E ( D E - P I l O S P ! l O )
35 I 15 1326 2 246 2.5 DO 39) I T I M T R l O i E P H O S P H A T E I S U X E K A S E
Iecrio (agglutinin)
2 15 n 1125 237 2.4 Y D 40) 3CNA CONC.\UAVALIX A
Lyasc, carbon-oxygen
4 23 5 1271 256
oxidoreduc~a~es
15 I2 13 937 162 2.5 IDFR
22 I1 10 1505 333 2.9 DI IGPU
I7 I1 9 I639 374 2.4 DJ 4ADli
27 6 7 1753 329 2.0 DZ 6LDH
22 I2 7 2356 661 2.0 _- 2GRS
I
33 I 686 IS1 2.0 HK 2S0D
oxygen r r o r r g e
65 0 0 842 I53 2.0 0 2 48) INBV MYOCLOBIN (FERRIC IRON - METXYOCLOBIN)
136 1.4 DS 491 IECD HEXOGLOBIN (ERYTHROCRUORIN DEOXY)

297 2.0 DD so I 2:IHB HEMOGLOBIN ( H O R S E , AQUO M E T )
I68 2.0 DL 5 1 ) lLHB HEXOGLOBIV(HEP)-CYANIDE V (SEA LAYPREY)
I53 2.0 D 2 52) IHBL L E G H E M O G L O B I N (ACETATE,MET) (YELLOW LUPII)
46 1.5 HK 5 3 1 ICRN CR.438111

proteina5c inhibitors
I3 I4 2 351 6 56 1.9 DJ 5 4 ) IOVl O V O M U C O I D T H I R D DOXAIN
13 23 2 632 107 2.6 D O 5 5 ) 2SSI STREPTOXYCES SUBTILISIN INHIBITOR
12 17 0 412 58 1.9 02 56) 3 P T I T R Y P S I N INRIBITOR
L 0 X l " S
3 I7 0 511 71 2.8 _ _ 57) I C T X A L P H A C O B R A T O X I N
71 0 0 222 2 26 2.0 H K 58) IXLT MELITTIN
0 29 0 406 62 1 . 4 HK 591 iNXB NEUROTOXIW B (PROBABLY IDENTICAL TO ERABUTOXIN B
trB"SferaSe5
47 0 I0 1251 194 3.0 ._6 9 1 2ADK ADENYLATE KINASE
20 2 10 1456 293 2.5 DI 6 1 ) IRHD RHODANESE
LransPOCr
7 33 7 652 114 1.8 DO 6 2 1 > P A 8 P R E A L B U X I N (HUMAW PLASMA)
TABLE A11
Structure Notation Used in Table AIII
First line: running number 1-62, data set identifier (3PTI,4LDH . . .), protein name,
[function], {sourcel
SHEET.. . One-character name of P-sheet (A, B, C . . .) in which residue i
participates.
H H I D G E ~. . . One-character name of P-ladders in which residue i participates,
HRIDGE1 . . . A, B, C . . . = antiparallel,
a, b, c . . . = parallel.
Ladders are named sequentially from N- to C-terminus.
A 8-strand can be part of two ladders, one to each side, so there are
two lines for the possible ladder partners. Each ladder name appears
twice, once for each participating strand. Partner strands can thus be
easily identified by identical letters. The sheet topology can he
reconstructed by starting from a P-strand and tracing all partners and
their partners.
CHIRALITY + or -
Chirality a t residue i is the sign of the dihedral angle defined by CC1
+
i - 1 to i 2. Thus, a right-handed a-helix has +, an ideal twisted
P-strand -.
.
HEN11 . . S = five-residue bend centered a t residue i.
5-TURN.. , Hydrogen-bonding pattern for turns and helices:
4-IURN ) = backbone CO ofthisresidue makes H bond (i,i + n )
:j-rURN ( = backbone NH of this residue makes H bond ( i - n,i)
X = both CO and N H make H bond
3, 4, 5 = residues bracketed by H bond
SUMMARY. .. Structure summary:
H = +helix (a-helix)
B = residue in isolated P-bridge
E - extended strand. participates in 8-ladder
G = %helix (3lo-heIix)
I = 5-helix (?r-helix)
T = H-bonded turn
S = bend
In case of structural overlaps. priority is given to the structure first in
this list.
EXPOSURE. .. Solvent exposure is the estimated number of water molecules in
contact with residue i. The scale is 0-9; I * = more than 9 water
molecules, Exposure can he read as solvated surface area in units of
10 A?.
SEQUENCE Amino acid sequence in one letter code:
- b,??i C c I f , . . are Cys residues labeled by their SS-bond name. !

chain break (peptide bond length exceeds 2,s A), Residues
including chain breaks are numbered sequentially within the
coordinate data set, irrespective of the residue identifier given there.
Thus, the tot,al number of residues is equal to the total number of
print positions minu8 ..
the number of.chain hreak8,
.. . . . .~ . .
TABLE A111
Strip Tables of Secondary Structure Assignment for 62 Different Proteins in the Notation of Table A11
1) lCPV CALCIUM-BINDING PARVALBUHIN B [CALCIUM B I N D I N G PROTEINS] (CARP: CYPRINLE CARPIO) ............................... 1CPV
SHEET.. .. A M M A
BRIDGE2..
BRIDGE1.. A M M A
CHIRALITY +-----+++ +++++++++- +++--+++++ ++-++++--+ ++++++++++ -+-+-+---+ ++++++++++ -++-----++ ++++++++++ +-+-+-+-++
BEND..... SS S SSS ssssssss s ss sssss ssss sss s ssssssssss ss ss s ssssssssss sss ss sssssssss ss ss ss
5-TURN.. > 5555<
4-TURN.. >>>> xxxx<<<< > > > > x < <<< >> >>xxxxx<<<< >>
>4<<< >444 < >>> >xxxx<<<< >>>
3-TURN.. >33< >>><<< > 3 3 < > 3 3< > > 3 < < 3xx3<<>33<> 3 3 <
>> >3 3< >33x 33< >3
...
SUUMARY.. TT S HHH HHHHHHHT S SS HHHHH HHTT TTS H HHHHHHHHHH SS SEEEH HHHHTSSTTT STT HH HHHHHHHHT TT SSEEEHH
EXPOS ORE. 4 4 5 9 3 8 47 4 26403*81*6 745392.518 580225*854 g 6 0 4 4 2 2 4 7 1 1*9*63804* * 2 1 9 6 0 8 7 5 3 49.1748443 12*901*701 *96838808*
1 SEQUENCE. LSAGVLNDAD I A A A L E A C M ADSPNHMPP AKVCLTSKSA DDVKKAFAII DQDKSGPIEE DELKLPLWP KAMRALTDG ETKTPLMGO SDGDGKIGW
SHEET.. ..
BRIDGEZ..
BRIDGEI..
CHIRALITY ++++++
BEND.. SSSSSS
5-TURN.. >5555<
....
4-TURN... >XXX<<<<
3-TURN.. . 3<>33<
SUIMARY.. HHHHHHH
EXPOSURE. 3136288.
101 SEQUENCE. EFTALVKA
2) lABP L-ARABINOSE-BINDING PROTEIN (BACTERIAL: ESCHERICHIA COLI).....................................................lABP

SHEET.. , . AAA A M B B
BRIDGEZ..
BRIDGE1.. aaa aaa b b
CHIRALITY +-+---+-- --+-++++++ ++++++++++ -+----+--+ +-++++++++ +++++-+--- --+--+-+++ ++++++++++ -t-+---+-
-+--+-+---
BEND.. ssssssss ssssssssss sss sssssssss ssssss s ss ssssssssss s ss sss
5-TURN..
....
4-TURN.. > 4 > > < > x x>xxxxx<<< < >>>>xx<xx x><<<< > 4 > > x > x x x < < <<
3-TURN.. > 3 3 < > 3 3< > 3 3 < >33x3 3<>>3<< >3 3< >33<
..
SUIMARY.. EEE SSTTHHHH HHHHHHHHHH S S S EEE SHHHHHHHH HHHHHT B S SS TTHHHHHHHH H B SS STT
EXPOSURE. "65100002 65*2401*10 5740S402** 631.16.540 492**11910 6 7 0 3 9 5 5 1 9 0 00000563*3 06402550*6 "29188018 48299'2.55
1 SEQUENCE. ENLKLGFLVK OPEEPWPOTE WKFADMGKU L Q E V I K I A V PDGEWLNAI CSLAASGAKC PVICTPDPKL GSAIVAMRG YDMKVIAWD WVNAKGKPM
SHEET.. C DDD D D D
BRIDGE?. ee
...
BRIDGE1.. C dd4 e e d
CHIRALITY ++---+---+ ++++++++++ +++++++-+- -+++----++ -+++-+++++ ++++++++++ +-+--+++-- ----+-+-++ ++++++++++ +++++++---
BEND..... SS s ssssssssss ssssssss sss sssssss ssssssssss sss sss ssssss ssssssssss ss s s
5-TURN.. >55>5<55< > 5 5 55< >5555<
4-TURN.. > >>>xxxxxxx xxxxx<<<< >4>>x >xxxxxxxx< <<< > > >>xxxxxxx< <<<
3-TURN.. >3><3< >33< >>3<< >>3<< > 33< >>3<<
...
SWMARY.. SS B S HHHHHHHHHH HHHHHHHHT S R EEE SSGGGHH HHHHHHHHHH HHS SSS E E SSSSSH HHHHHHHHHH HH S S E
EXPOSURE. * 9 2 1 1 0 1 0 0 0 7*108*017~3 08*21**963 8 6 * 4 0 1 0 1 # @ 119*3610*4 1 0 4 0 0 1 8 2 1 7 89216**33* *292*45695 1 0 8 * 1 0 6 6 1 2 **2**18400
1 0 1 SEQUENCE.. DTVPLVMMM TKIGERCGOE LYKEMQKRCW DVKESAWAI TANELDTARR RTTCSMDALK AAGPPEKQIY QVPTKSNDIP GAFDAANSML VQHPEVKHWL
nsua a d H i a x I u YSIZLIY~,LSH M ~ B W O L V ~D D V D ~ M M 3~3~d H a a i m ~ ~ M Y A H ' I I ~ M S Y S N N H X ~ IOB-JWAXAV ' ~ s ~ a n ~K a s
L..91 *L9091bLE+ .28r.E..9S L f r L E L r Z l S ZKZS.9ZL.8 E9rE.rIL.b KS109.8200 ZBE.BL~E+I 09rESbr.8* '3MflSOdXa
3333 DD a a a a a s ~XUHHHHH LLHHHHHH a IL.+LHHHHHS LL D ~ W U a a a a v n a ~3 3 a u 3 3 LL HHHH 38 --mvuYns
>>EXX E < < >>> x<<< >>E<< >E>XE<XEE< >EEX>C<XEE < >EE< > E E < > > E << '' ' N W J - E
>P bP< >>>><<<< >>>><<<< >>>b<<< >bP><PP < > >bP<< ' * 'NWL-P
sss ss ss ssssssss
> SSSS<
sssssss ss sssssss ss ssssss sss sss ss ssss
.
.....
* 'NlmL-S
aN3e
+++ ++-----+++ ++++++++-- --++++++++ -+++++++++ --+-++++++ ++---+---- ++--+-++++ ++++----- ALX1VMIH3
ww 5 3 eeee 888 ea3 a 3 We "KaMIME
aa a aaa 53 'zaxme
vw v Y Y W V Y VVY vee el3 vv . * * * La3HS
3s ez . . . . . . . . . . . . . . . . . . . . . . . . . . I . . . . . .
{snMnvJ soe :MMI+I ILMWSNYML N O M L J ~ ~ (I a a z r a r x o ) se 3 ~ 1 1 ~ 3 0 3~s e3z (P
3W1& S Y 3 M 3 N A N I 1 Y C d d l d 3 3 Y Ma(LLVDVVaV O W & X V 3 H O 3 3 d d l N M V Y VAM3SYLVaO N A M 1 V I V L Y N (IYVAYNVdVS '33NanOaS K
66.65 0bbZ006ZK0 BL8.19.20E 1 6 r 9 V 9 6 E r L 9C99KbPKSB ..ESE9r6SS 662*2+.098 915E8.09EE .61KZ9rESr 'aMnSOdX3
e LL e ~ 1 3 3 a .+LsLaaa 3ss usu B ~ U E D D ~ DDD sss H HHHSSDDDSS e LHHHHHH LL BJL *-AMVUUIIS
>EE< > t E < >EEXEE< > E t XE t < > E C X>E <<> > E < < >>E<< > E E < >EE< "'NWL-E
>> P b < < >>>><<<< * * 'NMRL-C
>5ss5< * * 'NWL-S
s ss sssss ss sss s ss sss sss sss s ss sssssss ssssss ss sss .***. aNae
+-- -++---++-- --++-++--- +++--++-++ --++-+++-+ +++---+--- ++++-+++-+ --+-*++++-
ALI1VMIH3 ++---++--
3 a w ee 88 3 a w * 'K3MIME
3 e
33 3
w v
33 3
vw v w 3 E V
"23MIME
u a ~ s ....
dIHK"" (YnSONIA U I I I L V W M H 3 ) (NIP&OMd Yfld'lllS-NOMI 'M3dSNVMJ NOML33131 (dIdIH)
N 1 3 U U d NOMI 1 V I L N 3 J O d H D I H a B Z I a I X 0 d I H 1 (E
Y331DY
.8EZSS
LL LL
>EE< ' * 'NWL-E
>P
>s5 ...NWJ-S
'* 'NWL-b
.....
ss ON3 e
+++- ALI1VMIHJ
* * K 3WIL1E
....
"Z8MIME
L33HS
~ 3 1 3 JNCY
3 ~ M A l L n S S Y A 3 H h C d S d l 7 S D A d 3 J V O W S 7 3 S A V M D N I 3 1 3 I I O Y W J 31)33LVW33 lALSUNY9AI '33N31103S K0Z
w6ZL.rZV.6 V89029K0SS 0 0 S Z 0 0 0 0 0 0 0L0025.6.8 0 1 6 b 0 2 2 0 1 0 00000SEE1Z t.LL0K8000 2 0 1 2 0 1 1 0 0 0 '3MnSOdXa
13333JLJSSS HHHWHHHHHH H L L U 33 S S S S S HHHHLLLSSO 3 U S SSSHHHHHHH H L U S S S 33 * 'AMVWiUlS
>>E<XEE< >>E<X>E< < > E E < >>E <XE E < >EE< > E E < > E EXE E < ' 'NMnL-t
>DXD<C< >xxxx<xx<> < X P < b < > >bbX<bb< >>>>xx<< X < t b < ' ' 'NMflL-b
55<
ssssssssss
S<
ssssssssss ssss s ssss ssssssssss sss ssssssssss sssssss .....
* ' 'NYnJ-S
aN3e
++++++*+ti ++++++++++ ++++++---- --++---+-+ ++++++++-+ ---+++++-- +--++t++++ +++++-+-+- ALI'lVMIH3
33 3 3 PP * 'K3XIIME
D
33
TABLE AIII (continued)
5) 1 5 6 8 CYTOCHRWE 8 5 6 2 ( O X I D I Z E D ) [ELECTRON TRANSPORT1 {ESCHERICIA C O L I ) . . . . . . . . . . . . . . . . . . . . . ........................ 156B
SHEET.. ..
BRIDGE2..
BRIDGE1..
CHIRALITY ttttttttt tt+tttttt- t-tttttttt ttt+tttttt t+---ttttt ttttttttt+ tttttttttt tttttt+-tt tttttttt+t ttt+tttttt
BEND..... SSSSSSSS SSSSSSSSS SSSSSSSSS S S S S S S S S S S S S S SSSSS S S S S S S SSSSSSSSSS S S S S S S S S S S S S S S S S S S S S S S S S S S S S S
5-TURN.. . >55>5<5 5< >5555<
4-TURN... >>>>XXXXX XX<<X<44< >4>>X>X XXXXXX<<<< >444< > > > > x xxxxxxxxxx xxxxx<<<< > > > > x x x x < xx x > < < x x 4 4 <
3-TURN.. . >>><<< >33x>3<< >33< >>> <<< > 3 3 < >33< >> 3<< >33< >33< > > 3 x x 3<< >33<
SUMMARY.. HHHHHHHH HMHHHTTTS STTTTHHHH HHHHHHHHHG GCS TTTTT SSTTHHHH H H H H H H H H H H HHHHHHHHT SHHHHHHHHH H H H H H H H H H H
EXPOSURE. *64'716'43 *'13*718*2 '698605608 8'19618'60 4*270'*2'* 77*'2'61*8 0 2 9 4 2 2 ' 0 6 6 603'31**59 4 * * 0 3 6 3 2 8 * 1782'564'.
1 SEQUENCE. ADLEDDMQTL NDNLKVIEKA BBZKANDAAL VKMRAAALNA QKATPPKLED NSQPMKDFRH GFDILVEGID DALKLANEGK VKEAQAAAEQ LKTTRNAYHQ
SHEET.. , .
BRIDGE2..
BRIDGE1..
CHIRALITY t
BEND..... S
5-TURN.. .
4-TURN... <
)-TURN.. .
SUMMARY.. S
EXPOSURE. 93.
1 0 1 SEQUENCE. KYR
6) 1CYT CYTCCHROME C ( O X I D I Z E D ) [ELECTRON TRANSWRTI (ALBACORE TUNA HEART: THUNNUS ALALUNGA] ... . . .... ..... ,... ........lCYT
SHEET.. .. A A
BRIDGE2..
BRIDGEl.. A A
CHIRALITY -ttt++ttt +ttt+t+--t -tt--t-t-- -tttt++--t tt-+t----t +ttt-t--+- ttttt++tttttt-++-t- t----t-ttt +tttt+ttt+
BEND..... SSSSSSSS SSSSSSS SSS SS SS SSS S S SS S SSSSS S SSSSSSSSS SSSSSSS sss ssssssssss
5-TURN.. . > 5555<
4-TURN... >>>>XXXXX (<<X444< >> >4<<< > > > > x x x < < < x> 4 4 < < >>>> x x x x x x x x x ~
3-TURN. .. >33< >33< >33x33<>3 3<>33< >> 3<< >33<
SUMMARY.. H H H H H H H H HHHTTTT STT SS TT TTSBT T TT H HHHHS 8 S H H H H H H H H H HHHHSTT HHH HHHHHHHHHH
EXPOSURE. 8'65'0**21 8'923'5321 * * 8 2 * 8 9 9 1 2 2 3 9 3 2 4 6 5 ' 8 0*0*84'43* 329.924927 8.21682298 0 * * 3 0 9 7 2 ' 5 * 5 * 1 1 * * * 4 5 3 9 2 0 1 1 3 1 7 9
1 SEQUENCE. GDVAKGKKTF VQKCAWHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD ANKSKGIWN NDTLMEYLEN PKKYIPGTKH IFAGIKKKGE RQDLVAYLKS
SHEET.. ..
BRIDGEI..
BRIDGE1..
CHIRALITY +
BEND..... S
5-TURN.. .
4-TURN.. , <<<
3-TURN.. .
SUMMARY.. HH
EXPOSURE. 20'
1 0 1 SEQUENCE. ATS
SUMMARY.. .., ...HIALPHA-HELIX.. . E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..GD3-HELIX.. ..1-5-HELIX.. ..T=3-, 4-, OR 5-TURN.. ..S-BEND.. ..
7) 1C2C FERRICYTOCHRQYE C2 [ELECTRON TRANSPORT] (BACTERIAL: RHOWSPIRILLUM RUBRUM). ................................... lC2C
SHEET.... A A B B
BRIDGE2..
BRIDCEI.. a a B B
CHIRALITY -++++++++ ,++++++--+ -++--+-t-- -++++-+--+ -+-++-t--+ +++++++--- -+-+++++++ ++-+*+++++ +--------+ ++----++++
BEND.. SSSSSSSS sssssss sss sss s s ss s s sss s sss ssss sssssss ssssssssss ss ss s ssss
5-TURN.. >5555< >5
....
4-TURN... >>>>XXX<< x<4><44< > 4 44< > > > > < x << 4 < > 4 4 4 < >>>>X
3-TURN... >> ><<x33< >33< >33< >33x33<>3 3<>33< > 33< >33<>3 3<
SUMMARY.. THHHHHHHH HTTTBTTB STT TTS TT TT BT T TTS T TTS SSSS B SHHHHHH TTSSSTTTTT TS SS S HHHH
EXPOSURE. '6'23286'1 2* * 2 9 6 6 2 1 2 **7364**12 1 2 4 2 1 3 ' 6 4 1 1 1 6 * * 6 8 4 2 * 1 3 6 4 3 * 6 * 5 2 5 2 5 9 8 2 1 3 5 3 2 * 9 0 8 4 1 1 6 * 6 2 5 8 8 * 2 * 1 * 568'2''921
1 SEQUENCE. ECDAAACEKV SKKCLACHTF DWGANKVCP NLFCWENTA AHKDNYAYSE SYTEMKAKCL WTEANIAAY VKNPKAFVLE KSCDPKAKSK MWKLTKDDE P
SHEET.. .. z
BRIDGE2..
BRIDCE1..
CHIRALITY +++++++-++
BEND..... SSSSSSSSSS
)-TURN.. . 55><555<
4-TURN.. XXXX<XX<4< <
3-TURN. ... >33<>33<
SUMMARY.. HHHHHHHHHH
EXPOSURE. 95184073'6 '3
101 SEQUENCE. IENVIAYLKT LK
8) 155C CYTCCHROME C 550 [ELECTRON TRANSPORT] (PARACOCCUS DENITRIFICANSI.. ............................................. 155C

SHEET.... AA A A
BRIDCE2..
BRIDCEl.. aa a a
CHIRALITY ++++++
--- ++++++++-- t--++----+ --++---+++ +++---++-+ t----+++++ ++++++++-- -++++++++- -++++++++- +-++---+++
BEND.. ssssss ssssssss sss ss sss ss sss ss ss ss sssss ssss s sssssssss ssssssssss s s
5-TURN.. >5555<
....
4-TURN.. >>>>X< <x<4><44< > > > > x x x<<<< > > > > x x < < << > 4 4 > < 4 4 <
3-TURN.. > >><<x33< >33<>33< > > 3 < <>33< > 3 3 <
..
SUMMARY.. SHHHHH HHTTTTTTEE S S S SS SSEEE S S TTS TT SS SS HHHHH HHHH S SHHHHHHHH SSTTTTTTTS S S
EXPOSURE. '*3726'0** 5 1' 9 4 7 8 6 2 3 0 7 2 * * 2 7 6 4 * 82'9122261 1 1 3 6 8 0 1 6 6 * 8 5 * 3 1 4 1 2 6 8 0 1 * * 6 9 9 1 1 2 5 7 6 2 1 5 8 4 3 4 6 0 9 5 1 1 3 8 7 3 '9'51'3'4'
1 SEQUENCE. NECDAAKCEK EPNKCKACHM IQAPOCTDIK CGKTCPNLYC WCRKIASEE CFKYCEGILE VAEKNPDLW TEANLIEYW DPKPLVKKMT DDKCAKTKMT
SHEET.. ..
BRIDGE2..
BRIDGE1..
CHIRALITY --++++++++ +++++++-++ -------+-+ ++
BEND.. s ssss ssssssss s ss s ss s
5-TURN..
....
4-TURN.. . >>>>X xxxx<<<<
3-TURN.. . >33x33< > 3 3<
SUMMARY.. S HHHH HHHHHHHS ST T S SS S
EXPOSURE. 9.27'44222 02112*31*' 6795678478 4146
101 SEQUENCE. FKHCKNQADV VAFLAQDDPD AXXXXXXXXX XXXX
.... CIN3E=S""NWL-S YO ' - P ' - E ~ L ~ ~ ~ ~ X I 1 3 H ~ ~ ~ I ~ ~ ~ ~ ~ X I l 3 H - E ~ 3 " 3 3 a I ~ ~ ~ " L 3 E ~ ~ ' ' ' ~ ~ N Y l L L S - V J 3 E - 3 ' ~ ' ' X I ~ ~ ~ -wwwns
YHdlV~H~~~~''''
a d a u w w 3 a D M D A S D ~ V A XX ~ S I X L S I1dadas33'1
~ ~ ~ h a a ~ w s 3 3 - 1n I a 3 N i i a a I t u a s A N I m I\arDsaIrDr V I ' I ~ V W ~ N OJDSMMIXW *a3~3nb~ I s
LBLrIBrBrZ rZS0000006 V S 6 0 r 6 E B r r 0199086rZI SPr9LZ1000 0 0 0 r E ~ 9 1 r r EBVr9TEPPr Trd9r600r 101L00rLBD ZeSZEZ00LV '3YflSOdX3
HHHHHHHS s ~ ~ 3 3 3 3 3 3 3 3LL LLLHHH HHHHHLLL s 9~~33
~ J L E 333 3 3 3 s LLLU 3 3 LLHHHHH HHHHHHHHHH sss 33333 **Iuvwwns
>EEXE ><E < >EE< >EE< >>E<< >EE< * ' 'NYflL-f
xxxx<<<< >>>> x x < < < < >PtV< >PPP < >>>>xx XXXXXXX<<< < * * 'NYflJ-P
ssssssss s ss s ss sss ssssssss sss
>5sss<
s sssss s sss
>SSSS<
sssssss ssssssssss sss .....
* * 'NWL-5
aN3E
++++++++-- ++-+-++--- -+++++++++ ++++++++-- -+--++--+- ---+-+++++ +--+++---- -+-+-+++++ ++++++++++ +-+-+-+-- ALIlVYIH3
33333 d d qqq qq meee epee "I33aIYE
aaaa pp qWqq "233aIYE
33
. . . " . . . . . . . . . . . . . . . . . . . . . . . . . . . E. . . . .E. . .QVV
N ~ d E " . . . . .VVVVVWY
333
, . . .VQV
(dW WflIaIlLLSO'I3)
VVVV
[LYOdSNVYL N O Y L 3 3 1 3 1
WWV -*.-
L3PHS
( a 3 Z I a I X O ) N I X O a O A Y l d NXdE (7.7
x i 3 3 a b ~x I~L 3 a s w . v A ~ J M A D V ~ Ibaaaidsoas b a I m s u m v a s 3 ~ 3 w 3s ; i d i a i D w a V v a ' I I A L a a o X I L ~ N I ~ a~ aVi immv m ~ n n b a s1:
L S E E r r 6 E rrrS9L9260 Z Z E B T E Z B r r 6r0tr9SV69 Z r V r V L 5 5 1 0 TBYZESI9.L 6 1 V 8 S r P L r r 9EISrrSrSr rPV2669TS2 L99rrr6rI1: '3MnSOdX3
sss ss LL LLS s s sss s ss LJSSSSS L L S SS S S S ' L LS U S L 5 S "AYVWWIS
>EE< > EE< >E E < >fE< >E E < > E E < >E E < "'NWL-E
* * 'NWL-P
' ' 'NMflL-5
sss ss ss sss s s sss s ss sssssss s s s ss ss s s ss sss s s s .'.** a N 3 E
---+-+ ++--+++--- +++--++++- +++++++--+ ---+-++--+ ++++-++-+- +++-++-+-+ +--+-+-+++ +-++-+-+-+ +++++--+- AJI'IYHIH3
....
* '1 3 1 M I Y E
"133aIYE
3XdI ......................................................... (SIS N I J V l d Y N I l f l Y I d S 1 [ L Y O d SNQYZ N O Y J 3 3 ' 1 3 1 NIXO(13YLIBd
L33HS
JXdI (17
a 3 d N d Q W d X S V 3 S3XI3SaW I V A I S S O I I N A d 3 3 d X 3 V 3 5 V I J S a N I A A Q '33NBflbPS T
r r 9 8 IBP96EYrPT ZZ96629rPL ZSS6eSrBTe L6Ze69IPZL SrE9rSZ9EL '3YflSOdX3
S3 3 S S HHHH H ALL 0 SSS E LL 33 LL 333LL "AYVWWIIS
>E E < >>EE< >EE< tEX>EX<E< * ' 'NYflL-E
>>>P< << >PIP< >PVP< * "WL-P
x s
+- +++-+-++++
ss ssss
t+-+--+++-
sss sss
----+-++++
ss ssss
-+-++++++- +--++----
S
.....
* ' 'NWL-S
aNae
ALIlVMIH3
Q Q 0 a vv **I~~CIIIE
"Z33aIYE
xadI...."........".,.............. .......................V V a
(S3N33013V S n 3 3 J 3 0 J d 3 d )
E VV * ' . .L33HS
[ L Y O d S N V Y L N O Y L 3 3 1 3 1 NIXOC13MM3d XalT (01
X b S l A M X Y l J d Y 3 C K l S A V N d d Y d I d 3 M S O S 3 N X I Y O Y 1 3 V 3 V3Vb3V91YV A C U A V d 3 A W U I I Q H 3 V A 3 3 X N X d ' I A 3 d 0 3 '33N3nO3S I
-9 8 E I Z 8 0 0 Z 9 0 2 ~ 6 1 1 6 P - 6 5 ; 8erC699rEZ 6928r02r56 IPrr8lrZrPB IBrZ02188r BrSZZS89ZE LrrZ08rILr '3WSOdX3
LHHHHHHHHH HHH s E ssssss EHHHHHHHHHH HLJ LLHHHH HHHH sss sss LDWJ JHHHHHHH **Aiivwwns
> >E<< >EEXEE< >>E<X CE< >EE< "'NYflL-E
>>>>xxxxxx <<<< > >>>xxxxx<<< < >>>>x x<<<< >PPP< >>>>X<<<< "'NMflL-0
>s s s s < * ' *NYflL-S
ssssssssss sss s ssssss ssssssssss ss s ssss ssss sss sss sss s ssssssss *.*.* a N 3E
++++++++++ +++--+---- --+--++++- -+++++++++ +++-+-++++ ++++---+-+ -++--+++++ -+++++++- ALIlVUIH3
V Q "133cIIME
Q V
3 1 5 ~ . . " . . . , . . " . . . . . . . . . . . . . . . . . . . . . . . . . .( V S O N 1 3 n Y 3 V
....
"za3aIYa
L33HS
SVNOWOan3Sd) [LYOdSNYML N O Y L 3 3 1 3 1 (03ZIaIXO) I S 5 3 3WoYH3JLA3 3TSZ (6
8
co
c.l
SHEET.. .. AA AAM
BRIDGE2..
BRIDGE1.. dd eeee
Y
CHIRALITY +++++-+--- +---+-'--+- ++++++++++ ++++++
BEND..... SSSSSSS S SSS SSSSSSSSS SSSSSS
5-TURN.. >5555<
4-TURN.. XX<<<< > > > > x x x xxx<<<<
..
3-TURN.. . >>3<< >>3<< >>3<<
SUMMARY.. HHHHHTT EE S E E E E S S GGGHHHHHH HHHHHHT
EXPOSURE. * 6 0 8 7 6 3 1 7 3 43*2261*87 09*29*'018 186.01.9
101 SEQUENCE. ERMNGYGCW VETPLIVQNE PDEAEQDCIE F G K K I A N I
13) 2RXN R U B R E D O X I N ( O X I D I Z E D , F E ( I I 1 ) ) [ E L E C T R O N T R A N S P O R T ] ( C L O S T R I D I U M P A T E U R I A N u n ) . . ................ ...... .2RXN

SHEET.. .. AAA AA B B AA A
BRIDGE2.. BBB
BRIDGE1.. AA AA C c BB B
CHIRALITY -----+t-+ ----+t--++ +-+--++--+ tt--++---t +-+--+++-- --
BEND.. sss sss sss 5 s s sss ss s 5 s sss
5-TURN..
....
4-TURN.. , >444< >444< > 4 44< >4 44<
3-TURN.. . >33< > 3 3 t >> 3 < < > 3 3 < > > 3 < < > 3 3 < >>3<<
SUMMARY.. EEETTT E E T T T G GGS TT G GGS T T B T TT BGGGEE E
EXPOSURE. * * * 4 4 0 7 R 6 5 5 7 0 4 8 * * 1 2 6 '951'95331 * * 0 8 * * 2 6 0 5 * 5 4 5 3 3 * 8 2 * 83"
1 S E Q U E N C E , MKKYTCTVCG Y I Y B P Z R G B P BBGVBPGTBF K B I P B B W V C P LCGYCKBZFZ Z V Z Z
141 1 A Z U A Z U R I N [ E L E C T R O N T R A N S P O R T , C O P P E R B I N D I N G ] (PSEUDOMONAS AERUGINOSA)..........................................lAZU

SHEET.. .. AAAA BBB AMAAA A c BBBB B C AAAAAA
BRIDGE2.. BBBBBB E
BRIDCE~. . aaaa ccc aaa a G DDDD E G B BBBBB
CHIRALITY -+----+-+ --+++----- ++-+-----+ --+-+--++- +---+-+--t ++++++++++ ++--++--+- ----+++++- --+--++-+- --+--+++--
BEND.. ... sss s ss ssss s s sss s s ssssssssss sss sss ss ss ss s ss sss
5-TURN. + . >5555< >5555<
4-TURN.. >444 < > 4 44x>>>xxxx < < < x > 4 4 < <
3-TURN.. >33< > 3 3x33< >33< > 33< >33<
..
SUMMARY.. E E E E SSS S S S E E E S S S S E E E E E E E SS TTT S B E E E E T TTTHHHHHHH HHH HHHHSS S S TT SB B T T E EEEEESSS
EXPOSURE. *3*09074*5 8274*61*8* **5**13040 41629759.7 3 0 8 8 8 8 8 8 2 6 9 5 3 9 1 0 3 8 6 8 8 8 2 2 7 * * 4 4 1 9**296351' 0 8 1 8 0 3 7 8 8 4 51*1836"1*
1 SEQUENCE. S M I Q G N D Q M B N T N A I T W K S C K Q F T W L S H P G N L P K N V MGHNWVLSTA A D n Q G W T D G MASGLDKDYL K P D D S R V I A H T K L I G S G E K D S V T P D V S K L K
SHEET.. .. BBBB BB BBBB

BRIDGE2.. FFFF FF FF
BRIDGEl.. DDDD ccc
CHIRALITY ++----+--+ --+++++++- -+-
BEND..... SS sss ssss
5-TURN..
4-TURN.. >444<
..
3-TURN.. . >3><3<
SUMMARY.. SS EEEE S T T T T T T S E E EEEE
EXPOSURE. '89'140808 264128'040 5863.
101 SEQUENCE. EGEQYMPFCT P P G H S A L R K G T L T L K
SUMMARY.. ..... .HIALPHA-HELIX.. ..E=BETA-STRAND.. ..BIBETA-BRIDGE.. ..G-3-HELIX.. .. 1 - 5 - H E L I X . . ..T-3-, 4-, OR 5-TURN.. .SEEEND..
. ..
TABLE A111 (continued) E3
Q)
0
l P C Y PLASTOCYANIN [ELECTRON TRANSPORT, C O P P E R B I N D I N G ] ( P O P L A R LEAVES: POPULUS NIGRA VARIANT I T A L I C A ) .............. lPCY Lo
SHEET,. .. AAAA AA E B B B AAAAA A C B B C AA AAA BBB B B B BBBBEB
BRIDGEZ.. BB ccccc F F F FFF FFFFFF
BRIDGEl.. aaaa BB ddd d aaa a G E E G CC CCC EE dddd
CHIRALITY ---t--t-+ -+--+t+t-t --+t------ +-+-++--I- --ttt--tt- -tt++---++ --tt-tt--- t--tt-t--- t---+t++t- t+t----
BEND.. ss ss s ssss ss ss ssss ss sssss ss sss s s SSSSSS s
5-TURN.. > 5 5 5 5<
....
4-TURN.. >>44<<
3-TURN.. >33< >33< >33< >33< >>3<< >33 < >33< >>3<x33 <
..
SUMMARY.. EEEES TT S E E S S E E E E T T E E E E E E S S B E E TTSS T T HHHHS T T B S T T E E EEE S EEE E E E GGGTTT T E E E E E E
EXPOSURE. 6 9 0 5 0 0 2 * * 4 6 6 3 0 6 5 5 ' 2 7 0 6 6 5 8 9 0 3 0 6 0 3 2 4 7 5 0 0 0 1 1 5 * * 5 2 2 * 9 3 829'1224'' 871*5'4765 *14089*3*0 3050474997 48715038'
SEQUENCE. IDVLLGADDG S L A F V P S F S S I S P G E K I M K N N A G F P H N I V F D E D S I P S G V D A S K I S M S E E D L L N A K G E T F EVALSNKGEY S F Y C S P H Q G A GMVGKVTVN
1 P P T A V I A N P A N C R E A T I C P O L Y P E P T I D E [HORMONE] [ T U R K E Y P A N C R E A S : M E L E A G R I S G A L L O P A V O ) . ................................ lPPT

SHEET.. ..
BRIDGEZ..
BRIDGE1..
CHIRALITY --------t t--tttt+tt tttt+ttt++ +-tt
BEND.. s ss SSSSSSS ssssssssss sss
5-TURN.. > 5 555<
....
4-TURN.. >>>>xxxx xxxxxxxx<< << x
3-TURN.. > 3 3<>33< > 33<
..
SUMMARY.. T T S HHHHHHH HHHHHHHHHH H T T
>
EXPOSURE. *6**3**63* * 2 7 * * 6 6 9 * 4 *8*69*6932 99'"' Z
SEQUENCE. G P S Q P T Y P G D O A P M D L I R F YDNLQQYLNV VTRHRY U
1 G C N GLUCAGON ( P H 6 P H 7 FORM)
- IHORMONEI (PIG P A N C R E A S : SUS S C R O F A ) .............................................. lGCN
SHEET.. ..
BRIDGE2.
TZ
Y
BRIDGEl.,
CHIRALITY ++-+++tt+ ++t+t++ttt tt+t+tt
BEND..... S S SSSS SSSSSSSSSS SSSSSS
5-TURN.. .
4-TURN.. , > > 4 4 x <4>X4>XX>X <x<<4<
3-TURN.. . >>3<x 3>x3<< >>3<<
SUMMARY.. S S HHHH TTTHHHHHHH HHHTTS
EXPOSURE. t*+4'**8** 9++7*B"5. 8*9******
SEQUENCE. HSQGTFTSDY SKYLDSRRAQ DFVQWIMNT
1 I N S I N S U L I N ( A AND B C H A I N ) [HORMONEI I P I G : SUS S C R C F A I .......................................................... .1INS

SHEET.. .. A B A BBB
BRIDGEZ.. ccc
BRIDGEI.. A B A B
CHIRALITY ++t+tt--- --t+ttttt ---++-- t++t+++t++ +++----++-
BEND.. , SSSSSSS SSSSSSS s ssssssssss ssss
5-TURN..
...
(-TURN... >>>>X<<<< >>44<< > >>>xxxxx<<<<
3-TURN.. . >>><<< >> 3<< >>3<<
SUMMARY.. HHHHHHHS B HHHHGGGB B T HHHHHHHHHH HGGG E E E
EXPOSURE. 6 1 2 5 7 0 5 ' 7 8 825'709'72 *0'**9'143 3'805106'4 1 2 * * 0 0 8 1 7 3 **
SEQUENCE. G I V E Q a b T S I a S L Y Q L E N Y c N I F V N Q H L b G S H L V E A L Y L V c G E R G F F Y T P KA
SUMMARY........H=ALPHA-HELIX....E~BETA-STRAND..~~B~BETA-BRIDGE....G-J-HELIX....I=5-HELIX....T~3 -,4-, OR 5-TURN....S=BEND....

19) 1 B P 2 PHOSPHOLIPASE A2 [PHOSPHATIDE ACYL-HYDROUSE] [ C W PANCREAS: 80s TAURUS)......................................lBP2
SHEET.. .. A A BBBB BBBB
BRIDGE2.. B
BRIUGEl.. A A cccc cccc
CHIRALITY +++++++++ +++++--+++ ++++--+++- --++-----+ ++++++++++ +++++++-++ +++-+--+++ -+-+--+--+ -----++--+ ++++++++++
BEND..... SSSSSSSS SS SS SSS SSSS S S S S S S SS S S S S S S S S S S S S S S S S S S S S SS S S S S SSS sss ss s ssssssssss
5-TURN.. . >55 55< >5555<
4-TURN... > > > > X X X X X < <<< > > 4 4 << > 4 4 4 < > > >>xxxxxxxx x x < < < < >>> 4 < < < > 4 4 4 < >> >>xxxxxxxx
3-TURN.. . >33<>33< >33< >>3<< >33< >33< >33 < >33<
SUMMARY.. H H H H H H H H H H H TT H H H HTTTBTTTBS S S S SSH H H H H H H H H H H HHHHHTT H H HHHTT TTT EEEETT EEEE TT H HHHHHHHHHH
EXPOSURE. 1 * * 0 2 4 2 0 1 7 1339*1'0** 6 2 7 6 0 0 0 3 0 3 '5383'352' 0 0 ' 8 1 4 7 2 4 7 32'90**4*4 0'*9*580*9 0'066667'8 *0844*'277 0546007007
1 SEQUENCE. ALWQFNGMIK aKIPSSEPLL DFNNYGbYcG LGGSGTPWD LDRdcQTHDN eYKQAKKLDS fKVLMNPYT NNYSYSaSNN E I q S S E N N A fEAFIgNeDR
SHEET.. .. A
BRIDGE2..
BRIDGEl.. B or
CHIRALITY ++++++++-- --++++---+ +
BEND..... SSSSSSSSS SSSSS S S
)-TURN.. .
4-TURN... XXXX<<<<
3-TURN.. . >>3<< > > 3 x < 3 < > >3 < <
SUMMARY.. HHHHHHHTS GGGBT G GG
EXPOSURE. 8 0 8 4 4 1 4 ' 4 8 9 5 4 + 4 6 * 3 9 7 **6
1 0 1 SEQUENCE. NAAIdFSKVP YNKEHKNLDK KNb
20) lLZM LYSOZYME [O-GLYCOLSYL HYDROLASE] [BACTERIOPHAGE T 4 ) . ,

........ .................................... . .....lLZM
SHEET.. .. ABAA AAAA AA A B
BRIDGES.. BBB
BRIDGE1.. ACAA AA A 88 B C
CHIRALITY -++++++++ +-+-+-+--+ ----+-+-++ +++++++++- +-+--++--+
----+-+--- ++++++++++ ++++++++++ -+++++++++ --++++++++
BEND..... SSSSSSSS S SS SSS SSS S S SS SSSSSSSSSS SS SS S SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS S SSSSSSSS
5-TURN.. . > > 5 5 5 <<
4-TURNe.. >>44<X44 4 < >444 < > >4>xx><<<< >> 4 > x x > x x < < x x>>xxx<<<<> 4 4 > x > > < < < <>>>>xxxxx
3-TURN.. . >>3<< > 33< >33< >33< > 3 3x33< > 3 3 < > 3 3 x > 3 < x 3 3 x > 3 < x 3 3 < >33< >>
SUMMARY.. SHHHHSTT T EEEEEE TTS EEEETT EEEES S S S HHHHHHHHHT TS TTB H H H H H H H H H H H HHHHHHHHHT STTTHHHHHH S H H H H H H H H
EXPOSURE. 8 6 3 6 9 0 6 ' 5 2 424*7*25*4 * * 4 9 3 0 1 0 1 2 3812.4'68' 3 0 3 7 6 8 3 ' 5 5 6*'1*0726* *309*119*4 17414'809' 3**0'504'2 1572381001
1 SEQUENCE. MNIFEMLRID EGLRLKIYKD TEGYYTIGIG HLLTKSPSLN AAKSELDKAI GRNCNGVITK DEAEKLFNQD VDAAVRGILH NAKLKPWDS LDAVRRCALI
SHEET.. ..
BRIDGE2..
BRIDGE1..
CHIRALITY +++++--+++ ++++++++++ ++-+++++++ +++++-++++ ++++++++++ ++++-+-+++ +-
BEND..... SSSSSS SSS S S S SSSSSS SSS SSSS SSSSSSSSSS SSSSSSSSSS SSSSSSS S SS
5-TURN.. . > 5555<
4-TURN... XXX<<<X>44 << >>>4XX< 4<< >444< > > > 4 < < x > > > x x < x xx > < < < <
)-TURN... 3<< >>3< X33< >>3 X<3< > 3 3 < >33< >3><3< >33<
SUMMARY.. HHHHHH H H H HTT HHHHHH HHTT TTTS SSSTTSHHHH HSHHHHHHHH HHHHHSS S SS
EXPOSURE. 00136636*4 01639881'4 19'**5'801 8583'3.17. '37.209581 508.725542 1*.*
1 0 1 SEQUENCE. NMVFWGFTC VAGFTNSLRM LQQKRWDEAA VNLAKSRWYN OTPNRAKRVL TTFRXTWDA YKNL t
9
a3
SUMMARY.. ..... .H=ALPHA-HELIX.. ..E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..Ga3-HELIX.. ..I-5-HELIX.. ..T=3-, 4-, OR 5-TURN.. .. S-BEND.. .. 0
w
TABLE A111 (continued)
7LYZ LYSOZYME (TRICLINIC CRYSTAL FORM) [O-GLYCOLSYL HYDROLASE] (HEN EGG WHITE: GALLUS GALLUS)......................7LYZ
SHEET.... A B B A CC CC CC DD DD
BRIDGE2.. DD
BRIDGE1.. A B B A CC CC DD ee ee
CHIRALITY t+++t+ ++++-tt-t- -t--+ttt+t tttt---+-t +-----t-t- ----t----t
--- ttt-t-t+-+ ++-++-t--+ +tt+-t-ttt +++++t+t+t
BEND.. ssssss ssssss sss ss ssssss ssssssss s s sss sss s sss ss s s ss s sssssss ss ssssssssss
5-TURN.. >5555< >5555< >5555<>5 555<
4-TURN.. > > > 4 x x x ><<<< >>>>xx xx<<<< >444< > 4 44< >>> >xxxxxx<<<
...
3-TURN.. . >33<>3>x 3<<>>3<< > 3 3< > 3 3< > 3 3 < > 3 3 < >> > x < < < >3 3< >33
SUMMARY.. B H H H H H H HHHHTT TTB TTB THHHHH HHHHHTSSBT T EE SSS EETTTTEET TTTEE SS T T TT EEG GGGGSSS HH HHHHHHHHHH
EXPOSURE. 9'1473.803 108'6506'7 ' 6 5 4 0 0 2 0 0 0 0 0 5 6 5 2 9 3 5 0 *287'7*720 8 2 2 0 0 0 1 0 3 0 6'38746'19 65'672*470 8304669152 1 0 9 0 0 5 '1 1 3
SEQUENCE. KVFGRaELAA AMKRHGLDNY RGYSLGNWVb AAWESNFNT QATNRNTDGS TDYGILQINS RWWcNDGRTP GSRNLdNIPc SALLSSDITA SVNdAKKIVS
SHEET.. ..
BRIDGE2..
BRIDCE1..
CHIRALITY -t--ttt-+t ttttt-t-tt tttttt-
BEND.. sss s ssss ssssssss ssssss
5-TURN.. >5555<
....
4-TURN.. < > > > ><<<<
3-TURN.. < >>><<< > 3 3 < > >3 < < > 3 3 <
..
SUMMARY.. SSSGGGGSHH HHHHTTTS G GGSSTT
EXPOSURE. * 7 * 1 0 5 5 1 7 1 2***0*97*1 '364'72.9
SEQUENCE, DGDGMNAWVA WRNRbKGTDV Q A W I R G a R L
lSNS STAPHYLOCOCCAL NUCLEASE ICWPLEX) [PHOSPHORIC DIESTER ( D N A ) HYDROLASE] (STAPHYLOCOCCUS AUREUS)

SHEET.. .. A AAAA A AAAAA AAAAAA 80 AAAAA A
..........AAAA
AAA
......AAlSNS
BRIDGE2.. ccccc ddd EEEEE F E EEEE
BRXDGEI.. A AABB B B BB CCCCC HH AAA F ddd GG GG
CHIRALITY +++-+---- +--+--+--+ ++-+----+- +------+-- ---++-+--+ --++++++++ ++++++++-+ -------++- t--+-t--+- -----+--++
BEND.. ssss ss s ss ss ss ssss s ssssssss ssssssss s ss sss s sss ss
5-TURN..
....
4-TURN.. >>>>xxx xxxx<<<< >>>
3-TURN.. .. > 3 3< >33< >33< > 3 3 < >33x33< >33< >33<
SUMMARY.. SSSS E EEEEEEE ST TEEEEE S S EEEEEETTEE S S STTS S TTHHHHHH HHHHHHHT S EEEEE SS B TTS EEE EEEETTEEHH
EXPOSURE. * * 7 + + + 4 * 6 4 '1'39'2718 0 1 1 7 8 7 4 * 6 * ' 5 3 8 3 1 1 1 0 3 0153*****3 "6'887'836 519'219'2' '1 4 8 13 0 * 2 9 * 9 2 + * 4 7 0 3 0 082075'218
SEQUENCE. ATSTKKLHKE PATLIKAIDG DTVKLMYKGQ PMWRLLLVD TPETKHPKKG VEKYGPEASA FTKKMVENAK KIEVEPNKGQ RTDKYGRGLA YIYADGKMVN
SHEET.. .. 8 8
BRIDGE2..
BRIDGE1.. H H
CHIRALITY ttttt-tt-- tt---tt+tt ttttt+tt+t +ttt---+++
BEND.. ssssssss ss s ssssssssss sssss sss
5-TURN.. >5555< >5555<
....
4-TURN.. >X<<<< >>>>xxxxxx x < < < <
3-TURN.. >33x33< >33<>3 3< > 3 3 < > > > < <<
..
SUMMARY.. HHHHHTTS E E TT T THHHHHHHHH HHHHTT GGG G
EXPOSURE. 4 2 0 8 8 * 0 1 8 9 01'3**4146 34'989'125 787'9'4444 5'
SEQUENCE. EALVRWLAK VAYWKPNNT HEPHLRKSEA QAKKEKLNIW SE
SUMMARY........H=ALPHA-HELIX....E~BETA-STRAND....B-BETA-BRIDGE....G~3-HELIX....I~S-HELIX....T~3 - , 4 -, OR 5-TURN....S=BENDe...
23) lRNS RIBONUCLEASE-S [PHOSPHORIC DIESTER ( R N A ) HYDROLASE] ( C W PANCREAS: 80s TAURUS). .lRNS
AAAAA BBB B B BBB A AAAAAAA C
SHEET.. .. A
.............................. C AM
BRIDGEZ.. BBBBB EEE C CCCCCCC
BRIDGE1.. a a DDD D D DDD BBBBB G G CCC
CHIRALITY --+++++++ +++--+-+ ---+++++ +++-+-++-- ---+----+- -+++++++++ --+---+-+- ++----+--- +---+---++ +-+++----+
BEND..... SSSSSSS SS SS sssss ssssssssss s s sssssssss ss sss ss ss ss ss
5-TURN.. >5555<
4-TURN.. > > > > X X X < <<< > > > > x x <<<< >>>4<<< >444<
..
3-TURN.. . >33< > > > x < << >33< >33 <>33<
SUMMARY.. HHHHHHH HHB SS H H H H H HHHTTSSSSS SEEEEE S HHHHHGGGG SEEEEETTTE E E E E E SS E EEEEEEE TT BTTB EEE
EXPOSURE. '584348688 3114667*6* kl"45801.3 8876580*9* 2 4 9 5 2 1 8 8 2 5 376987588' 4*9470**69 '48456'761 31138*6889 2*'7'241*5
1 SEQUENCE. KETAAAWER QHMDSSTSAA 1 SSSNYaNW MKSRNLTKDR bKPVNTPVHE SLADVQAVCS QKNVAdKNGQ TMYQSYSM SITDaRETGS SKYPNbAYKT
SHEET.... AAAAA BBBB B B B B B B

BRIDGE2.. FFFF F
BRIDGEl.. CCCCC EEE F F F F F
CHIRALITY -+-+---+-- ++-+-+-++- +--
BEND.. sss
5-TURN..
....
4-TURN..
3-TURN..
..
SUMMARY.. EEEEE E E E E E SSS EEE EEEE
EXPOSURE. 6.38660306 8*5*9*3126 3 3 2 4 8
101 SEQUENCE. TQANKH I IVA c EGNPYVPVH F DASV
24) ICPA CARBOXYPEPTIDASE A (C-TERMINAL A M I N O ACID HYDRCLASE] ( C W PANCREAS: BOS TAURUS) SICPA
..............................
SHEET.. AAAAA AA AAAAAA A A AAAA B B
BRIDGE.?. BB B d dddd
...
BRIDGEl.. AAAAA AA AAMAA A c cccc h h
CHIRALITY -+++-+++- ---+++++++ ++++++++++ ++---+---- +-+------- +--+------ -++++++-++ ++++++++++ ++++++++++ +-++++++++
BEND..... SSS SS SSSSSSS SSSSSSSSSS S sss s ss ssss ssssssss ssssssssss s ssssssss
5-TURN.. .
4-TLBN..
. .-......- >>>>YY!iY Y Y X < < < 0 4 4 A<
......................... >>>>xxxxx x x < x x < 4 x < 4 4 x > > > x < x < <
3-TURN.. >33<
. > 33< >33 < > 33< > 3 3 x33< >33< >33x33
SUMMARY.. STT SS HHHHHHH HHHHHHSSTT TEEEEEEEE TTS E E E E E E E S SS E EEEE SSTT THHHHHHHH HHHHHHHHBT TBHHHHHHHT
EXPOSURE. *30**38355 4351*803*0 695837748' 3076**22*1 * * 2 8 3 0 4 8 0 5 0 2 5 3 5 f 8 5 4 0 R000880003 0 4 8 0 0 1 0 0 1 4 8014018286 '594035067
1 SEQUENCE. RSTNTFNYAT YHTLDEIYDF MDLLVAQHPE LVSKLQIGRS YEGRPIYVLK FSTGGSNRPA IWIDLGIHSR WITQATGVW FAKKFTENYG QNPSFTAILD
SHEET.. .. AAAAA C C eeeee
A A AAAAA A
G
BRIDGES.. CCCCC
BRIDGE1.. EBB i i d d ddd f
CHIRALITY +------+++ +++++++++- ++++++--+- ++-+-+-+-- -++++-+--+ +-++--+-++ -++---+-++ +-++++++++ +++++++++- ---+-++-+-
BEND..... SS S S S SSSSSSSS S SS S ss s ssssssss sssss s ss sss ssss sssssssss sssss s ss
5-TURN.. . > 5 5 5 5<
4-TURN...
. . . . . . .A< >>>d<YYdA<
........... < >h44< > > 4 > x x > x x xx<<<<
3-TURN... < >33<>33< >33< >>3<< > 3 3< >33 x33< > 3 3 <>33x33< > 33<
SUMMARY.. TSEEEEES S SHHHHHHHHH T TT S ss s GGGSSSSST TSSSSBS TT STTB SSTT SHHHHHHHH HHHHH EEE EEEEE SS E
EXPOSURE. 6108000080 0 0 0 0 1 2 4 0 7 9 * 6 5 9 3 3 8 0 5 1 7*8*3*5381 0 0 8 3 8 0 8 0 1 6 5'61339737 374220**22 2160071807 41**36518R 0 0 0 0 8 0 7 3 2 2
1 0 1 SEQUENCE. SMDIFLEIVT NPNGFAFTNS ENRLWRKTRS VTSSSLaVGV OANRNWDAGF GKAGASSSPa SETYHGKYAN SEVEVRSIW FVKNHGNFM FLSIHSYSQL N
Q,
0
SUMMARY........H~ALPHA-HELIX....E-BETA-STRAND....B-BETA-BRIDGE....G~3-HELIX....I~5-HELIX....T-3-,4-, OR S-TURN....S-BEND.... UI
tQ
TABLE A111 (continued) 0,
0
SHEET.... AAA AAA A AAAAA Q,
BRIDGEZ.. GG GGG
BRIDGEl.. fff fff f eeeee
CHIRALITY t--++++-+- --++++++++ ++++++++++ +-------+- -++++----+ +-+++++++- +++++----- +--+-+-++- -+++++++++ ++++++++++
BEND..... S SS ss SSSSS ssssssssss sss S SSSSS s ssssssss s s s ssssss sssssssss ssssssssss
5-TURN.. > 5 5 5 5<
4-TURN.. >>>>xxx xxxxx<<<< >>44<< > > > > x x < < << >>>>xxx xxxxxxxxxx
..
3-TURN.. . >33< >>3< < >33< >>><< < >33< >>3<< >33<
SUMMARY., EEES SS TTHHHHHH HHHHHHHHTT SSS EEE EHHHHS S H H H H H H H H T S EEEEE S SSSSTT GGGHHHHHH HHHHHHHHHH
EXPOSURE. 00102044** 61948'5869 00*502630* 9 8 * 4 1 8 2 * 9 0 285857'610 0 0 0 0 0 2 0 2 7 8 6 1 6 0 0 0 0 0 0 0 31'5*+14*1 43*4053005 0024002200
2 0 1 SEQUENCE. LLYPYGYTTQ SIPDKTELNQ VAKSAVAALK SLYGTSYKYG S I I T T I Y Q A S GGSIWSYNQ CIKYSFWEL RDTGRYGFLL PASQIIFTAQ EIWLGVLTIM
SHEET....
BRIDGE2..
BRIDGE1..
CHIRALITY ++++
BEND.. SSSS
5-TURN..
....
4-TURN.. X<<<<
3-TURN.. >>3<<
..
SUMMARY.. HHHHT
EXPOSURE. 7604**042
3 0 1 SEQUENCE. EHTVNNIGY
25) 1APR ACID PROTEASE [HYDROLASE: PROTEINASE] (RHIZOPUS CHINENSIS). ................................................... lAPR
SHEET..
.. A AB C C CC BBB B DD E E F GGF H H
BRIDGEZ.. ccc
BRIDGE1.. A AB E E B D ff g 9 H IIH J J
CHIRALITY -+------- --++----+- --+--+-+--EE ----++-+-+ ----++--++ +++-+----- +++-+++--- +--+--+-+- ---+--++-+ +----+---+
BEND..... S ssss sss ss s ss ss ss sss ss ss sss
5-TURN..
4-TURN.. >444<
..
3-TURN... >33< > 33< >33<
SUMMARY.. TT B TTSS B B E E SSS EE EEESS B EE BS SS SS SS B TTT SS B SS EEB BSSS B
EXPOSURE. ''0489273' 5'04512090 4 0 1 2 ' 5 6 7 1 5 0 1 1 1 0 2 2 0 1 1 1 1 0 8 6 8 1 ' 5 5 0 0 * 8 6 2 8 7 1 5 4'80*66*75 9**175584* 2 6 1 5 1 5 0 1 1 4 1 0 6 1 2 6 1 7 0 5
1 SEQUENCE. GVGTVPMTDY GNDVEYYGQV TIGTFGKSFN LNFMGSSNL WVGSVQaQAS GaKGGRDKFN PSDGSWKAT GYDASIGYGD GSASGVLGYD TVQVGGIDVT
SHEET.. .. DDG G BBB I1 I I11 J K LL

BRIDGE2.. D
BRIDGE1.. ffI I ccc KK K KKK L H 00
CHIRALITY -------++- ---++++-+- ----++--+- ++-+-++--- +++++++-++ -+-++--++- --++-+---+ -+----+++- +----+---- ++----+---
BEND..... S S SS SSSSSSSS SS S SS S SSSSS SSSSSSSSSS SSS sss 5s ssss s ssss
5-TURN..
4-TURN.. > >4>x<4<< >444<
..
3-TURN.. . >33< > >3<< >33< >33<
SUMMARY.. S TT EEEEE SSSSSSSS SSEEE S SS S SSSSS HHHHHHHSSS SSS EE E TTT EEE SS TTSB S B SSSS EE
EXPOSURE. 4 0 1 5 1 2 1 0 4 9 1 2 4 4 6 2 4 6 3 1 0 0 2 0 0 0 0 1 4 9 7 3 1 5 2 * * 1 7 0 1 0 4 1 0 6 8 6 8 8 1 * * 3 0 0 0 0 4 0 0 2 3 * * 8 5 1 3 0 2132'5*'43 37'2591726 21'1701078
101 SEQUENCE. GGPQIQLAQR LGGGGFPGDN DGLLGLGFDT LSITPQSSTN AFDQVSAWK VIQPWVVYL AASNISDGDF THFGWIDNKY GGTLLNTNID AGEGYWALNV
SU~MARY ........H~ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIDGE....G~3-HELIX....I=5-HELIX....T~3 -,4-, OR 5-TURN....S=BEND.. ..

SHEET.. .. LL MM N 0 0 N LMM
BRIDGE2.. P
BRIDGEl.. 00 QQ R s s R PQQ
CHIRALITY +++--++-++ --+-+---++ +-+--+--++ +++-++++-+ ----+-+++- ---+++++-- ----+--+-- --++++++-- ---+--+--- -+-+-+----
BEND.. ssss s s ssss ss sssss ss ssss s ss sss ssss sss ssss
5-TURN.. > 5555<
....
4-TURN..
3-TURN.. >3 3< >>3x<3< >33<
..
SUMMARY.. SSSS S EE T TSSSEE S S TTTGGGTTS SSSS B S TTS BSSS B SSSS SSS B SSSSBEE
EXPOSURE. 5 1 0 5 0 6 * 5 * 0 2 6 * 2 ' 0 1 0 1 1 4 4 3 4 0 4 8 2 7 . 1 0 3 2 8 1 6 6 1 8 3897.73218 6155'4773. 301150**1* 0714800354 ***9314001 0 0 4 9 6 6 8 0 2 0
2 0 1 SEQUENCE. TGATADSTYL GAIF QAILDT GTSLLI LPDE AAVGNLVGF A GAQDAALGCF VIAbTSAGF K S IPWSIYSAI F EIITALGNA EDDSGbTSGI GASSLCEAIL
SHEET.. .. P KKK KKK PJ

BRIDCEZ., NNN
BRIDGE1.. T NNN M
CHIRALITY -++++++--- -+-+-+---+ --TL
BEND.. sssssss sss
5-TURN..
....
4-TURN.. >>44<< >444<
?-TURN.. >77<
. ....
..
SUMMARY.. HHHHTTB EEETTTEEE BB
EXPOSURE. 0 0 0 0 0 1 4 1 0 0 0 0 2 5 ' 7 1 0 5 0 854'
3 0 1 SEQUENCE. CDQFLKQQYV VFDRDNGIRL APVA
26) l A P P A C I D PROTEINASE, PENICILLOPEPSIN [HYDROIASE: PROTEINASE] (FUNGUS: PENICILLIUM JANTHINELLUM] ...,.......,.......lAPP

SHEET.. .. A BBBBBCC CCCC CCC CCCCC CCC CC C D D cc c cccc c cccccccc c cc ccc c ul
BRIDGE2.. HHH HHH jjj 1 1 N 00 PPPP P PP PPP P M
BRIDCE1.. a BBBBBGG GG I HHHHH H KK K q MM M MMMM M MMMM MM I
3-TURN.. . >33< >33< >33< >33 < >33< >33< >33<

SUMMARY.. B EEEEEEE TTS EEEE EEETTEEEEE EEESS E E E BSSS H H H HTTS B H H HH EEEEEEE EEEE TTS E EEEEEEEEEE EETTEEEEEE
EXPOSURE. '472618062 2781710206 0302768060 2020110000 00048877*3 4 9 5 3 5 3 0 7 0 . 7 8 2 * * 5 * 7 6 8 882'6**515 0 3 1 2 0 1 4 1 4 0 4026078'50
1 SEQUENCE. AASGVATNTP TANDEEYITP VTIGCTTLNL NFDTGSADLW VFSTELPASQ QSGHSWNPS ATGKELSGYT WSISYGDGSS ASGNVFTDSV TVCGVTAHGQ
SHEET.. .. cccc cc c ccc C A BBBBB BBBBB E B BBB F G GGGG

BRIDGEZ.. DDDD DDDD xxx
PPP ;;j N a CCCC BBBBB R E EEE
BRIDGE1.. 11 00 s wwwww
----+++--+ +++++++--- ---+--+++- +--+-----+ +++++++-+- ++---+---+ ----+-++-- -+++------ +---+++-+- +--------- h
CHIRALITY
BEND.. ss s ssss s s s sss sss s ssssssssss s ss s s ssssss ssss S
5-TURN..
....
4-TURN..
)-TURN..
..
SUMMARY.. EEEE S E E H H H H H TT S E E E E s GGG BSSS H H H H H T T T ~ S S E E E E E ss s E E E E E S GGGBSS E E E E GGGTS B E E E E E E
EXPOSURE. 1 0 1 0 0 7 * 1 3 4 8 3 7 ' 4 7 8 1 1 0 1 0 0 0 0 2 2 9 5 2 3 1 * * * 7 5 5 0 0 03486.615. 410000848' '812000874 5 7 9 5 3 8 7 9 3 5 9241887'84 020*194240
1 0 1 SEQUENCE. AVQAAQQISA WQQDTNNDG LLGLAFSSIN TVQPQSQPTF FDTVKSSLAQ PLFAVALKHQ QPGWDPGF I DSSKYTGSLT YTGVDNSNF WSFNVDSYTA t3
Q,
SUnMARY........H-ALPHA-HELIX....E~BETA-STRAND....B=BETA-BRIDGE....G~3-HELIX....I~S-HELIX..~~T~3-,4-, OR 5-TURN....S=BEND.... s
N
TABLE A111 (continued) Q,
0
03
SHEET.. .. GGG F FF FF F HHHH HHHH GGGGG GGGGG H HHH HHHH FFF FFF
BRIDGEZ.. t tt V AA YYYYY BBBB V
BRIDGE1.. xxx S uu u 2222 2222 w YYYYY B BBB AA uuu ttt
CHIRALITY ++------+- ---++-+--+ --+++t+++t +t-+++---+ +-++++--++ -----+---- -+------++ ++---++--+ -----++--- -+--+---+--+
BEND.. ss ss ss ssssssss 5s ss s ssss ss s ss ss ss sss s s s 5s s
5-TURN. > 5 555< > 5 5 5 5<
.....
4-TURN.. >>>>xx<<<< > 4 44< > 4 4 4< >>
3-TURN.. 33< >33< >>> <<< > 3 3< >33 < > 33< >>> <<< >33 < >3
..
SUMMARY.. TTEEE E E E TT SSEE E H H H H H H H H TT SSEEEET TTTEEEE TT S EEEEE TTEEEEE GG GGEEEEETTT TEEEESEEE S SSEEE H
EXPOSURE. 3*791*4260 1 8 2 8 3 2 4 3 0 3 0 5 9 8 0 0 6 6 8 1 952*52**4* * 3 5 1 5 0 8 7 6 * 3 * 2 2 8 8 2 0 2 1 6 7 4 8 0 6 8 6 0 8 38331922.8 8 2 8 1 0 8 0 1 3 1 * 6 8 5 8 0 2 0 8 0
281 SEQUENCE. GSQSGDGFSG IADTGTTLLL LDDSWSQYY SQVSGAQQDSNAGGYWDaS SSVPDFSVSI SGYTATVPGS LINYGPSGNG STaLGGIQSN SGIGFLIFGO
SHEET.. .. I BBB B BBBB IE

BRIDGEZ.. F F FF
BRIDGE1.. C CCC C EEEE CR
CHIRALITY +++++-+--- -+-----++- -
BEND.. sssss sss
5-TURN.. >5555<
....
4-TURN.. 4><<4<
3-TURN.. 3x>3<<
..
SUMMARY.. HHHTTB E E E ETTTTEEEE B B
EXPOSURE. 8 0 0 1 1 0 0 0 0 0 33*7170080 5 4 8 P
3 8 1 S EQUENC E . IFLKSQYWF OSDGPQLGFA PQA
27) ZTLN THERMOLYSIN [HYDROLASE: NEUTRAL METALLO-PROTEINASE] (BACILLUS THERMOPROTEOLYTICUS)............................ZTLN

l3
SHEET.. .. AAAAAA A AAAA AAA AA B BB BBB BB AA AA B
BRIDGEZ.. bb C DD ff fff
BRIDOEl.. AAAAAA A AAAA A M C E E GG GG DD bb f
CHIRALITY +--+-+-+- --+-+-+--- +--+-+---+ -+++------ -----+-+-+ -----+-+-+ -++-++++++ ++++++++++ +++++++-+- --+-+-----
BEND.. sss sss ssss s s s s sss sssssss ssssssssss ssssssss ssssss
5-TURN.. >5555< >5555<
....
4-TURN.. > 4 4 4 < > 4 4 > < > > x >x < x < < 4 <
3-TURN.. >33< >33< >>3x<3< >33<
..
SVPIMARY.. E E E E E E E S S S E E E E E E E SSSEE B SSTT E E E E E TT S S S E E EESSS EE SGGGTTT SSTTTTTHHH HHHHTTTS STTTTS E
EXPOSURE. 9.48749138 *83'55*3*8 400*4**558 106853'082 0320'**8*6 6 3 5 3 2 5 2 6 9 2 9875'92118 0888'18018 1 3 1 8 7 * 7 2 * 3 88244*4228
1 SEQUENCE. ITGTSTVGVG RGVLGOQRNI NTTYSTYYYL QDNTRGDGIF TYDAKYRML PGSLWADAON QFFASYDAPA M A H Y Y A G V T YDYYKNVHNR LSYDGNNAAI
SHEET.. .. BBBB B BB B B B C DD C
BRIDGEZ.. hh h I 1
BRIDGEl.. ffff I1 h h h J KK J
CHIRALITY ---++---+- t-t---t+-- ------tt-- --ttt-tt++ +++ttt+t++ t-----++-t t+ttt++++t ++++tt+t+- t--+-+--tt +t--++-+++
BEND., s sss sss sss sss ssss ssssssssss sss ssss ssssssssss ssssssssss ss s ss sss ss ss
5-TURN.. > 5 555< >555 5<
....
4-TURN.. >444< > > > > x xxxxxxxx<< << >>> >xxxxxxxxx xxxxxxx<<< <
3-TURN.. >>3<< > 33<>33<
..
SVPIMARY.. EEEEEE'ITT E E SSSE E E E SSSB GGG H H H H HHHHHHHHHH HTT SSHH HHHHHHHHHH H H H H H H H H H H TSS SEES SSB SS SS
EXPOSURE. * 8 8 0 1 3 4 * 3 6 5 7 8 6 3 7 3 8 1 0 0883195'61 4 2 8 8 0 8 8 0 1 0 0 1 1 0 0 1 0 0 0 7 *4121998*6 1 8 8 8 0 8 8 8 8 0 1 8 8 0 1 8 8 3 9 4 * 4 * 4 3 3 3 8 0 3 587277**64
1 0 1 SEQUENCE. RSSVHYSQGY NNAFWNGSEH WGDGDGQTF IPLSGGIDW AHELTWVTD YTAGLIYCHE SGAINEAISD IPGTLVEFYA NKNPDWEIGE DWTPCISGD
SWMARY.. ..... .H-ALPHA-HELIX.. ..EsBETA-STRAND.. ..B=BETA-BRIDGE.. ..G-3-HELIX.. ..1-5-HELIX.. ..T=3-, 4-, OR 5-TURN.. ..SIBEND.. ..
SHEET.. .. DD EE EE
BRIDGE2..
BRIDGE1.. RK LL LL
CHIRALITY ----++++++ -+--+-+++- ++-++---++ ++++++++++ +++++-4-+- -+-------+ ++++++++++ ++-+--++-- ++++++++++ +++++--++-
BEND.. ... s ss sss ss ssss ssssssss ssssssssss ssssss s ss s ssssssssss ssss ss ssssssssss ssssss ss
5-TURN.. a > 5 5 55< >5555< > 5555< >5555<
4-TURN.. > > 4 4 x < 4 4 < > > > > x x x xx<<<< > 44>X4>XX4< << > >>>xxxxxxx x<<<< >
3-TURN.. .. >>3< < >>3<< >>><<< >> 3 < < > 33x33< >33< >33< >33<
SUWUARY.. SEESS GGG TT SGGG SSSHHHHT TTTTHHHHHH HHHHHT EES SS EE S TTTHHHHHHH HTTT TT HHHHHHHHHH HHHHTT TT
EXPOSURE. 0 5 3 0 0 4 8 0 5 * 77222369'' 7'34.59108 5 4 1 0 0 0 0 0 2 0 86001813*2 '758174239 '688908370 04'9167'14 0 5 9 0 3 4 1 8 4 9 80456839*1
201 SEQUENCE. SLRSUSDPAK YGDPDHYSKR YTGTQDNGGV HINSGIINKA AYLISQGGTH YGVSWGIGR DKLGKIFYRA LTQYLTPTSN FSQLRAAAVQ SATDLYGSTS
SHEET.. ..
BRIDGE2..
BRlDGE1..
CHIRALITY ++++++++++ ++-+
BEND..
5-TURN..
.... ssssssssss sss
> 5555<
or
4-TURN.. >>>xxxxxxx <<<<
3-TURN.. >33< > 3 ><3<
..
SWUARY.. HHHHHHHHHH HHHT
EXPOSURE. '204809508 80020'
301 SEQUENCE. QEVASVKQAP DAVGVK
28) 2GCH G M U A CHYUOTRYPSIN A [HYDROLASE: SERINE PRoTEINASEl ( C W PANCREAS: BOS TAURUS) ............... , ..2GCH
SHEET.. A 88 CCCC D CC
.. ccccc c cccc c c cccc c ccc ccccc
............... D
BRIDGEZ.. KKKK L L L unun N NNN 00
BRIDGEI.. A 88 JJJJJ J JJJJ LLL K KKK NNNNO 0000 P P nn
CHIRALITY +--+----- +++-----++ +++++----- +-+-++---- ---++--+-- ++----++-- --++++-++- ++-+-----+ +-----++-- ++-++-++--
BEND.. ss sss ss ssss ss ssss sss sss s s ss sss ss sss s
5-TURN.. > 5555<
....
(-TURN.. > 444<
3-TURN.. >33< > 3 3 <>33< > 33< >33< > >3<< >33< >33< >33<
..
SUUMARY.. SS SET E E TT SSTTEEEEE TT E E E E E E EEETTEEEE GGG TTSE EEES S TT SSS EEEEE E E E E E TT B TTTTBS EE
EXPOSURE. 48.854'29' 32*28*0472 8 1 0 0 1 0 0 0 2 4 *'5*141000 0 2 4 9 6 i 0 0 0 0 1 6 2 5 2 7 9 7 2 3 0002223464 '*5'64*0*: 5'44'0*'57 8'55338010
1 SEQUENCE. aGVPAIQPVL SVNGEEAVPG SWFUQVSLQD KTGFHFbGGS LINENWVVTA AHBGVTTSDV WAGEPDOCS SSEKIOKLKI AKWKNSRYN SLTINNDITL
SHEET.. .. CCC B B BBBBB 888 BBBB BBBBB A B BBBBB BBB

BRIDGE2.. 000 EE DDD DDD GGGGG H HHHHH HHH
BRIDGEl.. UU C D DDDDD 88 F F A EE C
CHIRALITY ---+----+- +++------- ++----++-+ ---+-+--+ -+----- +-----++++ +++--++--4 +--++++-+- ---+++++-- +--+--+---
BEND..... SS ss ss ss ss s ss ssss sssssss s s ss ss ss sss
5-TURN..
4-TURN.. > > 4 4 x <44<
..
3-TURN.. . > 33< >33< >> 3 < < > > 3 < < > 3 3< >33x33< >33<
SWUARY.. EEESS SS B TT TT E EEEEESS S SS EEE EEEB HHHH TTTSGGG T TEEEEE SS B TT TT E EEEEETTEEE
EXPOSURE. 8 6 8 7 6 5 1 8 7 7 '583102415 5.5'356559 080000846' '0929'1381 5840253'60 ***63*'18' 1 0 1 0 8 0 3 6 3 2 1 2 1 7 1 0 2 0 0 0 080'7'5221
1 0 1 SEQUENCE. LKLSTAASFS @TVSAVsLF5 ASDDFMGTT cVT'NiWGLTR Y I TPDRLQQA SLPLLSNTW KKYWGTKIKD AMIdAGASGV SseMGDSGGP LVCKKNGAWT N
Q,
SUWUARY.. ..... .H-ALPHA-HELIX.. ..E*BETA-STRAND.. ..B-BETA-BRIDGE.. ..G-3-HELIX.. ..I - ) - H E L I X . . ..T-3-, 4-, OR 5-TURN.. . .S=BEND.. .. 0
(0
N
TABLE AIII (continued)
2
0
SHEET.... B BBB B B B B B SB
BRIDGE2.. H HH I 1 I1
BRIDGE1.. I11 I GGGG G
CHIRALITY ++--+-++-+ ---++---+- --++++++++ +++++
SEND.. s s sss ssssssss sssss
5-TURN..
....
4-TURN.. > 4 4 > x > > x xxx<<<<
3-TURN.. >3 3<>33< >>3<<
..
SUMMARY.. EEEEEEE T T TTSEEEE EEGGGTHHHH H H H H H H
EXPOSURE. 0 0 0 0 1 0 5 3 2' 7 0 3 4 8 3 0 1 0 0 0 50 3 6 0 5'1 0 ** 138 8
2 0 1 SEQUENCE. LVGIVSWGSS TeSTSTPGW ARVTALVNWV QQTLAAN
2 9) lALP ALPHA LYTIC PROTEASE [HYDROLASE: SERINE PROTEINASE] (MYXOBACTER495: LYSOBACTER ENZYMOGENES) ........., , ,..... . .lALP
SHEET.. .. A BBB B BBB BBBB BBB BB BBBS BB BBB BBB C BBSBBB AAA A AAAA D
BRIDGE2.. DD D FF G GG HHHH I11 111 111111 BBB B
BRIDGE1.. a CCC CCC EEEE E E E E DDD H H HH j GGG a BBBB q
CHIRALITY -+-++---- --++-+---- -+----+-t- -+--+++--+ +----+-+-+ -----+--++ --++-..---- ++----+--+ --+----+++ +----++-+-
BEND.. ss sssss sss ssss s s ssss s s sss ss ss
5-TURN..
...
4-TURN..
3-TURN.. >33< >33< > 3 3< >33< >33< >33<
..
SUMMARY.. BT EEE ESSSSEEE EEEETTEEE EE SSSS T T EEEETTEE EEEEEEEE S S EEEEEE SSS EEE ETTEEEE B TT
EXPOSURE. 6'02817702 1 8 * 7 8 8 0 0 0 0 0105'89640 0 0 0 0 0 4 2 0 9 6 ' 0 5 8 6 1 8 8 6 8 0 0 6 1 4 3 9 6 2 4 3 4 0 4 0 2 0 3 2 6 993'443.03 58'7'140.1 3973675370
1 SEQUENCE. ANIVGGIEYS INNASLaSVG FSVTRGATKG FVTAGHaGTV NATARIGGAV VGTFAARVFP GNDRAWVSLT SAaTLLPRVA NGSSFVTVRG STEAAVGAAV
SHEET.... CCCC CCC C C CC C CC CC CCCC E CCC D CCC C C E cc ccc BS

BRIDGE2.. LL MU MMMM 00 PPP P P PP PPP
BRIDGE1.. KKKK KKK K M MM M MM j NNN R LL q 00 R NN N FF Z
CHIRALITY --+-++--+- +--++-++-- -+-+-----+ --+-+----+ ++++--+--+ -+-+---+-+ ----+-+-++ +--+++-+-- ---+++++++ -+----
BEND. sss s S sss s ssss s s ssssss ss sss sssssss s U
5-TURN.. >55 55< M
.....
4-TURN. >444< >444< > > 4 > x < 4 << z
3-TURN.. >3 3x33< >3 3< >33< >>3<< >33<
...
SUMMARY.. EEEETTTEEE E EEEEEEE EE SSSEEEE EEEE S BT T TT EEE T T B EEEEE E TTSBSS SS GGG E E EEESHHHHHH HT E E
EXPOSURE. 0081.55455 6 2 4 8 5 3 7 ' 4 7 1*6'*360*2 004020010* 102000003* 7 0 6 0 1 0 0 0 0 1 3367**0207 6383**5401 1080*302** 24172395
1 0 1 SEQUENCE. bRSGRTTGYQ bGTITAKNVT ANYAEGAVRG LTQGNACMGR GDSGGSWITS AGQAQGVMSG GNVQSNGNNC GIPASQRSSL FERLQPILSQ YGLSLVTG
30) IPTN BETA-TRYPSIN (NATIVE AT PH 8) [HYDROLASE: SERINE PROTEINASE] ( C W PANCREAS: 80s TAURUS) ............ lPTN
SHEET.... A BB ccccc c ccccc c cccc cccc ccccc cc cc
...........ccccc
BRIDGE2.. KKK LL L MMMM NNNN 00000
BRIDGEl.. A BB JJJJJ J JJJJ LLL KKK N N N N O 00 00 MMMM
CHIRALITY ++------+ +-++----+- +-++-+--+- -++--+--++ ++-++----+ +++-++-+-+ +--+---+-- ---++--++- +++++----- +----+-+++
BEND...,. S SS SSSS S SS sss ss s ss s sssss s S ss sss s ss sss
5-TURN..
4-TURN.. >444 <
..
3-TURN.. . >33 0 3 3 < >33< > > 3 << >33< >33< >33<
SUMMARY.. BS EE TT SSTTEEEEES SSEEEEEEEE ETTEEEE GG G SS EEEE S SSTTS S EEEEEEEE EE TT TTT TT EEEEE SS SSS
EXPOSURE. 0153.82364 9132100023 7 * 4 3 1 0 0 0 0 2 5 4 7 1 0 0 0 0 0 7 0 * 5 * 6 1 5 0 5 0 1 1 2 3 3 * 7 * * 5 5 3 3 8 2 4 2 7 6 4 452'7678'7 3420000040 *851887*70
1 SEQUENCE. IVGGYTaGAN TVPYQVSLNS GYHFbGGSLI NSWWSAAH bYRSGIQVRL GEDNINVVEG NEQFISASKS IVHPSYNSNT LNNDIMLIKL KSAASLNSRV
SUMMARY. ....... H-ALPHA-HELIX. ...E-BETA-STRAND ....B~BETA-BRIDGE....G~3-HELIX....I-5-HELIX....T=3 -,4-, OR 5-TURN....S-BEND....

SHEET.... B . BBBBBB BBBBB BB B BBB A B BBB BB BB B B D
BRIDGE2.. EE DDDDD D G GGG H HHH HH H H
BRIDGEl.. c DDDDDD BB F F A EE c I I I I P
CHIRALITY ------+--- -++----++- +--+-++-+- --+-----+- ----++++++ +-+++--++- -++--+-+++ ---+++++-- ----+-++-- +-+----+-+
BEND.. ... ss ss s sss ss ssssss ssss ss s ssss ss s ssss ssss s
5-TURN..
4-TURN.. . > > > > x < << x 4 4 4 <
3-TURN.. . >33< >33< >33< >33< >33x33< >33< >3
SUMMARY.. B SS TT EEEEEE S SSS S S EEEEE EB H H H H H H HSTTT TTE EEES TTSS B TT TT E EEETTEEEEE EEE SSSSBT
EXPOSURE. 351851'763 8664'14000 0 0 0 2 * 6 * 5 +6 ' 2 7 3 0 4 0 1 * 0 4 1 2 5 9 9 2 0 9 8 1 0 9 9 9 2 4 8 3 1 2 0 0 0 7 7 * 1 4 ' 1 1 1 * 2 0 2 0 0 0 010'490100 115375118'
101 SEQUENCE. ASISLPTScA SAGTWLISG WGNTKSSGTS YPDVLKaLKA PIffiNSSeKS AYFCQITSNM FeAGYLQGGK DSfQCDSGGP WdSGKLQGI VSWGSGfAQK
SHEET.. .. D BBBBB
BRIDGEZ.. 1111
BRIffiE1.. P GGGG
CHIRALITY ++------++ ++++++++++ t or
BEND..... S ss ssssssssss s
5-TURN..
4-TURN.. > > > > x x x x <<<<
..
)-TURN.., 3< >>> <<< > 3 3<
SUMMARY.. TB EEEEEGG GGHHHHHHHH H H
EXPOSURE . 870 0 0006 0 2 7 1 3950**14 8 89
2 0 1 SEQUENCE. NKPGWTKVC NYVSWIKQTI ASN
31) lSGA PROTEINASE A ISGPA) . . [HYDROLASE: SERINE PROTEINASEl ISTREPTWYCES GRISEUS) , ... ................................. lSGA
SHEET.. .. AA AA BB BB BBBBBB i 'BBB B c BBBB B - D DD DDD EEEEE
BRIDGE2.. C C DDDD FFF F FFF F NNN
BRIDGE1.. AA AA BB BB BBBB E E a DDDD L LL LLL MMMMM
CHIRALITY -++-+++-- +-+-----+- ---+-+--+- -+++++--++ -+----++++ +++-+----- -+-+++--+- ---+-+---- +-+----++ -----+-++-
BEND..... SSS SS S sss ssssss s ss sss sssss ss sss ss sss
5-TURN.. .
4-TURN.. >>44<<
3-TURN.. .. >33< >33< >33< >33 <
SUMMARY.. SSSEE SS S EE EE EETTEEEEEE HHHHSS S BTTEEEEE SBS EEEE ESSTTS SE EE S S S EEE TT EEEEE S S S
EXPOSURE. 4 0 0 0 5 5 0 4 5 7 9 5 * 1 0 0 0 1 1 1 42'6422008 0040068349 1 6 2 1 7 7 9 1 5 3 478202000* 18'9832528 0447'7776' 08724*2*96 2817000251
1 SEQUENCE. IAGGEAITTG GSRCSLGFNV SVNGVAHALT AGHCTNISAS WSIGTRTGTS FPNNDYGIIR HSNPAAANGR WLYNGSYQD ITTAGNAFVG QAVQRSGSTT
SHEET.... EEEEEC C C CC cc cccc C E EEE EE C CC F F CCC BB

BRIDCEZ.. HH H HH 00 K KK KKK
BRIffiEl.. MMMMMH H H HH 9 1x1 1 N NN 00 1 P P I11 cc
CHIRALITY ---+--++-+ +---t-++-- --++----+- +--+++++-- +---+-+-+- +-+-+--++- +---+---++ +++++-+--
BEND.. s s ss s s ss ss sss ss sss ss ssssss
5-TURN.. >5555<
....
4-TURN.. . >444 < >>4 >x<4<<
3-TURN.. , >>3<< >33x33< >33< >33 x33x33<
SUMMARY.. EEEEEEEEE E E E E E GGG EEEEEEEES TT BT E EEETTEE EEEESSBTTT B EEE HH HHHHHTT EE
EXPOSURE. 1 5 8 * 1 5 0 6 1 9 * 28 2 * 6 3 * 9 1 7 0 ' 3 0 1 7 8 7 1 1 1 8 * 0 0 2 0 0 0 0 0 2 5 3 3 0 0 0 0 1 1 2 5 9 6 6 1 * * 2 3 5 0 3 0 0 3 0 5 9029655093 '
1 0 1 SEQUENCE. GLRSGSVTGL NATVNYGSSG IVYGMIQTNV CAQPGDSGGS LFAGSTALGL TSGGSGNCRT GGT'ITYQPVT EALSAYGATV L
1111 NNNN NWWW W o rrrrr x xx 1 1 1 I 1111 I I 111111 8 8 4' "K3MIYE
NNNNN muww TI 11 x nx rrrrr * *zaxaIw
.a 33 33 3 3333 3 3333 33 333333 88 Y * * * . L33HS
s ~ I . . . . . . . . . . . . . . . . . .3333
L33333 . . . . .3333
. . . . .3. . . . . . . . {YaOMSS
33x3
SnS :SY3UWYd D I d ) [ 3 S V N I Z & O M d 3 N I U 3 S : 3 S \ n O W A H 1 3SYLSM3-1XSOL LS31 (EE
OYYVO A N I 1 3 X D A A I S ( I D l P L J L N ( I 1 S S U A O J N J M N d H Y S 1 1 1 Y Y YDYAHdSYWS L D N A V 3 A X N 3 dlLSO1ShM ' 3 3 N W l O 3 S KBZ
r00P6 Bt010rKP65 6 r E P . L E P r Z KESS06828I *6ECEZ0000 000K000001 006r9K9.rE EE008K9EQB ' 3 M n S O d X 3
HHHH H E JLHHH H s ESLLH HHHHHHHH s LJSHHHHHHH HHHHHHHHHH H 3 3 3 3 3 ~~ ~3 3 3 3 3 s3~ **mvwwns
>EE<>E E < >>E< XCEXEC< > EE<>EEXEE< >EEXEE<>E E< * * 'NMIIL-E
<<
>>>I< > > P I << >> > > P > X X > X xxxxx<xx<r < <
E
n sss s sssss s s
P>XX><<<<
ssss ssssssss s ssssssssss ssssssssss s
>PV
ss s
P<
ss
* ' 'NWJ-P
* 'NYnL-S
* * . * * (IN38
+++ +---+---++ +---+--+++ ++++++++-- ++++++++++ ++++++++++ +-+---+-+- +---+-+-++ ALIlWIH3
4 I 11111 11111 3 "13MIM8
I "23!XIME
\I Y aaaaa aaaaa v '*** JaaHs
A V M a 7 3 d M S S d S V M O N S S a A Y M Y I A S d A x M A 3 A L S S S X S 3 3 N D Y Y Y M A A 3 S Y A Q X MYYX'IYYSD S d D D l S W N I A a W N N Y I Y M 3 1 D N I I M S A O D S ' 3 3 N B n O 3 S T01
5 000f096000 09rlSwSBLS 0 0 0 0 0 1 0 E ~ Z S009KKZE+* 9r8KrLKBT0 BQBKE+6EBr 900S80P6SZ 8rTSE00000 91rLLC0990 06ElSS9r9C
333 LL
>EE<
SLL E LL 333333SJL.5 LLLE
>EE< > E E < m x Ec<
SL LS
x E<
S 33 3 3 3 L H H H H H H H H H H H H H
>>E< <
SE 3333 S LLHHHHHH H H H H H H H 33
>EEX>E<< >EE<
'3MnSOdX3
"AUYWWIIS
"'NUnJ-E
x >PCt< >>>>xx xxxxx<<<<
>SSSS<
>>>>XXX XXXX<<<< >
>ssss<
"'NMnJ-C
'*'NMIIL-S
53a -+--+++-+-
ss sss
-++---+-+-
ss
-+-----++-
ssss ssss ss ss
++++--++-+ --+--+----
s ssssss ssssssss
+---+-++++
s
++++++++-- -+--++-+--
s s sssssss sssssss
+---++++++ +++++++-+-
.....aNae
ALI1YYIH3
< 333 3 3 aaa x P PPP n ww rr
-*'..
*-I~MIME
'zma1~8
z q
Y W Y
3333
VVYWY 3
aa a
YY Y W 3
PPPP
VYYY BE L33HS
3 Y a D 7 A X A Y A 1 Y S S d Y A D l A 3 I S N N ' l Y Y A J 3 Y A H J 3 H S N a Q O d N d J 3 S d A WSYDDYAX1a d H S S Q I D S C I I A Y A X A N S D W D O S H l Y d Q X I O S A D A d A S O Y '33N3003S 1
Pr60V0000P 0 Z Z E Z 0 0 0 Z l 1966rK0101 0 0 0 0 0 0 S E S 6 266KS.SrrK P E E Z Z S E I Z ~ L069E00000 0009T.L0ZB SB.EBZP090 PL008C6LLr '3MnSOdX3
JLL33 3333 33 JLSS SSSSS HHH HHHHHHHSSS SS JL 3333 L L LL 833 3333 JJ S LLLHHHHHJH H H H H H * 'AMVWwnS
>EE< >EE< > >E<< >EE< >E E X E C < >EE< >EE< > EEXEE< ' ' 'NMnL-C
PPP< >>>P < X X > P < < < > > > P < < X > >><<<< "'NMIIJ-P
ss
--+--++-+- s ss
---++++--- sssss
--+-+--+-+ ss ++++++++-+
ssssssssss +-++-+-++-
ss s ss
ss +---+----+ s +-++-----+ss ---+-+++-+
> ssss< >ss ss<
ss s +-+++++++-
ssssssss s +++++----
sssss .....
'*'NMnL-S
A L I I Y aMNI 3HE3
rr w e e ee 3535 we PSPP "K3XIME
5553
88 YYVY YY
~EsK"........"".*'".......
YVYQ YY
9 99q
YWY ....
"Z3MIUE
LaaHs
(SN313Vd3Il61101AWV Sn1113YE A l E V 8 0 M d ) [ 3 S Q N I 3 L O k ! d 3 N I U 3 S :3SV7OtlCIAH1 aNdE N I S I l I L E f l S JBSK (ZE
SHEET.. .. E E BBBB B F F D BBBB 88 BBBB A BBBBBB 88
BRIDGE2.. ODD D DDDD FFFF GGGGGG
BRIDGE1.. P P CCC Q Q 0 88 EE EE A CCC GG
CHIRALITY ----+-+++- ------++-- --++-+---+ -+--+-++-- --+-----+- ----+++++- ++---++--+ +--+-++-++ +---+++++- ----+--+-+
BEND.. ... s sss ss ss s ssss ss ssssss sss sss s s sss s ss ss ss
5-TURN.. , > 5555<
4-TURN.. . >>44<<
3-TURN.. , >33< >33< >33< >33< >33x 3 3 < > > 3 < < > 33 < >33x33< >33<
SURUARY.. S BTTB TT TT EEEE ES BSSTT B SB EEEE EE HHHHTS TTTTGGGS T TEEEE S S S SB TT TT EEEEEETTEE
EXPOSURE. ' 70 9 66 8 9 09 6 1 6 5 1 * 6 5 4 * 4 7 6 ' 2 5 8 6 0 0 0 0 0 2 6 * 5 * 4 * 7 1 * 2 1 3 3 0 8 0 2125.76845 * 7 6 3 2 * 5 0 7 9 3 2 2 0 0 2 1 7 2 9 9 0 0 1 * 1 0 3 0 0 001064'7*'
1 0 1 SEQUENCE. QSVTLNSYVQ LGVLPRAGT I LANNS PbYIT GWGLTRTNGQ LAQTLQQAYL PTVDYAIC S S SSYWGSTVKN SMVCAGGOGV RSGd QGDSGC PLHb LVNGQY
SHEET.. .. B B BBB B G G H H BBBBB

BRIDGE2.. HHH H HHHH
BRIDGE1.. GG GG R R S S FFFF
CHIRALITY -++--+---- +--++-++-- -----+++++ ++++++++
BEND.. ss ss ss sssss ssssssss
5-TURN..
....
4-TURN.. >> >>xxx<<<<
3-TURN.. 33< > 3 3 <
> >>3<< >>3<<
..
SUUUARY.. EEEEEEEE B TTBSSBTTB EEEEEGGGSH HHHHHHHHT 0
EXPOSURE. 1 0 1 0 0 1 0 3 2 1 ** 1 0 5 4 8 * 5 0 0 0 0 0 3 0 0 5 1 2 84R7.12899 c3
2 0 1 SEQUENCE. AVHGVTSFVS RLGdNVTRKP TWTRVSAYI SWINNVIASN f3
34) 2ACT ACTINIDIN [HYDROLASE: SULFHYDRYL PROTEINASE] (KIWIFRUIT: ACTINIDIA CHINENSIS]. ............................... .2ACT z
SHEET.. .. AA B C D D E C
BRIDGE2..
BRIDGEI.. AA I J K K L J
CHIRALITY -+++-+++- +-++++++++ ++++++++++ +-+-+---++ ++++++++-- ++-++-+--+
++-------- +++++++++- -----+++-- +-+-+----+
BEND..... S SSSS S ss sssss ssssssssss sss s ssssss s s sss s ssssssssss s ssss ss s
5-TURN.. > 5 5 5 5< > 5 5 55< >5555< > 5 5 5 5<
4-TURN.. >>>>xxx xxxxxxxxx< <<< > > >>x<<<< >> >>xxxxx<<<< >444< >>
..
3-TURN.. . >>><< < > 3 3< > 3 3 < > 3 3 < > > 3 < < >> 3<<
SUMMARY.. S EEGGGG T B T TS H H H H H H H H H H H H H H H H HHS 8 H HHHHHH BT TB GGG H H H H H H H H H H H T B BTTTS SS H
EXPOSURE. * 6* * 2 24* * 5 4822.23515 * 1 3 0 2 0 0 1 0 0 0 1 0 0 0 0 1 1 6 7 6 7 4 6 7 5 4 0 0 0 0 0 0 0 2 2 1 * 6 * *0*03*23*1 33006284.2 4 0 0 0 2 3 9 6 1 7 573973'489
1 SEQUENCE. LPSYVDWRSA GAWDIKSQG EaGGCWAFSA IATVEGINKI TSGSLISLSE Q E L I BG RT Q NTRGaDGGYI TDGFQFIIND GGINTEENYP YTAClDGDbDV
SHEET.. .. E AAAA AAAAA AA AAAAA AAA AA AAAAAA A B A AAAAA

BRI.DGE2.. D FF FFF FF GGGG G GGGGG
BRIXEI.. L BBBB ccccc ee CCCCC AA FFFFFF F I H H ee
CHIRALITY ++++-++--- -------++- +++++++++- ---+-+-+++ -++++++-+- -+--+--+-+ +-+--+--+- ---+-+---- --+--++--- -+-----++-
BEND.. ssss ss ssssssssss s ssssss ss ss sss ss sssss ss
5-TURN..
....
4-TURN.. >4<<< > >>>xxxx<<<< >>>4<<< >44 4<
3-TURN.. >33< >33< >33< >33< >33< > 33<
.. 3
SUMUARY.. HHHH B EEEE TT HHHHHHHHHH S EEEEE SHHHHH S S EE SS EEEEEEEEE EETTEEEEEE E SB TTSTB TTEEEEE M
EXPOSURE. 7 4 4* 6 **0 6 1 8559'18.67 1*2014103* 2000010215 3.489'2793 4292.43984 9 1 1 0 1 0 0 B 0 0 7.87652080 111766.226 *020404187
101 SEQUENCE. ALQDQKYVTI DTYENVPYNN EWALQTAVTY QPVSVALMA GDAFKQYASG IFTGRGTAV DHAIVIVGYG TEGGVDYWIV KNSWDTWGE EGYURILRNV N
SUMMARY. .......HIALPHA-HELIX.. ..EmBETA-STRAND.. ..B-BETA-BRIDGE.. ..G=3-HELIX.. ..I-5-HELIX.. ..T=3-, 4-, OR 5-TURN.. .. SIBEND.. .. E
w
SHEET.. .. AAAA
BRIDGE2.. D
BRIDGE1.. BBBB
CHIRALITY +-----++++ ++---+
BEND..... SS SSSSSS S
5-TURN.. .
4-TURN..
3-TURN... >33X>3X<3<
SUMMARY.. T T GGGTTS S EEEE
EXPOSURE. 5521 100004 8005034*
201 SEQUENCE. GGAGTCGIAT MPSYPVKY
35) EPAP PAPAIN (HYDROLASE: SULFHYDRYL PROTEINASE] (PAPAYA FRUIT LATEX: CARICA PAPAYA]. ............................ .BPAP
SHEET.. AA B C B
BRIDGE?.
...
BRIDGEl.. AA H I H
CHIRALITY -+-+-+++- ++-------- +-++++++++ ++++++++++ +-+-----++ +++++++++- -++++--+++ ++++++---- --+++--+-+ -+--+++++-
BEND..... S SSSS S ss SSSSSS ssssssssss ss s SSSSSS sss sss sss ssssssss ssss 5 s ssss
5-TURN... > 5 5 5 5< >555 5<
4-TURN.. > > > > x x x xxxxxxxxx< <<< >> > > x < < < < >>>> xxxx<<<< >>44<
3-TURN.. >33 < >33< >33< >33< >33< >33
..
SUMMARY.. S EESTTT T SS HHHHHH HHHHHHHHHH HH B H HHHHHH TTT TSTT HHH HHHHHHHS B BSSSS S S HHHH
EXPOSURE. *7**134*** 3022932714 *030210100 0100000155 *85*636000 0000031**0 '04'3281'8 005202**00 194'606491 86**150*'9
1 SEQUENCE. IPEYVDWRQK GAVTPVKNQS SaGSCWAFSA W T I E G I I K I RTGNLNQYSE O E L L W D R R S YGaNGGYRJS ALQLVAQYGI HYRNTYPYEG VQRYbRSREK
SHEET.. .. C A AAA A AAAA AA AA AAA AA A AAAA AAAAA
BRIDGE2.. D FF F G GGGG GGGGG
BRIDGEl.. I B BBB c cccc ee CC CCC AA F FF ee
CHIRALITY +--++----- ----++-+++ ++++++---- +-+-+++-++ ++++-+--+- -+--+-++-+ --+----++- -----+--++ ----+----- ++-+-+--+-
BEND..... S S S ss sss ssssssss s ss sss sss s s ss ss ss sssss ss ss ss
5-TURN.. .
4-TURN... < >>>> x x x x < < < < > 444< >444<
)-TURN... < >33< > 33< >>3
SUMMARY.. S SB S E EEE S S HHH HHHHHHHS E EEEE S SS TTT SSSEE S S EE EEEEEE SSE EEEE SS SS STTTSEEEEE SS S S G G
EXPOSURE. 3'951'8925 '*1*5*7552 12'1028210 670202871'7 0**2'3372' 2'42'*5921 0000010565 0102016398 216'028807 45'777'018
101 SEQUENCE, GPYAAKTDGV RQVQPYNQSA LLYSIANQPV SVVLQAAGKD FQLYRGGIFV GPcGNKVDHA VAAVGYGPNY I LIKNSWGTG WGENGYIRIK RGTGNSYGVC
SHEET.. .. AAAA
BRIDGE2.. D
BRIDGEl.. BBBB
CHIRALITY +++-+-+---
BEND..... S SS
5-TURN..
4-TURN..
..
3-TURN... X<3<
SUMMARY.. GTTS EEEE
EXPDSURE. 0013412403 '5
201 SEQUENCE. GLYTSSFYPV KN
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....~=3-HELIX....I=5-HELIX....T~3-,4-, OR 5-TURN....S=BEND....
361 lFAB LAMBDA IMMUNOGLOBULIN FAB (NEW1 lHUMAN).......................................................................lFAB
SHEET.. .. A BB BB AA AAA BBBBBB BB AAAA AA AAAAAA BB BBBBBBB B BBBBB BBB
BRIDGE2.. BB EBB FF cccccc GG GGGGGG G GGGGG GG
BRIDGE1.. A dd dd A EEEEEE FF CCCC CC BBBBB E EEEEE ddd
CHIRALITY -+-+--+-- +--++----- +-+--+-+++ -+------+- -++------- +-+-+++--- +--+ ---- +- ---- ++----
BEND..,.. S S ss ss
sss sssss ss ssss
___ss+++---- +-+-++++--
s ss s sss
5-TURN.. >5555<
4-TURN..
..
3-TURN.. . >33< >33x33 c >33< >33< >33<
SUMMARY.. S B S E E E E TTS EE EEE TTTTT SS EEEEEE SSSS E E SS SSEEEE EETTEEEEEE S STT EE EEEEEEETTE E E E E E E E E E E
EXPOSURE. 9 3 * 1 * 2 3 * 7 2 7 0 2 7 7 8 ' 1 7 8 5 0 5 2 5 ' 6 0 8 3 5 6 7 6 1 5 0 0 5 1 886908'43. 6*+5**2676 * 8 6 5 4 0 2 0 1 0 538'4'1211 0101004'41 1010420'84
1 SEQUENCE. XSVLTQPPSV SGAPGQRVTI SaTGSSSNIG AGNHVKWYQQ LPCTAPKLLI FHNNARFSVS KSGSSATLAI TGLQAEDEAD YYaQSYDRSL RVFGGGTKLT
SHEET.... B c cc cccc ccc DDDDD D CCC CC CCC CCCCC DDDD DD DDDD

BRIDGE2.. 1111 I11 M KK JJJ NNNN NN
BRIDGE1.. d H HH HHH LLLLL M JJJ KK I1 11111 LLL LL NNNN
CHIRALITY -++------- -------+++ ++-+------ -+++-+-++- -+----++-- ++++------ -+-+-+--+- ----+---++ ----++---- -+--+-----
BEND..... S sss ssss sss sss ss sss s s s s sss
5-TURN..
4-TURN.. >4>4 x4<4<
..
3-TURN.. . >3 ><3< >33< >33<
SUMMARY.. ES E EE TTT TTTT EEEE E E E SSS EEEEE SSSB TTEEE E E STT E E E EEEEE S S S S EEEE EESSS EEEE
EXPOSURE. 17'39.3616 0221451'78 7 * 8 * 7 1 1 1 0 0 0 0 2 5 0 5 1 3 7 3 '331618'79 4 * * 1 2 5 6 3 * 4 5 5 7 8 ' 3 4 4 1 0 0 0 1 0 6 5 7 7 9 f * * 6 6 * 2 4 1 0 4 041'8485'6
1 0 1 SEQUENCE. VLRQPKAAPS VTLFPPSSEE LQANKATLVb LISDFYFGAV TVAWKADSSP VKAGVETTTP SKQSNNKYAA SSYLSLTPEQ WKSHKSYSbQ VTHEGSTVEK
SHEET..,. DD EEEEE F F EEEE EEEE GGGGGGG GG GGG G GGG EEEE EEEE E G v1

BRIDGE2.. PPPP P TTTTTTT uuu QQQ Q V M
BRIDGE1.. NN 00000 r r 0 0000 ssssss ss sss s uuu QQQQ PPPP P
CHIRALITY ++-+++ +-+--+--++ --++---+-- ---++--+++ ----+----+ -+-+------ -+-++----+ ++++++---- --+-++--++ -+-+-++++-
BEND..... SS s sss sss sss s s sss s sssss ssss s sss s
5-TURN..
4-TURN.. >444 <
..
3-TURN.. . >33< > 3 3c >33< >33< >>3<<
SUMMARY., E E SS E E E E E S E E TTS E E E E EEEESS TTT EEEEEEE T T EEEEEE ETTS EEE S SSTTSEEEE SSSS EEEE E S GGG E
EXPOSURE. 8347*'4*0* 7'2.372714 2*58*40403 041562934. 250000224+ 8'31610810 3 4 ' 5 4 7 5 4 1 7 91*'4374B5 6 * * * 6 7 0 2 0 * 0 4 6 1 6 8 8 0 3 0
2 0 1 SEQUENCE. TVAPTECSI X VQLEQSGFGL VRPSWLSLT d T V S G S V S N DYYTWVRQPP GRGLEWIGYV FYHGTSDTDT PLRSRVTMLV NTSKNQFSLR LSSVTAADTA
SHEET.... GGGGGGG GG G GGFF H I J JJJJJI J H KKKK J JJ JJ J J J J J

BRIDGE2.. W W zzzzz 2 BB A
BRIDGEl.. TTTTTTT w vwrr w x Y Y x w cccc A BB Z 22227,
CHIRALITY ---+--+--+ ---+------ ---+-+---- --------++ --++-+-++- ----+++-+- ++-------+ +++-++---- ----+-+--- ---------+
BEND.. ss s ss s ss ssss s s s ssss s ss sss sss
5-TURN..
....
4-TURN.. . ,... .
3-TURN.. . >33< >33< >33< >
SUMMARY.. EEEEEEE S S S EEEEE EEEE SS B B B S SS STTS EEEEEEEEBS S EEEETTT S TT B EE SSS EE EEEEE SSS
EXPOSURE. 3 0 1 0 0 3 1 7 * 3 3 3 1 8 5 2 1 9 1 3 40285'6'59 2 2 5 2 3 3 0 1 2 3 2 ' 4 3 8 9 6 3 1 2 1 0 0 0 0 0 3 0 3 0 8 4 2 8 2 4 1 3 * 6 85*'33*623 30'37.5648 1002093888
3 0 1 SEQUENCE. WYdARDLIA GCIDWGQSS LVTVSSASTK GPSVFPLAPS SKSTSGGTAA LGeLVKDYFP EPVTVSWNSG ALTSGVHTFP AVLQSSGLYS LSSVVTVPSS
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....G=3-HELIX....I=5-HELIX....T=3 -,4-, OR 5-TURN....S=BEND....

to
TABLE AIII (continued) 03
+
03
SHEET.. .. KKK KKK KKK KKK
BRIDGEZ.. DDD DDD
BRIDGEl.. C C CC DDD DDD
CHIRALITY ++++------ -+-++-+--- ---+---
BEND., SSS sss S
5-TURN.. >5555<
....
4-TURN,.
3-TURN.. 33< >>3<<
..
SUMMARY.. T T S S S EEE EEEGGGTEEE E E E S
EXPOSURE. * 3 9 * * 8 2 4 0 3 0 6 0 * 2 3 * 3 * 4 '1391.688.
4 0 1 SEQUENCE. S L G T Q T Y I e N VNHKPSNTKV D K K V E P K S c
37) l R E I BENCE-JONES IMMUNOGLOBULIN VARIABLE PORTION ( R E 1 1 (HUMAN). .................................................... 1REI

SHEET.... AAAA B 888 AA AAAAA BBBBBB 88 B B BB AAAAAA BBBBBB
A AAAAA B
BRIDGEZ.. BB BBBB FFF GG c ccccc HH I
BRIDGE1.. AAAA d ddd AAAA EEEEEE FF F GG CCCCCC B BBBBB EEEEEE I
CHIRALITY -----+-++ -+--++---- -----+-+-- ++-------- +----++-+- ++----+--+ ++--+---++ -----+---+ +++------- ++-+------
BEND.. s s ss ss s s ss ss ss ss s s sss ss s s s ssss
5-TURN..
....
4-TURN.. >4 44<
3-TURN.. >33< >3 3< >3 3< >33<>3 31 >33< >> 3<<
..
SUMMARY.. E E E E S E EEE T T E E EEEEESS T T EEEEEE T T S E E E E E T T T E E T T T T E E E E E E T T E EEEEESS G GG S E E E E E E SSSS B
EXPOSURE. *0*1606467 3814857115 040918*908 870008325' 8'31.00854 078638815. 5061739269 0403073068 *061301010 474834328'
1 SEQUENCE. D I Q M T Q S P S S LSASVGDRVT ITaQASQDII KYLNWYQQTP C K A P K L L I Y E ASNLOAGVPS R F S G S G S G T D Y T F T I S S L Q P E D I A T Y Y a Q Q YQSLPYTFGQ
SHEET.. .. BBBBB
BRIDGE2.. HH
BRIDGEl.. dddd
CHIRALITY
BEND..
5-TURN..
.... -----
4-TURN..
3-TURN..
..
SUMMARY.. EEEEE
EXPOSURE. 0090*5*
1 0 1 SEQUENCE. GTKLQIT
38) 3PGM PHOSPHOCLYCERATE MUTASE (DE-PHOSPHO) [ISWERASE] (YEAST: SACCHARWYCES C E R E V I S I A E I ........................... .3PGM
SHEET.... AA B AAAAA AAA
BRIDGE2.. BB ddd
BRIDGE1.. a f ccc dd d
CHIRALITY +--+----- -+++++-+++ -+-+----++ ++++++++++ ++++-+---+ -----+-+++ ++++++++++ -++++----+ -+++------ ++++--++++
BEND.. sssssss ss ss ssssssssss ssssss s s sss ssssssssss ss s sss s s SSSS
5-TURN.. > 5555< > >555<< > 5 5 55< >
....
4-TURN.. >>44<< >>> >xxxxxxxxx xx<<<< >>>> XXXXXXKX<< << >>>
3-TURN.. >33< >33<
..
SUMMARY.. EE B SSHHHHS TT HH HHHHHHHHHH HHHHHS S E E E E E S HHH HHHHHHHHHH HT S EE ESSS S S SSHH
EXPOSURE. 5400014104 07525'8552 1 1 3 4 3 9 1 2 5 * 0'*601900* 1181.36986 1110062521 3 5 0 0 8 2 1 2 * * 1'5**4957* 1371140041 8321845391
1 SEQUENCE. PRLVLVRHGQ SEWNERNLFT G W W V K L S A K GQQEAARAGE LLKEKGVNVL W Y T S K L S R A I Q T A N I A L E R ADRLWIPVNR SWRLNERHYG DLWKDKAQT
SHEET.. .. AAA
BRIffiE2.. ccc
BRIDGE1.. a
CHIRALITY +++++-++++ +++--++t-- ----++-++- +-+-+++++- -+++--+--- ++t+++++++ ++++++++++ +-+---+-+- ++++++++++ -+--++++++
BEND., , ssss sssss sssssss s sssss sssssss ss s ss ssssssssss sssssssss ss s ssssssssss ss ssssss
5-TURN.. 5555< > 5 5 5 5< >>555<<
...
4-TURN.. 4 < < < > > > 4 < << > 44>x>4xxx> x<<<x>44<< >>>>xxx<<<<
)-TURN.. >33< >33< >3><3< >>3<< >>3<< >3 3<
..
SSSSS SSTTTTS _.
-..... ~ SS
S S S ~. TTTHHHHHHH HHHHTHHHH SS EEE T THHHHHHHHH SS SSSSSS
SUMMARY.. HHHT SHHHH HSTTSSS S
EXPOSURE. ~ * + * i * * * s * 1 6 6 9 3 * + 6 4 a 3739;;;;93 3*39*71**2 *9*413*211 2 4 8 1 5 9 2 2 6 4 33**412*51 8 9 3 0 8 1 0 0 2 1 1 1 0 3 0 1 2 4 ' 1 9537.7625'
101 SEQUENCE. LKWGEEWN TYRRSFDVPP P P I 3 A S S P F S QWCDEKYKYV DPNVLPETES LALVIDRLLP YWQDVIAKLV GKTSMIAAHG NSLRGLVKHL EGlSDADIAK
SHEET.. .. B A A A
z4
BRIDGE2.. E
BRIDGE*. . f 88 E
CHIRALITY +---++---- -+--+-+-++ ----- t t +
BEND.. sss ss s s s
5-TURN..
....
(-TURN.. . >444<
3-TURN.. . >33< >33<
SUMMARY.. BSS EE TTT S B S T T
EXPOSURE. **24301011 1416**4*47 *969725**6
2 0 1 SEQUENCE. LN I PPGT I LV F ELDENLKPS KPS Y Y L DPEA
39) l T I M TRIOSE PHOSPHATE ISOMERASE [D-GLYCERALDEHYDE-3-PHOSPHATE-KETOL-ISOMASE] (CHICKEN BREAST MUSCLE: CALLUS GALLUS) l T I M
SHEET.. .. AAAAA B AAAA A AAA M A C AA Ah
BRIDGE2.. bbbb ccc , ee
BRIDGE1.. aaaaa I aaaa a c c c ddd J dd d 0
CHIRALITY --------- --++--++++ +++++++++- +++-t----- +--+++++++ +++--++--+ --+---+--+ -+-++---++ ++++-+-+-- +++-++++++
BEND.. s ssss sssssssss ss sssssss ssss sss s ssss s ss ss ssssss ssssss 0
5-TURN.. >5555< >555
....
4-TURN. >>>>X xxxxxx<<<< > 4 > > x > x x <<<< >>> >x<<<< >>>>X<<
3-TURN.. >33< >33< >33 < >33<
...
SUMMARY. . EEEEE B HHHH HHHHHHHHH
.................. S
.S. EEEE
~ _ _ _E TTHHHHH HHHS TTEEE EEE S S S S BS SS H H HHHHHT EE EE H H H H H H
EXPOSURE. * 9 9 9 3 0 0 0 0 1 13042'8'41 1*20*71362 * 9 6 8 * 3 7 1 1 0 0 0 0 2 1 0 0 1 3 0 5 * 8 1 6 9 9 0 2 0 0 1 1 2 0 1 6 5 7 * 2 5 5 0 1 2 1 0 0 4 01'7231630 10001213'6
1 SEQUENCE. APRKFFVGGN WKMNGKRKSL GELIHTLDGA KLSADTEW C GAPS I YLDF A RQKLDAKIGV AAQNC YKVPK GAFTGE IS PA M I KD I GAAWV ILGHSERRHV
SHEET.. .. AAAAAAA AA AAAAA

BRIDGE2.. fffffff 4 499
BRIDGE1.. ee ff fffff
CHIRALITY -+--++++++ +++++++-+- ----+----+ ++++-+++++ ++++++++++ ++---+++-- ----++++-+ -+----++++ ++++++++++ ++++--++++
BEND..... S SSSSSS SSSSSSSSS s ssssss sss ssssssssss ss ss ssss sss ssss ssssssssss sssss ssss
5-TURN... 5< >5555< >5555<
(-TURN... << > > > > X X X X X X X < < < < >> >><<<<>>>> xxxxxxxxx< <<< > > > > xxxxxxxxxxx x x < < < x > > > <
3-TURN.. . >33< >3 3< >33< >33< >>3<<
SUMMARY.. H H H H H H H HHHHHHHTT EEEEEEE H HHHHHTTHHH H H H H H H H H H H H H TTEE EEEEEGGGSS SSS HHHH H H H H H H H H H H HHHHH H H H H
EXPOSURE. 55246.3807 0 0 3 3 0 1 9 6 6 1 1 0 1 0 0 0 1 0 9 4 * 9 5 * 8 4 6 2 9 * 2 0 4 * 2 0 * 2 0 2 '41'728618 0 0 0 1 1 1 3 2 8 9 6 5 * * 2 4 3 + 7 1 3 9 1 0 9 ' 0 3 3 4 0'9*45*720
1 0 1 SEQUENCE. FGESDELIGQ KVAHALAEGL GVIACIGEKL OEREAGITEK VVFQETKAIA DNVKDWSKW LAYEPVWAIG TGKTATPQQA QEVHEKLRGW LKTHVSDAVA
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....G~3-HELIX....I=5-HELIX....T=3-~4-, OR 5-TURN....S=BEND....
SHEET.. .. AAAA AAAA
BRIDGEZ.. h h
BRIDGE1.. qgqq bbbb
CHIRALITY tt-----t-- t-tttttttt t-ttt----t ttttt-+ttt ttttt
BEND..... SSS S SSSSSSSS SSSS ssssssssss ssss
5-TURN..
4-TURN.. <<< > 4 > > x > < < << > 4 4 4 < >>>> <<<<
..
3-TURN.. . > 3 3x33< >>><<x33< >33<
SUMMARY.. HHSEEEE S TTHHHHHH TSTT EEEE SGGGGSTHHH HHHT
EXPOSURE. 8 8 0 2 0 0 1 1 2 8 045451'701 62'5100028 26207.7502 *0151**
2 0 1 SEQUENCE. VQSRIIYGGS VTGGNCKELA SQHDMGFLV GGASLKPEFV D I I N A K H
40) 3CNA CONCANAvALIN A [LECTIN, AGGLUTININ] (JACK BEAN: CANAVALIA ENSIFORMIS] . .... ,... . ... ...CCA .... ,.3CNA
....AAAAAA
B
SHEET.... AAAAAAA AAAAAA AAA BBBB BBBBB
..BBBBBB
........, , ...BBBBBB
BRIDGEZ.. BBBBBB ccc H H HHH I 11111 EEEEE x
BRIDGEl.. AAAAAA BBBBBB ccc GGGG GGGGG HHHHH 111111 OOD DD 3.
CHIRALITY --+-+----+ +-ttt+-t-- t-+-+----+ -+--+----- ---++----- -tt--t+-+- ++--+--++- ---t---t-- tttt--tt-- t-t---ttt- w
BEND., s sss ss ss sss ss ss sss sss ssss ss sss cn
5-TURN.. >5555<
....
4-TURN.. >444< >444< 2
3-TURN.. >33< >33< >33<
..
SUMMARY.. EEEEEEE S TTTT S S EEEEEES SSS SSEEE TT EEEE EEEEETTT E E E E E E E TTS EEEEEE TTTS SEEE EEEEEE S S S 5,
EXPOSURE. * 5 4 1 0 0 1 0 0 0 6 5 4 1 9 ' 2 5 1 3 9 8 4 0 1 0 0 0 2 ' 21'29'62'1 * 5 7 7 3 * 8 0 5 0 807174'*9* 12261518.4 '729138'27 2**4169*04 10000002*8
1 SEQUENCE. ADTIVAVELD TYPNTDIGDP SYPHICIDIK SVRSKKTAKW NMQDGKXTA HIIYNSVDKA LSAWSYPNA DATSVSYDVD LNDVLPEWVR VGLSASTGLY
SHEET.. . BB BB BBBBB BBBBBBB A AAAA BB BB A AAAAA CC BB BBBBBBBB

8
BRIDGE2.. K MM MMMMM NN FFFFF M M MMMMM K
cn
BRIDGE1.. JJ LL LLLLL LLLLLLL F FFFF NN JJ E EEEE 00 G GGGGGGGG
5,
CHIRALITY t--t--t-tt tt--ttt-t- t--t-tt--t t---t--tt- -t--tt-tt- -t---t-t-- t-t---tt-- t-t--t---t tt-ttttttt --tt----tt
BEND.. S sss s s ss ss s sss s sss ss ss ss s
5-TURN..
.. ..
4-TIIRN..
. .. . . . .. . >444 <
3-TURN.. . >33< >33<
SUMMARY.. EES E E EEEEE TTT EEEEEEE S S SSE EEEES E E S SSSEE S SSS S S E EEEEESS E E TT S E E E E E E E E E E
EXPOSURE. 8 0 1 0 0 0 5 3 1 3 1 2 1 9 0 7 2 2 . 6 **6975'3*4 8*0R**3'61 4 7 7 4 4 1 8 1 4 7 * 1 2 0 3 0 0 * 5 6 * * 4 7 2 5 1 8 0 2 0 1 0 6 3 . 4 6 2 3 5 6 4 * 6 4 7 3 1 2 3 * 0 3 1 1 0 6 0 *
1 0 1 SEQUENCE. KETNTILSWS FTSKLKSNST HQTDALHFMF NQFSKDQKDL ILOGDATTGT DGNLELTRVS SNGSPEGSSV GRALFYAPW IWESSAATVS FEATFAFLIK
SHEET.. .. A AAAAA
BRIDGE?. . DDD
BRIDGE1.. A AAAAA
CHIRALITY -+-+-----+ -+-+--++-- --+++-++-- tt--t
BEND.. ssss ss ss sss sss s
5-TURN..
....
4-TURN.. >4 44<
3-TURN..
..
SUMMARY.. SSSS E EEEEE S S SS S S S T TTS S
EXPOSURE. 1*5**10100 0 0 0 2 0 2 8 * 2 9 41'4858930 0 1 0 7 9 6 7
2 0 1 SEQUENCE. SPDS HPADGI AFF I S N I D S S I PSGSTCRLL GLF PDAN
SUMMARY........H~ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGEI...G=~-HELIX....I=~-HELIX....T~~-,~-, OR 5-TURN....SeBEND....
41) lCAC CARBONIC ANHYDRASE FORM C [CARBON-OXYGEN LYASE, CARBONATE DEHYDRATASE] [HUMAN ERYTHRDCYTESl...................lCAC
SHEET., .. AA BBBB BBBB BBBB BBBB BBB BB BBBB
BRIDGEZ.. EEE FFF GG H H H HH HHHH
BRIDGEl.. aa cccc DDD E EE cccc GG F F F
CHIRALITY +-+-+++-+ ++++-+++++ +-++-+---+ -+++--++++ ------++++ -----+-+-+ +-------++ -+++-++-++ -+----+--+ --+--+-+++
BEND..... SSSSSSS SS SSS SS S SS SS SSSS S S ss s s s ssss ss ss ssss
5-TURN.. .
4-TURN.. , >444<
3-TURN., . > 3 3 < > > 3 < x 3 3 < > > > < << >33 < >33 < >33 < >33<
SUMMARY.. SSTTSSG GG TTS GGG G SS SS EE TTTS TT S E E E E TT EEEE S S EEEE S SSSSEEEETT SS EEEEEE EEEE SSTT
EXPOSURE. * 5 1 4 3 * * 4 0 3 * 5 1 * * * 7 9 7 1 * 3 ' * 0 0 0 1 5 1 85*917'3** 4.734561'' 2666.03171 5 0 0 3 0 5 0 7 4 9 '68111'222 2.53051431 2 1 1 1 0 4 * 8 6 5
1 SEQUENCE. HWGYGKHDGP EWHKDFPIA KGERQSPWI DTHTAKYDPS LKPLSVSYDQ ATSLRILNDG HAFNVEFDDS EDKAVLKGGP LDGTYRLIQF HFHWGSLDGE
SHEET.. , . AA A BBBBBBBB B BBBB BBBBBBB BB B BB BB

BRIDGE2.. 0 11111111 jjjj j kkkk MM
BRIDGEl., aa B HHHHHHHH H 1111 1111 DD D L NN
CHIRALITY +++----+-- -------+-- -++---++++ ++-+++---- -----+---- ++++++++++ ++++-++--- -+++--++++ --+-+---+- +---+-+-+-
BEND..... SS SSS S sssssssss ssssss s s sssssssss ss ssss sssss ssss
5-TURN..
4-TURN.. >>44< < > >4>x<4<<
..
3-TURN.. . >33< >>3<< >33x 33x33< > 33x>3<x>>< x<3< >3><3 <
SUMMARY.. SSEETTB SEEEEEEEE EGGGSSHHHH TTSTTSEEEE EEEEEEES H H H H H H H G G G GTTSSSS EE E TTTT S S E E E E SSSS
EXPOSURE. 0001136'*8 5 0 1 0 0 1 1 1 0 2 13'76665'0 3**9500001 0011'53873 9 2 1 4 * 1 0 * 5 1 *6071*5*81 *28*692'51 52.2860212 4004013705
1 0 1 SEQUENCE. GSQHTVDKKK YAAELHLVHW NTKYGDFGKA VQQPDGLAVL GIFLKVGSAK PGLQKVVDVL DSXKTKGKSA DFTNFDPRGL LPESLDYWTY PGSLTTPPLL
SHEET.. .. BBBBB BBBB C C BB

BRIDGE2.. NN L
BRIDGEl., jjjjj kkkk 0 0 MM
CHIRALITY ++--++--+- -----+++++ ++++--+--+ +-++--++++ ------+++- -
BEND.. S ss sssss ssss ss s s s S
5-TURN..
....
4-TURN.. >>4>x< 4<<
3-TURN.. >>3<< > 3 3<
..
SUMMARY.. S EEEEE SS E E E E H H H H H HHTT BSS T T S B S EE
EXPOSURE. 5 0 1 3 0 0 1 0 * 7 4 2 5 6 4 4 ' 1 2 8 814.83552' 6'7'2'0358 8144468*'4 * 3 8 1 2 9
2 0 1 SEQUENCE. ECVTWIVLKE PISVSSEQVL KFRKLNFDGE GEPEELMMN WRPAOPLKNR QIKASF
42) 1DFR DIHYDROFOLATE REDUCTASE [OXIDOREDUCTASE: NADPH/DONR, DIHYDROFOLATE/ACCPTRl (BACTERIAL: LACTOBACILLUS CASE11 , lDFR ...
SHEET.... AAAAAAA A B AAA AAA A AAA
BRIDGE2.. bbbbbbb eee f eee
BRIDGE1.. aa C C I aaa ddd f aa
CHIRALITY --+------ +-+---+--- -+++++++++ ++++++---+ --++++++-+ -+--++---- -+-+-++-+- ++--+-+-++ ++++++++-+ ++---++--+
BEND.. ss s s ssss s s sssssss sssssss ssssssss sss sss ss sss s ss sssssssss s s s
5-TURN..
....
4-TURN.. >>>>XXKX X<<<< >>4><<4< >>> > x < < < < >>
3-TURN.. >33 < > > 3 << > 3 3 < >>3<< > 33< >33< >>
..
SUMMARY.. EEEEEEETT B SBSSSS S S H H H H H H H HHHHTTSEEE HHHHTTSS SSS SSSEEE SS TTB S HH HHHHHTTSS S E E E S H
EXPOSURE. 32082121" 2 1 3 1 5 * 5 9 8 0 2 ' 0 6 5 2 9 * 4 4 ' 6 5 0 4 5 2 0 0 2 Bl''30755f **435*4400 041*9**3*1 '524548956 327581**3* '7'2002821
1 SEQUENCE. TAFLWAONRN GLIGKDGHLP WHLPDDLHYF RAOTVGKIMV VGRRTYESFP KRPLPERTNV VLTHQEDYQA CGAWVHDVA AVFAYAKQHL DQELVIAGGA
SUMMARY. . ......H=ALPHA-HELIX.. .,E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..G=3-HELIX.. ..I = 5 - H E L I X a . . .T=3-, 4-, OR 5-TURN.. ..S=BEND.. ..
TABLE A111 (continued) tQ
6,
p\3
SHEET.. .. AAAAAAA B A A AAAA A AAA A AA 0
BRIDCE2.. GGGGGGG HHHHHH
BRIDGE1.. bbbbbbb I H H HHHH GGGGGGG
CHIRALITY ++++++++++ +-------+- --+-++---+ -++-+--+++ +-----+-++ ++--+-----
BEND..... SSSSSSSSS S ss s s s s ssss s
5-TURN.. .
4-TURN... >>XX<<<< > 4 4 4<
?-TURN...
. .. . .. 1<< >??<
__ >
.??
-- <.
SUMMARY.. HHHHHHHTS SFEEEEEESS SB S S EEE EEEE SSTT T EEEEEEE
EXPOSURE. * 2 0 8 5 2 8 * 8 1 6 3 1 2 0 0 6 0 7 1 68'387.22' 2R9.929986 7**3*5*6*3 2 2 0 2 2 2 3 4 * * **
1 0 1 SEQUENCE. QIFTAFKDDV DTLLVTRLAG SFEGDTKMIP LNWDDFTKVS SRTVEDTNPA LTHTYEVWQK KA
43) lGPD D-GYCERALDEHYDE-3-PHOSPHATE DEHYDRCGENASE [OXIDOREDUCTASE: ALDEHYDE/DONR,NAD/ACCPTR] (LDBSTER: HIMARUS AMERICAlGPD

SHEET.. AAAA AA B E CCCC CCCC CCC AA A AAA
BRIDGE?. bb cc I11 d ddd
. ..
BRIDGEl.. aaa a bb G G HHHH H H H H I11 c c a aaa
CHIRALITY +---+-+-+ ++++++++++ +--+-+---+ +++--+++++ +++++-++-- --+--+-++- +-----+-+- ---+-+-+++ -++++-+++- --++-++++-
BEND.. s s s s ssssssssss sss sss s s s s s s s s s sss s s ss sss s s s s s s sss s ss s
5-TURN.. > 5 5 5 5< > 5 5 5 > x 5 55<< > 5 555< >5555<
....
4-TURN.. . > > > > x x x x < < << > > > > x xx < < < < > 4 4 4 < >444 < >444< >
3-TURN.. . > 3 >x3<< >33< > 3 3< > 3 3 < >33 < >33<
SUMMARY.. EEEE TTT H H H H H H H H H H TTT E E TTS H H H H H H R H H BTTTB S EEEET TEEEETTEEE E E SSTTT S TTTT E EEE S S S
EXPOSURE. 5 5 1 0 1 1 2 1 3 5 3 0 1 1 0 1 4 0 1 4 * 5 3 5 7 5 2 0 0 1 23.247'412 6 0 1 5 9 0 3 2 6 4 82'6.2'9'. 81131.59'1 533*6**09* 0 3 0 8 * 7 3 1 6 1 080155'541
1 SEQUENCE. SKIGIDGFGR IGRLVLRAAL SCGAQWAVN DPF IALEYMV YRFKYDSTHG W K G E V K M E D GALVVDGKKI TVFNEMKPEN IWSKAGAEY IVESTGVFTT
SHEET.. .. AAAAA A AAAA D DDDDD E E

BRIDGE2.. eeee f LLLL
BRIDGE1.. dddd f eeee J kkkkk P P
CHIRALITY +++++++++- +-+-+--+-- -++--+--+- ++-+++-+++ ++-----+++ ++++++++++ +++----+-- --------++ ----+++-++ ----+--+++
BEND..... SSSSSSSSSS S S SS SSS SS S SSS SS S sss ssssssssss s s s s ss ss s s sss
5-TURN.. . >5555< >>5 55<<
4-TURN... >>><XXX4<<< >44 4< > > > > <xxx>xxx<x x < 4 < <
3-TURN.. a >>>X<<< > 3><3< >33< >3 3< >33< >33 < >3 3x33<
SUMMARY.. H H H H H H H H H H S SEEEEES SSS B TT TTTTS TT SEEEE H H H HHHHHHRHHH HHHH B EEEEE TT SB T T TT BSSS
EXPOSURE. 4*803205*2 21*3001226 1.74331011 13***16*+4 6 8 0 0 8 0 3 4 1 0 1 1 0 0 1 1 1 5 1 1 4**2*14'1* 138610148* 243120536. **42240276
101 SEQUENCE. IEKASAHFKG GAKKWISAP SADAPMFVCG VNLEKYSKDM TWSNASCTT NCLAPVAKVL HENFEIVEGL MTTVHAVTAT QXTVDGPSAK DWRGGRGAAQ
SHEET.. .. DDDDD DDDDD DDD DDDD F F F F FF DDD

BRIDGE2.. MMMMM N NNNN
BRIDGEl.. MMMMM kkkkk LLL L J ... a a a a aa
1 .. 000
..
CHIRALITY ---+---+++ ++++++-+++ ++++-----4 -+-++----- -+---+---- ++++++++++ +++-++++++ ---+-----+ ++++-+---+ --++-+--+-
BEND.. s ssssssssss sss s s ss ssssssssss sssss ss s s sss ss ssss
5-TURN.. >5555<
....
4-TURN., >>> >xx<<<< > >>>XXXXXXX <<<<
3-TURN.. >33< >33< >3><3< >33 < >33< >
..
SUMMARY.. EEEEE HH HHHHHHSSSS SSS EEEEE S S EEE EEEE TT HHHHHHHHHH HHHTTTTTSE EEE S TT SSS S S E EESSTT EEE
EXPOSURE. 5 ' 3 9 1 6 4 5 8 2 '0889216'8 6 6 ' 3 8 2 6 8 6 5 3 6 5 3 0 0 0 3 8 4 1 3 0 9 0 5 * * 2 3 2.913321'7 31'3'2.342 3319'**493 92637.8110 1 1 0 * 5 4 2 * 8 8
2 0 1 SEQUENCE. NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPDVSVVD LTVRLGKECS YDDIKAAHKT ASEGPLQGFL G Y T E D D W S S W I G D N R S S I FDAKAGIQLS
SUMMARY.. ......H=ALPHA-HELIX, ...E=BETA-STRAND.. ..B=BETA-BRIDGE.. ..G-3-HELIX.. ..I=S-HELIX.. ..T=3-, 4-, OR 5-TURN.. . .S-BEND.. ..
SHEET.. , . DDDDD
BRIDGE2.. 000
BRIDGE1.. NNNNN
CHIRALITY +++-t-+--- ++++++++++ ++++++++++ +
BEND.. ss ssssssss ssssssssss s
5-TURN.. >55 55<
....
4-TURN.. >>>><xx<>xx>xxxxxx<< <<
3-TURN.. 33< >>3xx3<< >33<
..
SUMMARY.. TTEEEEE HHHHHHHHH H H H H H H H H H H HT
EXPOSURE. 85'1711831 0123120310 8 3 1 1 9 6 0 3 ' 3 28.
3 0 1 SEQUENCE. KTF VKWSWY DNEF GYS QRV I DLLKHMQKV DSA
44) 4ADH APO-LIVER ALCOHOL DEHYDRWENASE IOXIDOREDUCTASE: CHOH/DONR, NAD/ACCPTR] (HORSE LIVER: EQUUS CABALLUS). ...... ..4ADH
SHEET.. .. AAAA AAAB AAAAAAA CCCCC DDD B D CC CC CEE E
BRIDGEZ., B cc HHHH K f I
BRIDGE1.. AAAA AAAE AAAAAAA GGGGG JJJ E K H H HH IMM M
CHIRALITY -++---+-+ ---++-++-- --+------- --++-----+ ------++++ +++-++-+-- ++--++++-+ --++---+++ ++--++-+-- --+--+-++-
BEND.. sss ssss ss ssss sssssss ss s ss s ss ss sss
5-TURN.. >5555<
....
4-TURN.. > > > > X <<<< >
3-TURN.. >33< >33< >>3<< >33< >33<
..
SUMMARY.. SSS EEEE EEEB STTS EEEEEEE TTEEEEE EEE H H H H HHHTTSS SSB B E E E E E TT S TT B E E E S S SSS
EXPOSURE. *'54*81'09 00008*'**9 1 4 7 5 9 0 5 1 3 5 1'4'100060 4 0 0 0 0 1 ' 5 0 1 3015244.14 5 2 0 1 0 0 0 0 0 0 0 6 1 3 2 3 2 * 5 1 * 6 0 * 7 6 2 5 0 0 0 0 2 0 1 2 4 6 * 2
1 SEQUENCE. STAGKVIKCK AAVLWEEKKP FSIEEVEVAP PKAHEVRIKM VATGICRSDD HWSGTLVTP LPVIAGHEAA GIVESIGEGV TTVRPGDKVI PLFTPWGKC
SHEET.. .. A AA AA B A CC CCC EEE FFFF cn

BRIDGEZ.. DD 0000 M
BRIDGE1.. C C DDf B GG GGG MMM nnnn
CHIRALITY ++++-++++- -++-++--+- +--+-+--++ +--+------ -+-+++-++- +--+++---- -++--+++,+ ++-+++++++ ++++++---- ++-----+-+
BEND.. sssssss ss ssss s sss s ssss ss ssss sss ss sssss ssssssssss sssssss ss s
5-TURN.. >5555< >>>55<c<
....
4-TURN.. 444< > 444< >444< >>>>xxxx<<<<
3-TURN.. >33< >33< >33< > 33< >>3<< > 3 3 x > > x<<< > 3 3< > 33<
SUMMARY. TTTSSTT S S SSSS S TTS SE EETTEE B TTT SBSEE EEEGGGEEE SS TTTGG GGGTHHHHHH HHHHTTT TT EEEE
...
EXPOSURE. *32*8"229 09'2268'3' 031*756128 10+7*71510 1 3 0 1 0 0 0 3 5 0 00323100*0 867041'780 0 0 0 1 1 0 0 2 0 2 0005811*18 '612008011
101 SEQUENCE. RVCKHPEGNF CLKNDLSMPR GTMQDGTSRF TCRGKPIHW LGTSlTSQYT VWEISVAKI DAASPLEKVC LIGCGFSTGY GSAVKVAKVT WSTCAVFGL
SHEET.. .. FF FF FF F G FFFF G FFF F

BRIDGE2.. P PP 4949 rrr r
BRIDGE1.. n n nn PP P s 0000 5 444 4
CHIRALITY -+++++++++ +++---+--- -+-+-+++++ ++++-+-+-- --+++-+--+ +++++++-+- --+---++-+ -+++++++++ t--+++---- +++--++---
BEND.. ssssssssss sssss s sssss ssssss s ssssss s ssssssssss s s sssssssss ss sss ss
5-TURN.. >5555< >5555<
....
4-TURN.. . >>>>xxxxxx x < < < < >K<<<<
>>> >444< >> 4>x<4<< >>>>xxx<<<< > 4 4 4 <
3-TURN.. >>3<< >33< > 3 3<>33x33< > 3 3<>33< >33<
SUMMARY. SHHHHHHHHH HHHHS EE E E S G G G H H HHHHHT S E E E TTTSSS H HHHHHHTTTS BSEEEE S H H H H H H H H H TB TTT E E E E TT
..
EXPOSURE. 3 1 4 0 0 0 0 0 2 0 0 ' 6 4 1 4 5 7 8 0 01379**5*6 60'*120774 1 2 4 * * 8 * 9 6 1 7'104*62*4 0 0 4 2 0 0 0 2 8 1 9 5 ' 1 0 3 3 0 8 2 003'5'0300 332836'5.'
2 0 1 SEQUENCE. GGVGLSVIMG CKAAGAARII GVDINKDKFA KAKEVGATEC VNPQDYKKPI QEVLTEMSNG GWFSFEVIG RLDTMVTALS CCQEAYGVSV IVGVPPDSQN N
SUMMARY.. ......H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....G=3-HELIX....I=5-HELIX....T13 -,4-, OR 5-TURN....S=BEND.... w*
TABLE A111 (continued) E.3
Q,
h3
SHEET.. .. FFFF D DDD D DD DDD E.3
BRIDGEZ.. 11
.. 111
___
BRIDGE1.. rrrr 1 111 1 JJJ
CHIRALITY -+--+++++- +--+-+-+-- +--+++++++ ++++++-++- +++++++-+- -+++++++++ ++++-+-+-- --
BEND.. ssssss s sss s SSSSSSS ssssssss sss ss sssss sssss
5-TURN.. >555 5<
. ..
4-TURN.. . >>44<< > > 4 > x x > x xxx<<<< >444< > > > > x x x <<<<
3-TURN... >>3<X33 < > > 3 << >33< >33< >33< > 3 > < 3 < > 3 3x33<
SUMMARY.. THHHHT T EEEE SGG G H H H H H H H HHHHHHTS TTTEEEEE ETTTHHHHHH HHHTS EE EEE
EXPOSURE. 5*896*46*6 4 3 7 6 8 5 4 6 1 0 1 2 3 0 5 * 1 0 4 * 1 0 5 5 3 8 5 * * 1 5 0 7 2 0 3 4 5 9 3 50**04*009 538'5'1328 0057
3 0 1 SEQUENCE. LSMNPMLLLS GRWKGAIFG GPKSKDSVPK LVADFMAKKF ALDPLITHVL PFEKINEGFD LLRSGESIRT ILTF
45) 4LDH LACTATE DEHYDROGENASE, APO ENZYME M4 [OXIDDREDUCTASE: CHOH/DONA, NAD/ACCPTRl [DOGFISH MUSCLE: SQUALUS ACANTHIUSILDH
SHEET.. .. AAAAA AAAA A AAAAA AAAA
BRIDGEZ.. bbbb cccc c dd
BRIDGEl.. aaaaa aaaa a ccccc bbbb
CHIRALITY -++++++-- -+++--+--+ +----+-+++ ++++++++++ +-++-+---- +-+-++++++ ++++++++++ +-t-+++--- +-++++++-+ ---+++----
BEND..... SSSSSS S s s ss ssssssssss ss ss s ssssss ssssssss s ss s ssssss s s
5-TURN.. >5555< >5 555<
4-TURN.. >>44<< > > >>xxxxxx<< << > > > > x x <x x x 4 < < <
..
3-TURN.. >>3<<
. >33< > 3 3x33< >37< > > 3 < < > 1 > x 7 << >>7<<
SUMMARY.. THHHHS TT s S E E E E E S H H H H H H H H H H H HTT S E E E E E s HHHHHH HHHHHHTTGCGS S E E E E E SSSGCG s s E E E E
EXPOSURE. * 8 * * 9 * * 9 6 * '*9*****2' 6 1 0 0 0 0 0 1 6 3 3 8 2 1 0 0 8 1 0 1 * ' 7 1 0 6 1 0 8 1 0 2 * 9 9 + 9 1 ' 4 43'*37*25' *4'1882421 *927303417 00001442*6
1 SEQUENCE. ATLKDKLIGH LATSQEPRSY NKITWGCDA VGMADAISVL MKDLADEVAL MVMEDKLKG EMMDLQHGSL F LHTAKIVSG KDYSVSAGSK LVVITAGARQ
SHEET.. .. AA A BB C BB
BRIDGEZ.. e
BRIDGE 1. . dd e FF C FF
CHIRALITY -++--+++++ ++++++++++ ++++++++++ ----++-+++ ++++++++++ -+--++++-- ++++++++++ +++++++-+- -+++-+-+++ +-++++----
BEND..... SS S S S S S SSSSSSSSSS S S S S S S S S S ss s ssssssssss s sss ssssssss sssssssss SSSS ssssss
5-TURN.. >5555< >5555<
4-TURN.. > > > 4 x x x>xx<xx<4x x>>x<<<< >> >>xxxxxx<< << >4>>X4X< < > < 4 > < 4 4 < > 4 4 4 < >
..
3-TURN.. . > 33< >33x33 < >33< >33< >33< > > 3 << >33<
SUMMARY.. SS H H H H H H H H H H H H H H H H H H H H H H TT EE S S H HHHHHHHHHH H TTS B TTTTHHHHH TTTTTTTTT TTTS E E BSSSTT E E
EXPOSURE. + * 5 8 4 * 6 * 1 1 3 9 0 0 8 7 8 7 ' 1 06583'387' 0800822'31 0 2 0 0 3 0 0 3 9 2 2 6 1 7 ' 7 4 0 0 8 1 0 0 2 2 1 1 4 7 0 7*310"*75 '386030580 0262'40118
1 0 1 SEQUENCE. QEGESRLNLV QRNVNIFKFI IPNIVKHSPD C I I L W S N P V DVLTYVAWKL SGLPMHRIIG SGCNLDSARF RYLMGERLGV HSCSGVGWVI GQHGDSVPSV
SHEET.. .. D D E E PPF CCC CCC F FFG G F

BRIDGEZ.. HHH L
BRIDGEl., I 1 1 3 KKK HHH G K KKM M L
CHIRALITY ++++-+-+-- ++++-+++-+ --++++++++ ++++++++++ +---++++++ ++++++++++ +-+-+---+- +--+++--+- +-+-+-+--- -+-+------
BEND..... SSS SSS SSSSS SS S S S S S S S S S S SSSS SSSS SSS SSSS SSSSSSSSSS SS sssss ss sss s
5-TURN.. . > > 5 55<< >5 555<
4-TURN... 444< > >>4<<< >44>x4 4<< > > 4 4 << > > > > x x<x<x>x><<<<
3-TURN.. . >33< > 3 3 < >>><<< >33<>33 < >33< >>3<< > 33< >33x33< >33<
SUMMARY.. TTT BTTB HHHHH S S SSSGGGGTHH HHTSTTSHHH HBS H H H H HHHHTHHHHH HTT EEE EEE TTSTT SS EEE E EEBTTB SB
EXPOSURE. 3 6 1 0 7 5 6 * * 8 2 4 8 * 6 5 4 2 * * 9*947*23'6 60262**68* '*6*51*420 * 1 0 0 6 0 0 3 8 0 2'98696118 81106'7551 " 6 4 1 0 0 0 8 1 0 1835'014'3
2 0 1 SEQUENCE. WSGMWNALKE LHPELGTNKD KQDWKKLHKD VVDSAYEVIK LKGYTSWAIG LSVADLAETI MKNWRVHPV SMVKDFYGI KDNVFLSLPC VLNDHGISNI
SUMMARY........H=ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIffiE....G~3-HELIX....I=5-HELIX...~T~3 -,4-, OR S-TURN....S=BEND...,

SHEET.. ..
BRIDGEZ..
BRIDGE1..
CHIRALITY ------++++ ++++++++++ +++++-+
BEND.. ssss ssssssssss ss s
5-TURN..
....
4-TURN.. >>4>x x>xxxxxxxx <<<<
3-TURN.. >33x3 3<>33< >33<
..
SUMMARY.. HHHH HHHHHHHHHH HHH S
EXPOSURE. 6'4*29**16 *785*01962 7*28*2*49
301 SEQUENCE. VKMKLKPNEE QQLQKSATTLWDIQKDLKF
46) 2GRS GLUTATHIONE REDUCTASE IOXIWREDUCTASE: GSSG/ACCPTR, NADPH/DONR, FLAVOENZYMEI (HUMAN ERYTHRCCYTE)..............ZGRS
SHEET.. .. AA B AA AAA B
BRIDGEZ.. b cc ccc
BRIDGE1.. aa f aa f
CHIRALITY +--++--+- +-++++++++ ++++-+---- -+-+--+--+ ++++++++++ ++++++++++ ++-++++-+- --+----+++ ++++++++++ ++++++++++
BEND.. s s sssssssss sssss ss ss s ssssssssss ssssssssss ssss ss ss ssssssssss ssssssssss
5-TURN.. >5555<
....
4-TURN.. > 4 > > < > x x >x < < < < > > > > < < < x > > > x xxxxxxxxxx< <<< >>> >xxxxxxxxx xxxxxxxxxx
3-TURN.. >>3<< >3><3 < > 3 3< >>3<< >33<
..
SUMMARY.. S EES BTTnHHHHH HHHHTT E E EEESS TBHH HHHHSHHHHH H H H H H H H H H H HHSS GGGS H H HHHHHHHHHH H H H H H H H H H H
EXPOSURE. * 5 5 3 7 0 0 0 0 1 0 1 3 1 0 1 1 0 0 5 702*960*80 0836**2826 2 8 2 4 2 5 3 0 3 7 4028304.23 *5*6045*7* **8*5*7*1* 732**05391 7'23698'86
1 SEQUENCE. VASYDYLVIG GGSGGLASAR RAAELGARAA WSHKLGGT aVNVCaVPKK WNTAVHSE FMHDHAWGF PSCEGFFNWR V I K E K R D A Y V SRLNAIYQ"
SHEET.. .. AAAAA C C C M A DD EE EEEE EEE
BRIDGE2.. H ddd 111 mrn
BRIDGEl.. ccccc G G H b 11 __ ii kkkk 111 m
CHIRALITY +++-+----+ --+---+-+- +--+--+--- +-+---++++ +------+++ -+++++---+ +++++++--- ++---+-+-+ ++++++++++ +-+-----+- 2
BEND.. SSSS s ssss s sss ss sss sss ss s sssss ss ss ss ssssssssss sss
5-TURN.. >5555< > 5 555<
....
4-TURN.. <<<< >> 44<< >> >>xxxxxx<< <<
3-TURN.. .. >33< >33< >33 < >33< >3 3x>3<< >33<
SUMMARY.. HHHTTEEEEE S B S S S S S B STT B SSEEE EE STT SSS TT E E H HHHTT S S SSEEEE SH H H H H H H H H H H HTT EEE
EXPOSURE. 09'391961' 2*12117*9* 51081.6854 5885000150 183392**9* 4 7 1 0 9 7 2 6 3 1 4282*5**61 3200021248 5 0 8 l l l l B R 3 1 2 4 1 9 0 0 1 0 0
1 0 1 SEQUENCE. LTKSHIEIIR GHAAFTSDPK PTIEVSGKKY TAPHILIATG GMPSTPHESQ IPGASLGITS DGFFQLEELP GRSVIVGAGY IAVEMAGILS ALGSKTSLMI
SHEET.. .. EE FFF FFF FFFFFF FFF F EEEE DD G G

BRIDGE2.. 0000 kkkk
BRIDGEl.. mm NNN NNN NNNNNN 000 0 jj 11 P P
CHIRALITY +-+-++++-- ++++++++++ +++-++---- +--++---++ -+-------+ +-+------- -----+---+ +-----++++ -++++-+--- -+-+--+--+
BEND.. , sssss ss ssssssssss sssss S s sss ssss ss s s . s s s sss sss s
5-TURN.. >5555<
...
4-TURN.. > >>>xxxxx<<<< >444<
3-TURN.. >33<> 33< >33< > 3 3< >33 < >33 0 3 3 < >33<
..
SUMMARY.. SSSSS TTS H H H H H H H H H H HTTSS EET TEEEEEEETT SSS E E E E E E SSSS E E E E SS E E E E S E E S TT S TTTTT B TTS B S
EXPOSURE. * 6 8 3 8 1 * * 4 8 54816181*2 386532922' 5 0 9 1 + 9 8 8 * * 4.33613143 57*6**6**8 3 9 2 * 9 5 2 1 0 1 29555172'. 141**351*8 6**248647*
2 8 1 SEQUENCE. RHDNVLRSFD SMISTNCTEE LENAGVEVLK FSQVKEVKKT LSGLEVSMVT AVFGRLPVMT MIPDMCLLW AIGRVPNTKD LSLNKLGIQT D D K G H I I M E
E3
Q,
SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B~BETA-BRIffiE....G=3-HELIX....I~5-HELIX....T~3-,4-r OR 5-TURN....S=BEND.... to
w
N
TABLE A111 (continued) 03
N
SHEET.... A AA A HHH H HHHH A
HH HHHHHH H
BRIDGE2.. E R RRRR
BRIDGE1.. E dd d QQQ Q QQ s s ssssss S
CHIRALITY -+--+-+++- ++-++-+--+ -+++++++++ +++++++-+- +++---+++- ----+-+--- +++---++++ +++--++++- -+--+---++ +++-+-+---
BEND..... SS SSSS SSSSSS SSSSSSSSS SSSSSSSS S SSS ss s ssss ssss sss ss sss ss
5-TURN..
4-TURN.. >>>4xxx>xx xxxx<<<< ,
> >_
\>Y
.,.. ((<(
....
..
3-TURN.. . >33< >33<>33< > 33< > > 3 <<
SUMMARY.. SSB S S S S E E E STTSSS HHHHHHHHH HHHHHHHS TT SSS E E E SS E E E E E HHHH HHHS S S S E E E E E E E E GG C S S SS E
EXPOSURE. 524274'101 0824023.46 4 3 9 1 1 5 2 0 0 7 6005411*** * * 2 9 3 7 7 7 4 4 4 4 4 0 4 1 4 1 1 0 0 2 0 2 3 1 5 * 9 0 4 * * 4 3 * * 4 3 ' 52748381'6 0880*6*180
381 SEQUENCE. F Q N T N V K C I Y AVGDVCGKAL L T P V A I A A G R KLAHRLFEYK E D S K L D Y N N I P T V V F S H P P I GTVGLTEDEA I H K Y G I E N V K T Y S T S F T P M Y HAVTKRKTKC
SHEET.... HHHHHHH HH HHHHH H

BRIDGEZ.. TTTTTTT TT TTTTT
BRIDCEI.. SSSSSSS U RRRRR U
CHIRALITY +---+---+- --++-++-+- ++++++++++ +++++----+ +++++----+ t-+++++++
BEND.. sss s ss sssssss ssssss s ssssss s sssssssss
5-TURN.. >555 5 < >5555<
....
4-TURN.. > > 4 4 x x > > x x<<<< >> >4<<<
3-TURN.. >33< > 3><3< >>3<< > 3 7<>77< >>><<<
..
SUMMARY.. E E E E E E F T T T T E E E E E E E E S T T H H H H H H H H HHHHTTTB H HHHHTS s SSSCGCCSS
EXPOSURE, a ~ i a a ~ 8 8 *s*8 i : a ~ e a 7~4 8~3 . 2 e . 5 3 e73a**s:i: 79:6*7*5** 8~335sa:g:
4 0 1 SEQUENCE. VMWMVCANKE E K W G I H M O G LCCDEMLOCF AVAVKMGATK ADfDNTVAIH PTSSEELVTL R
47) ZSOD C U , ZN S U P E R O X I D E D I S M U T A S E [OXIDOREDUCTASE: SUPEROXIDE/ACCPTRl ( C c W ERYTHROCYTE: BOS TAURUS1 .....,........... .2SOD

SHEET.. .. AAAAAB AAAAAA AAA AAAAA AAAA B B BBBBBB B B . ___.
BBBBC ~
CAAAAAAA~ ~ . ~ .
BRIDGEZ.. BB cccccc ccc DDDD DUD GGCG
BRIDGEl.. AAAME AAAAA CCCCC C C C C FF FF F H H F FFFFJ JDDDDDDD
CHIRALITY ++----++- +-+++----+ -+--+---++ --+++--+-- --+---+-++ ++--+++--- -+++-+--+- -++-++--++ +-----+++- ++-+++---+
BEND.. S sss sss s ss s sssssss s ss ss ss ss ss s S
5-TURN..
....
4-TURN.. >44 4<
3-TURN.. >33< >3>X3X<3< >17c >?7 <
..
SUMMARY.. S E E E E E B sss E E E E E E EEETTEEEEE EEEES SEE EEEEEES TTGCGTT s B s s TT SS EEEEEEEBTT TBEEEEEEES
EXPOSURE. 89600040*1 '4*1*04060 43'6'40385 3 6 0 3 3 2 * + 3 8 1 0 0 0 0 6 6 3 0 3 7 7 ' 3 2 8 2 8 2 7 00476*6*10 0 5 * 5 * 8 1 0 0 0 0 1 0 4 1 5 1 9 * 7 052*1*3*0*
1 SEQUENCE. ATKAVCVLKG D C P V Q G T I H P EAKGDTVVVT G S I T G L T E G D HGFHVHQFGD N T W a T S A G P H F N P L S K K H G GPRDEERHVG DLGNVTADKN C V A I V D I V D P
SHEET.. .. D D BBBBB B B B B B AA
BRIDGEZ.. 11111 I I111
BRIDGEl.. k k GGGG E BB
CHIRALITY ++-t-+++-+ ++------+- ----+++--+ ++++--+++- +++-----+
BEND.. s sssss sss ss ss ss sssss s
5-TURN..
....
4-TURN.. > 4 44<
3-TURN.. > 3 3 < > 33< >33<
..
SUMMARY. . S BSSSTTB TTSEEEEESS SS S T TTTTS S EEEEEE EE
EXPOSURE. 683293'820 10310000** 71571*649* *047404037 6301110021
1 0 1 SEQUENCE. L I S L S G E Y S I I G R W I W H E R PDDLGRGGNE E S T R T G N A G S R L A a G V I G I A K
48) l M B N MYOGLOBIN [OXYGEN STORAGE] (FERRIC I R O N METWYOGLOBIN) (SPERM WHALE)
- ......................................... lMBN
SHEET.. ..
BRIDGEZ..
BRIffiEl.,
CHIRALITY --+++++++ ++++++++++ ++++++++++ +++++-++++ ++-+++++++ -++++++-++ ++++++++++ +++++++--+ ++++++++++ ++++++-+--
BEND..... SSSSSSS SSSSSSSSSS ssssssssss sssss ssss ss sssss sssssss ss ssssssssss ssssssssss sssssss sssssss
5-TURN.. . >5555< >>555<<
4-TURN... > > > > X X X X X X X X < < < < > >>>xxxxxxx x x < < < x > > 4 << < > > 4 4 < < > > > > < < < x >>xxxxxxxxx
> xxx<<<< >>4>xx>xx xx<<<< >
3-TURN.. . >3>x3<< > > 3 < x 33X33X33< >33< >>3x<3 <>33< >
SUMMARY.. H H H H H H H HHHHHHHTTS H H H H H H H H H H H H H H H H H H H HT HHHHT SHHHHHH HH H H H H H H H H H H HHHHHHTTTT H H H H H H H H HHHHHTT
EXPOSURE. *15*551*50 5'81650997 3 2 1 0 0 2 6 1 1 1 * 1 1 * 5 5 8 8 1 2 * 8 6 + * 8 8 + 1 + 68791*83*6 0 7 * 3 0 5 * 4 0 8 418310'882 '8'781'748 74508'9'25
1 SEQUENCE. VLSEGEWQLV LHWAKVEAD V A G H G Q D I L I RLFKSHPETL EWDRFKHLK TEAEMKASED LKKHGVTVLT A L G A I L K K K G HHEAELKPLA QSHATKHKIP
SHEET.. ..
BRIDGE2..
BRIDGE1..
CHIRALITY ++++++++++ ++++++++++ +++-++++++ ++++++++++ ++++++++-+ +
BEND..... SSSSSSSSSS SSSSSSSS S ss sssssss ssssssssss ssssssssss
5-TURN.. . >5555 <
4-TURN... >>>XXXXXXX XXXXX<<<X4 4 4 < > > > > x x x xxxxxxxxxx xxxxxx<<<<
3-TURN... 33< > 3 3 X 3 3< >33< >33< >33<
SUMMARY.. HHHHHHHHHH H H H H H H H H T TTTSHHHHHH H H H H H H H H H H HHHHHHHHHT
EXPOSURE. 4'42634091 119189892' 78848'1730 0 6 9 0 0 + 2 2 3 * 6 0 1 6 2 1 * * 6 7 '8'
1 0 1 SEQUENCE. IKYLEFISEA IIHVLHSRHP GNFGADACGA MNKALELFRK D I A A K Y K E L G YW
49) l E C D HEMOGLOBIN (ERYTHROCRUORIN, DEOXY) [OXYGEN TRANSPORT] (CHIRONOMOUS THUMMI THUMMI) ............................. lECD I/,
SHEET.. , .
BRIDGE2..
M
BRIDGE1..
CHIRALITY -++++++++ ++++++++++ ++++++++++ -++++++-++ +++--+++++ +-++++++++ ++++++++++ +-++++++++ +++++++++- t--+++++++
BEND.. ssssssss ssssssss s ssssssssss ssssss ss ssss sssss ssssssssss ssssssssss ss s ssss ssssssssss sssssss
5-TURN.. >555 5<
....
(-TURN.. >>>>xxxxx x < x < < 4 < > > >>xxxxx<<<x > 4 4 < < > 4 4 4< > > 4 4 < < >>>>xxxxxxxxxxxxx<< << > > > > xxxxx<<<< >>>>xxxx
3-TURN.. >33< >>3<x33< > 3 3 x > 3 < x 3 3 x33<>33<>3 3< >> 3x<3< >>3< <
..
SUMMARY.. H H H H H H H H HHHHTTTT H H H H H H H H H H H HHHHTT TT TTTS HHHHT TSHHHHHHHH HHHHHHHHHH HTTT HHHH HHHHHHHGGG T HHHHHHH
EXPOSURE. 768'526507 611'+1*861 31114100'5 295226.5'9 859'82'818 8 6 7 5 0 * 7 5 0 8 '514724'11 5428'8'620 8832755'" 4367'21754
1 SEQUENCE. LSADQISTVQ ASFDKVKGDP WILYAVFKA DPSIMAWTQ FAGWLESIK GTAPFETHAN RIVGFFSKII GELPNIEADV NTFVASHKPR GVTHDQLNNP
SHEET.. ..
BRIffiE2..
BRIDGE1..
CHIRALITY ++++++++++ +-++++++++ ++++++++++ ++++
BEND.. ssssssssss ss ssssss ssssssssss ssss
5-TURN..
....
4-TURN.. xxxxxxxx<< << > 4 4 > x > > xxxxxxxxxx xx<<<<
)-TURN.. >>><<< >33<
..
SUMMARY.. H H H H H H H H H H HS GGGGHHH H H H H H H H H H H H H H H H
EXPOSURE. 65003710'8 *3'1571981 02201'6214 4 0 6 9 5 5
1 0 1 SEQUENCE. RAGFVSYMKA HTDFAGAEAA WGATLDTFFG MIFSRCI to
Q,
SUMMARY.. .... .H~ALPHA-HELIX....E=BETA-STRAND....B~BETA-BRIDGE....G~3-HELIX....I=5-HELIX....T-3-,4-, OR 5-TURN....S=BEND.... to
v1
TABLE A111 (continued) N
03
N
50) 2MHB H E M O G L O B I N ( A Q U O MET) [OXYGEN TRANSPORT] (HORSE: EQUUS CABALLUS) .2MHB
............................................. Q)
SHEET.. ..
BRIDGEZ..
BRIDGE1..
CHIRALITY --+++++++ +++++++-++ ++++++++++ +++++-++++ +++++--+-+ t - + + + + + + + + ++++++++++ ++++++++++ ++++++++++ ----++++++
BEND..... SSSSSSS SSSSSSS S SSSSSSSSSS SSSSS SSSS SS SSS SS S SSSSSSSS SSSSSSSSSS SSSS SSSSS SSSSSSSSSS S SSSSSS
5-111111..
.......... . > ~
. > > 5 5 < <. <
4-TURN... >>>>XXXX XXXX<<<< > >>>XXXXXXX XX<<<< > > > > x x x x x xxxxxxx<x< < 4 < > > 4 4 < x >>>xxx<<<< >>>>xx
3-TURN.. . >33<>>3<< >>>xx <<x33< > 3 3< >3 3x33< > 3 3 < >>><<<
SUMMARY.. H H H H H H H HHHHHHHGGG H H H H H H H H H H H H H H H GCGG GG TTS ST T HHHHHHHH HHHHHHHHHH TTTT HHHHT HHHHHHHHHT S THHHHH
EXPOSURE. * 3 6 8 6 3 5 9 5 0 *4 1 2 9 * 0 4 8 8 1 1 * 1 0 1 4 0 0 6 0116138*0* *73**4855* 71871'6609 *309316702 6 8 2 '91 8 4 2 1 7*419750** 7.186822.2
1 SEQUENCE. VLSAADKTNV XAAWSXIICGH AGEYGAEALE RMFLGFPTTK TYFPHFDLSH CSAQVKAHGK XVCDALTLAV GHLDDLPCAL SDLSNLHAHK LRVDPVNF K L
SHEET..
BRIDGE?.
...
BRIDGEl..
CHIRALITY ++++++++++ +++++++-++ ++++++++++ +++++++++ ---++++ +++++++++- -+++++++++ ++++++++++ ++++++-+++ +-++++++-+
BEND..... SSSSSSSSSS SS SSS SS SSSSSSSSSS SSSSSSS S ssss sssssssss sssssssss sssssss s s sss ss ssssssss s
5-TURN.. .
4-TURN... XXXXXXXXX< < < X 4 4 4 < > > >> X X X X X X X X X XXX<<<X444 < >>>>X XXXX<<<< >>>>XXXXXX XXX<<<< >>>4<<<>>
3-TURN. >33< >33< >3><3< >>3<< >33< >>>x xx<xx3<< >33<>33<
SUMMARY.. HHHHHHHHHH H H TTT HH HHHHHHHHHH HHHHHHTTTT HHHH HHHHHHHTT HHHHHHHHH HHHHHHSGGG GGGGGGG SSHHHHHT H
EXPOSURE. 4220110010 1 63 4 ' 6 1 5 2 4 2 1 1 0 1 2 7 0 1 6 2227221679 *09*255*45 5406521**2 74**001200 00102036*1 5*74*'3591 '8 6 5 3 8 5 5 2 "
1 0 1 SEQUENCE. LSHCLLSTLA VHLPNDFTPA VHASLDWLS SVSTVLTSKY RIVQLSGEEK AAVLALWDKV NEEEVGGEAL GRLLWYFWT QRFFDSFGDL S NPGAVMGN P
SHEET.. ..
BRIDGE2..
BRIDGE1..
CHIRALITY ++++++++++ ++++++++++ ++++++++++ +++++++-+- -+++++++++ +++++++++- +++--+++++ ++++++++++ ++++++
BEND..... SSSSSSSSSS SSSSSSSS S SSSSSSSS SSSSSSSS SSSSSSSSS SSSSSSSSSS SSS SSSSS SSSSSSSSSS SSSSSS
5-TURN.. . >>555<<
(-TURN... >>XXXXXXXX XXXX<<<< > > 4 4 < X > > >X X < < < < >>>>xxxxx xxxxxxx<<< < > > > > x x xxxxxxxxxx x < < < <
3-TURN.. . >>3xx 3<< >>3<< > >3<<
SUMMARY.. H H H H H H H H H H HHHHHHHTTG GGHHHHSHHH HHHHHTTS THHHHHHHH HHHHHHHHHH GGGS H H H H H H H H H H H H H H H HHHHSS
EXPOSURE. *896706*30 9310900*81 * 9 1 * 4 5 0 2 7 5 8.8528'7'2 '4'2282362 1 0 0 0 0 0 0 6 7 4 1 * * 0 5 2 * 2 0 1 1 0 1 9 1 0 4 1 0 1 *023**5*
2 0 1 SEQUENCE. KVKAHGKKVL HSFGEGVHHL DNLKGTFAAL SELHCDKLHV DPENFRLLGN VLWVLARW GWFTPELQA SYQKWAGVA N A L A H K Y H
511 lLHB HEMOGLOBIN(MET)-CYANIDE V [OXYGEN TRANSPORT] [SEA LAMPREY: PETRWYZON MARINUS]. ......................... ....... lLHB
SHEET.. ..
BRIDGEZ..
BRIDGE1..
CHIRALITY --++----- ---++++++++ ++++++++++ ++++++++++ ++++++++++ +-+++++++- ++++++-+++ ++++++++++ +++++++++- -+++++++++
BEND.. SSS ssssssss sssssssss ssssssssss ssss SSSSS s sss s s ssssss sss ssssssssss ssssssssss s sss
5-TURN..
.... > 5 5 55< ,
4-TURN.. > > 4 > x x > < x < < > x > 4 < < x 4 >>x>xxxxxx x < < < < > 4 4 4 < > 4 4 4 < > > > > xxxxxxxxxx xxxx<<<< >>>>
3-TURN.. >33< > 3 3 < > 3 3 x 3 > < 3< > 3 3 < > 3 3x>3x<3< >33< >> 3 < x 3 3 < >33< >3>x>x<<<
..
SUMMARY.. SSS H H H H H H H H HTTHHHHHTT THHHHHHHHH H H H H TTTTT T GCCTT S SSTTTS H H H H H H H H H H H H H HHHHHHHSSS STTGGGHHH
EXPOSURE. *3 4 2* 6 * 379 2788436'1' 732663.997 ' 7 2 0 1 7 1 6 2 6 1 0 6 7 2 8 4 0 3 * 4 4 9 * 1 * 7 3 * 7 5*70**1780 8 * 4 0 4 * 3 1 9 3 1 4 9 1 2 6 2 1 * * 6 * * 2 3 9 3 * * 5
1 SEQUENCE. PIVDTGSVAP LSAAEKTKIR SAWAPWSDY ETSGWILVK PFTSTPAAEE FFPWKGLTT ADELKKSADV RWHAERIIDA VDDAVASMDD TEKMSSMKDL
SUMMARY.. ..... .H-ALPHA-HELIX.. ..E-BETA-STRAND.. ..B-BETA-BRIDGE. ...G=3-HELIX.. ..I-5-HELIX.. ..T=3-, 4-, OR 5-TURN.. .. SxBEND.. ..
SHEET.. ..
BRIDGE2..
BRIDCE1..
Y
CHIRALITY +++++-+--- -t+ttt+++t tt+tt--+-+ - t + t + + t t t t ++++++
BEND..... SSSSSSSS SSSSSSSSS SSSSSS S SSSSSSSSS SSSSSS
5-TURN.. . 5555<
4-TURN... XX<<X<44< >>>>XXX XXX<<<< >>>>XXXXX X<<<<
3-TURN.. . >>3<< > 3 3 < >>><<<
SUMMARY.. HHHHHTTT CCCHHHHHH HHHHHH S SHHHHHHHH HHHHCCC
EXPOSURE. 83*71****2 62'5182385 221.62378' 2 1 2 4 8 1 1 7 3 2 1421'55'
1 8 1 SEQUENCE. SCKHAKSFEV DPEYFKVLAA V I A M V A A C D AGPEKLLRMI C I L L R S A Y
52) I H B L LECHEMOGLOBIN (ACETATE,MET) [OXYGEN T R A N S W R T ] (YELLOW L U P I N ROOT NODUI.ES: LUPINUS LUTEUS L ) . ................. lHBL
SHEET.. ..
BRIDGE2..
BRIDGEI..
0
CHIRALITY -+-t+tt44 4tttt4ttt+ ttttt+++4+ t t t + t + - 4 t +t t t - t t t - 4 t - - - - t + - + t t t t t t + t t t t t t t t + t t t + + t- t - - - t - + t + t t t t t t t + t -
r
BEND..... S SSSSSS SSSSSSSSSS SSSSSSSSS SSSSSS SSS SSS SSS SS SS SSS SSSSSSSSSS SSSSSSSSSS SSS SSS SSSSSSSSSS
5-TURN.. . >555 5< >555
4-TURN... >>>>XXX XXXXXX<<<< >>4>XX>XXX <XX<4<< > 444X444< > > > > xxxxxxxxxx xxxxxxxx<< << >>>> xxxxxx<<<<
3-TURN.. >33<
. >>3 x<3< >>>x x<<x>3<x33 < >33< >33
SIRIMARY.. T T HHHHHH HHHHHHHHHT THHHHHHHHH HHHHHH GCC CCC CCC T T SS H H H HHHHHHHHHH HHHHHHHHHH HSS HHH HHHHHHHHHT
EXPOSURE. 2.56'61156 89703'7088 654'285818 3103.83981 5.65628'3' 3 * 2 3 * * 4 * * 8 47782'4844 14'114826' 8682578762 99305555"
1 SEOUENCE. CALTESQAAL VKSSWEEFNA NIPRHTHRPF I L V L E I A P A A KDLFSFLKCT SEWQNNPEL QAHACRWKL W E A A I Q L E V T C W A S D A T L KNLCSVHVSK
SHEET.. ..
BRIDGEZ..
BRIDGEI..
CHIRALITY t--ttttttt +ttt+ttttt +ttttt-ttt ttttttt+tt ttt+tt+ttt +
BEND..... SSSSSSS SSSSSSSSSS SS SS SSS SSSSSSSSSS SSSSSSSSSS S
5-TURN... 5<
4-TURN... >44>X>>X XXXXXXXXX< <<< >>>> XXXXXXXXXX XXXXXXXX<< <<
3-TURN... < >>3X<3< >>3<< > 33<
SUMMARY.. T CCCHHHH HHHHHHHHHH HHCCC HHH HHHHHHHHHH HHHHHHHHHH HT
EXPOSURE. 535'863734 4*882'809* 114"54*61 3 4 8 0 3 5 8 2 6 8 119225'41' *4*
1 8 1 SEQUENCE. CVADAWPW K E A I L R T I K E V V G A M S E E L NSAWTIAYDE L A I V I K K E M D DAA
53) l C R N CRAMBIN [PLANT SEED PROTEIN] ( A B Y S S I N I A N CAEIBACE SEED: CRAMBE ABYSSINICA).....................................lCRN

SHEET.... AA AA
BRIDGE2..
BRIDGE1.. AA AA
CHIRALITY +-t+++
--- + t + + t + + + ---+++++t+-
+ +----+-+-- -+tt
BEND.. SSSSSS sssssssss ssssssss s sss sss
5-TURN.. >5555 <
....
4-TURN.. >>>>x xxxx<<<< >>>>xx<<< <
3-TURN.. >3><3< >33< >>3<<
..
SUMMARY.. EE SSHHHH HHHHHHHTTT HHHHHHHH S EE SSS CGG
EXPOSURE. 8 2 8 8 5 5 * * 1 6 6819*29'*5 4876*81'*2 41583.48'5 58'778
1 SEQUENCE. T T a b P S I V A R SNFNVCRLPG T P E A I C A T Y T C b I I I P C A T a PGDYAN to
0-2
to
SUMMARY.. ..., . .H=ALPHA-HELIX.. .. E-BETA-STRAND.. . .B=BETA-BRIDGE.. . .C=3-HELIX.. .. I-5-HELIX.. . .T=3-, 4-, OR 5-TURN.. ..S=BEND.. .. 4
54) l O V 0 OVOMUCOID THIRD D O M A I N [PROTEINASE INHIBITOR, KAZAL] (JAPANESE QUAIL: COTURNIX COTURNIX JAPONICA) ............. lOV0
SHEET.. .. AAA BBB B B B 88
BRIDGE2.. ccc
BRIDGE1.. aaa BB B B c cc
CHIRALITY +----++++ +--+---+-+ -----+-+-- ---+++++++ +++--+++-+ --+-
BEND.. s ss sss sssssssss sssssss ss
5-TURN.. >5555<
....
4-TURN.. > > > > x x x x <<<<
3-TURN.. >33 < >33< >>3x<3<
..
SUMMARY.. EEE TT SS EEETTS E ESSHHHHHHH HHHTTTS E EEES
EXPOSURE. '96971582' 258'837.9' *300055'*6 5 5 1 8 0 6 0 0 2 2 12'374'171 779348
1 SEQUENCE. tAAVSVDaSE YPKPAbPKDY RPVCGSDNKT YSNKbNFaNA WGSNGTLTL NHFGKC
55) 2S S I STREPTOMYCES SUBTILISIN INHIBITOR [PROTEINASE INHIBITOR]. .................................................... .2SSI

SHEET.. , . AAAAAA B AAAACC cc D B AAAAAA
AAAAAA B D
BRIDGE2.. BBBB E CCCCCC
BRIDGE1.. AAAAA D BBBBFF FF g D AAAAA CCCCCC E g
CHIRALITY --+++---+ -+-+-+++-- +------++- +-++-+-+++ +++++++++- -+-+++---- -+----+-+- -----++--- -+--++++-- ---++++++-
BEND.. s sssss s s s S S S S s ssssssssss s ss s ss s s sss sssssssss
5-TURN.. > 5 5 5 5<
....
4-TURN.. >> >>xxxxx<<< < >>>><X<<
3-TURN.. >33< >33< >>><< < > 3 3 < > 33< >33<
..
SUMMARY.. EEEEEE B SSTTS SEEEEEE S S EESSTTH H H H H H H H H H H TS STTS SS B B EEEEEE TTEEEEEE BSBHHHHHHT
EXPOSURE. ' 4 8 2 4 2 5 1 3 0 0'0936'936 * * 8 5 2 5 1 5 2 4 '376491'42 47017717.3 6 2 6 1 9 6 2 + + 5 *f9'49*7*9 1110208223 *5**4*2*67 0 6 1 8 3 6 0 7 2 0
1 SEQUENCE. YAPSALVLTV GKGVSATTAA PERAVTLTaA PGPSGTHPAA GSAaADLAAV GGDLNALTRG EDVMbPMVYD PVLLTWGW WKRVSYERV FSNEbEMNAH
SHEET.. ..
BRIDGE2..
BRIDGE1..
CHIRALITY -++++
BEND.. SSSS
5-TURN..
....
(-TURN... 4<
3-TURN.. .
SUMMARY,. TSSSS
EXPOSURE. 2'11055
1 0 1 SEQUENCE. GSSYFM
56) 3 P TI TRYPSIN INHIBITOR [PROTEINASE INHIBITOR] [CCW PANCREAS: 80s TAURUS).................................... .......3 P TI
SHEET.. .. AAA AAAA A A AAAAA A
BRIDGE2.. B
BRIDGE1.. AAA AAAA A A AAAAA B
CHIRALITY -++++---- --+-+-+-+- ----++-+-- -+----++-- -+++-+-+++ +++++-
BEND.. SSSSS S sssss sss ss sssss ssssss
5-TURN.. >5555<
....
4-TURN.. >444< >>>> xx<<<<
3-TURN.. >>><<< >33<
..
SUPIMARY.. GGGGS S EEE EEEETTTTEE EEEEE S S S SS BSSHHH HHHHHS
EXPOSURE. '5.40'5'59 7295'5'6'5 72145'5482 88272842'5 ''822'33.8 07.5024.
1 SEQUENCE. RPDPaLEPPY TGWKARIIR WYNAKAGW QTFWGGbRA RRNNPKSAED cMRTaGGA
SUPIMARY...~~...H~ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIDGE....G~3-HELIX....I~5-HELIX....T-3 -,4-, OR 5-TURN....S-BEND....

l C T X A L P H A C O B R A T O X I N (COBRA: NAJA NAJA SIAMENSIS).................................................................lCTX
SHEET. +. A AMAA AAAM AAAAA
BRIDGE2.. BBBBB
BRIDGEl.. A AAAA BBBBB AAAAA
CHIRALITY --t-++--+ -++-++-t-- -+---+-ttt ++------+- +-+----+-+ +-+----+-+ +++----+-
BEND.. sssss sss sss sss ss s s s s s sss
5-TURN..
....
(-TURN,. >> 4 4 < <
3-TURN.. >33< >33x 33< > 3 3< >33<
..
SUMMARY.. sssss T T S E E E E E E T T H HHH E E E E E SS S S EEEEE T T S STT
EXPOSURE. 5*0253***9 5 5 9 5 7 . 1 ' 2 8 3240977**1 9 * * 4 4 * 5 6 0 0 345*83*7** 6 5 5 4 * 3 3 9 9 9 * 3 0 7 * 4 9 * 8 *
SEQUENCE. I R a F I T P D I T S K D b P N G H V a YTKTWCDAFC S X R G K R M L G bAA,TdPTVKT G M I Q d e S T D N e N P F P T R K R P
l M L T M E L I T T I N [ H E M O L Y T I C P O L Y P E P T I D E ] ( H O N E Y B E E VENOM: A P I S MELLIFERA) ........................................... .1MLT
SHEET.. ..
BRIDGEZ..
BRIDGE1..
CHIRALITY +++++++++ ++++++++++ ++++
BEND..... SSSSSSSS SSSSSSSSSS SSSS
5-TURN.. .
4-TURN... >>>>XXX<X< <>X>>XXXXX XX<<<<
3-TURN.. . >33<
SUMMARY.. HHHHHHHHH TTHHHHHHHH HHHHH
EXPOSURE. 9.3 671 **58 '4 387 72 7'3 a*****
SEQUENCE . G I G A V L K V L T T G L P A L I SW I KRKR QQ
l N X B N E U R O T O X I N B ( P R O B A B L Y = E R A B U T O X I N 8) ( S E A S N A K E : L A T I C A U D A S E H I F A S C I A T A ) .......................... ......... lNXB

SHEET.. .. AAA AAA BBBBBBB B BBBBBBB B BBBB
BRIDGE2.. cccc rn
BRIDGEl.. AAA AAA BBBBBBB B BBBBBBB B cccc M
CHIRALITY +-++---+- -+------++ ++-----+-+ -+------+- -------++- ++---+--++
BEND.. sss s ss ss ss ss sss
2
v
5-TURN..
.... Z
4-TURN..
3-TURN.. >33< >33 < >33< > 3 > < 3<
..
SUMMARY.. E E E STT S E E E TT E E E E E E E E T T E E E E E E E ES SS E E E E STTT T
EXPOSURE. B 6 0 2 5 1 8 5 9 * **69**17*8 7 6 2 0 3 4 3 9 8 7 6**3*21721 4 0 6 5 * 6 * * 6 5 * 4 7 5 4 * 6 9 3 3 0.
SEQUENCE. R I a F N Q H S S Q PQTTKTbSPG E S S a Y H K Q W S D F R G T I I E R G b G c P T V K P G I K L S C d E S E V d NN
2ADK A D E N Y L A T E K I N A S E I A T P - A M P P H O S P H M R A N S F E R A S E ] ( P O R C I N E M U S C L E : S U S S C R W A ] . . . . . . . . . . . . . . . . . . . . . . . . . . ........ .2ADR

SHEET., .. A AAM MAA A A M
BRIDGE2.. bbbb c ccc
BRIDGE1.. a aaa cccc a aaa
CHIRALITY ++++++--+ --++--++-+ ++++++++++ +-+---+-++++++++++-- -+++++++++ ++-+----++ ++++++++++ +++++++--- ---++++-++
BEND..... SSSSSS sss ssssssssss ss ss sssssssss sssssssss ssss ss ssssssssss sss ss s ss SSSS
5-TURN.. . > 5 5 55< >5555 < 4
4-TURN... >>>><<<< > 4 > > x > x x x < <<< > > > >xxxx<<<< >>>>xxxxx<<<< >>> >xxxxxxxxx <<x<44< >
3-TURN., >33 < >33 < >33c E
SUMMARY.. HHHHHHS E E E E E SSTT TTHHHHHHHH H T E E E E H H HHHHHHHHS HHHHHHHHH H H S S HH HHHHHHHHHH H H H T T T S E EEES SSSS
EXPOSURE. 9***2**240 1 0 3 2 1 1 4 2 4 2 '3651.926. '543362488 923.429974 3940*883*2 5**6**554* 131812*921 77*4**2*00 1 1 2 4 2 1 * * 7 '
SEQUENCE. M E E K L K K S K I I F W G G F G S G K G T W E K I V Q KYGYCHLSTG D L L R A E V S S G S A R G K H L S E I MEKGQLVPLE T V L M L R D A M VAKWTSKGF LIDGYPREVK N
Ga
N
SUMMARY. .......HFALPHA-HELIX....E=BETA-STRAND....BIBETA-BRIDGE. ...GL~-HELIX....I-~-HELIX....T-~ -,4-, OR 5-TURN. ...S-BEND. CD
TABLE A111 (continued) E3
03
0
SHEET.. .. AAAAA A AAA 0
BRIDCE2.. dddd
BRIDCEl.. bbbb d ddd
CHIRALITY +++++++-++ --+-----+- -+++++++++ +++++-++-+ ++++++++++ ++++++++++ ++++++-+++ ---+++--++ ++++++++++ ++
BEND.. SSSSSSSSS S sssssssss ssssss ssssssss ssssssssss ssssssss s ss ssssssssss s s
5-TURN.. >5555< >5555< > 5.5.5.
5_<
....
4-TURN... >>>XX<<<< >>>>xxxxx<< x < 4 4 < >>>>xxxxxx x x x < < x < > >x > x x < < < < >>> >xxxxxxxxx <<<<
)-TURN... >33< > >3<x33< >33< >33 < >33<
SUMMARY,. HHHHHHHHS SEEEEE HHHHHHHHH HHTTTT H H H H H H H H HHHHHHHTTH HHHHHHHS E E E E S HH HHHHHHHAHH HHH
EXPOSURE. 4 0 5 2 0 6 * 8 2 0 8 2 5 2 8 5 6 3 7 1 2**316*'1* *94'*46*8* 86**52***4 "636'31980 1 2 * 2 7 * * 3 6 5 7'2'4'699. 7347524943 *+2*
1 0 1 SEQUENCE. Q C E E F E R K I G QPTLLLYVDA GPETnTKRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEXRGIV RKVNAEGSW DVFSQVCTHL DTLK
61) l R H D RHODANESE [THIOSULFATE-CYANIDE SULFURTRANSFERASE] (CCW LIVER: BOS TAURUS) , , .......I). l R H D

.. ........ .... . . ......
SHEET.. .. AA A AAA B B c BB AAAA
BRIDGE2.. ccc ddd
BRIDCE1.. aa b b ee F ee ccc
CHIRALITY ++---++-- -+++++++++ -+++-++--+ -++++--++- -+++++++++ ---+-----+ +++--++-+- ++++++-+-- ++---++--+
-+----++++
BEND.. sssssssss s sss sss ssssssss ss s ssss s sss s ssss ssssssss sss
5-TURN.. >55 55x5555<
....
4-TURN.. >>>>xxxx<<<< >444 <>>>4x<<4< > > > > xx<x<<4<
3-TURN.. > 3 3 x 3 3< >33< >33< > 3 3< > 3 3 < > 33<>>3<< > 33<
..
SUMMARY.. E E H H H H H H H H H HT BTTTEEE EE TTT HHHHHTTS B TT EE T TSSS TTSSS S H H H H HHHHGGGS TTSEEEE
EXPOSURE. * * * + 7 5 * 1 5 1 51'801*13* 75'51'4141 0 1 0 1 6 3 4 ' 9 9 7*1'*729** 0 0 3 4 0 2 3 0 5 1 9'077'83'4 5 2 2 2 2 7 ' 7 3 8 1'50882084 6 * 0 2 0 0 8 1 0 2
1 SEQUENCE. VHQVLYRALV STKWLAESVR AGKVGFGLRV LDASWYSPGT REARKEYLER HVPGASFFDI EECRDKASPY EWLPSEAGF ADYVGSLGIS NDTHWWNG
SHEET.. .. AAAA C DD DDDD

BRIDGE2.. ddd il
BRIDGEl.. aa F 99 hhhh
CHIRALITY -+-+++++++ +++++++-+- +++---+--+ +++++-+--- -+--+---+- ---+---+++ +--+++++++ ++-++--+-- +--++++-++ ---++--+--
BEND.. ssss sssss ssssssss ss s ssssss sss sssssss sss s s ssssss s ss ss
5-TURN.. >5555< >5555<
....
4-TURN.. >>>> xxxx<<<< >>> >xx<<<< >4>>x4xx <4<< >>>4c<<
3-TURN.. >33< >>3x<3< >33< >33< >33x33<
..
SUMMARY,. STTS SSHHH HHHHHHHT EEEETTHH HHHHHHT B TTS EE TTHHHHH H H H SEEEE S HHHHHT s'.17*5*737 ss ss
EXPDSURE. 2 * 5 0 1 6 1 0 0 0 8 0 0 1 0 3 0 0 5 1 ' 3 0 0 0 1 4 8 0 2 8 2 0 8 * 8 5 5 7 6 4 9 * * 2 * 4 * 8 4 * 1 * 1 9 7 6 * 7 1 3353'506'1 5 * 7 * * 4 5 2 0 0 012'25471'
181 SEQUENCE. DDLCSFYAPR VWWnFRWGH RTVSVLNGGF RNWLKEGHPV TSEPSRPEPA IFKATLNRSL LKTYEQVLEN LESKRFQLVD SRASRYLGT QPEPDAVGLD
SHEET.. .. E DD F F DDDD E
2 2 ??
BRIDGE2.. JJ
-J J_
BRIDGEI.. K il L L hhhh 4 4 K
CHIRALITY +---++--+- -++++--+-+ ----++++++ ++++-+--++ ----++---+ ++++++++++ ++-++++--- -+--++++++ +--+++-+-+
BEND.. ss sssss sss ssssss ssssss ss s sss ssssssssss ssss ss ssssss ss ssss s S
5-TURN.. >5555< > 5555<
....
4-TURN.. > > 4 > x x > x<<<< >>>>xxxx <<<< > > > > x < <<<
3-TURN.. >33< >3><3<>33< >33< >>3<< >33 < >3><3< > 33< > 3 3 < >3>X3<X33< >>3<<
..
SUMMARY.. B TT EE TTTTB TTS B HHHHHH HHHHTT TT S EEEE SSS STTHHHHHHH HHHT TT EE ETTTHHHHHH HS GGGSB S S
EXPOSURE. 1 8 3 0 * 6 1 5 2 8 2 2 9 7 0 1 4 ' 9 8 5 2 5 3 8 * 8 0 * 5 4 0 * 8 8 * 1 6 4 + ' 6 8 0 0 0 8 2 4 8 0180080000 1 5 4 5 1 1 8 8 8 8 810083204* *167*2353* 5 * *
2 8 1 SEQUENCE. SGH IRGSVNM P F M W LTENG F EKS PE ELRA MFEAKKVDLT KPLIAXRKG VTACHIALAA YLCGKPDVAI YDCSWFEWFH RAPPEWVSQ G KG
62) 2PAB PREALBUMIN [THYROXIN, RETINQL TRANSPORT] (HUMAN PLASMA).....r......................,.......................,..2PAB
SHEET.... AAAAAAA AA B BBBBBB BBB BBBB AA BBB BBBB BBBBBBB AAAAA
BRIDGEZ.. BB cc FFFFF GGG GGGG DDDDD
BRIDGEI.. aaaaaaa CC E EEEEEE EEE EEEE BB F FFFF CGGGGGG aaaaa
CHIRALITY ++------+ +-+---++-- -------+-+ ---+--+--- -+-+-+++-- -++++-+--- ----++++++ ++-+--+-- ----+--+++ -___-___--
BEND.. s ssss s sss s sss s ssss ss ssss ssss s s s ss
5-TURN.. > 5 555< > 5555<
....
4-TURN.. > 4 44< r444i >>>>xx ::::
j-TURN.. >33< >33< >33< > >3<<
..
SUMMARY.. EEEEEEET TTTEE S E EEEEEE TTS SEEEEEEEE TTSEE S TTTS SEEE EEEE HHHHH HHHT S S EEEEEEE S SS EEEEE
EXPOSURE. 6284888785 8.74486'81 0704761"'* 99'*4282*8 5'68418822 B"'16'160 3050515630 '"77693'5' 789274783. *3'2'34040
1 SEQUENCE. CPLMVKVLDA VRGSPAINVA V H W R K A A D D TWEPFASGKT SESGELHGLT TEEQFVEGIY KVEIDTKSYW KALGISPFHE HAEVVFTAND SGPRRYTIAA
SHEET.... AAA AAAAA hAA
BRIDCE2.. DDD m
BRIDGEI.. aa DDDDD DDD 0
CHIRALITY -+-+++--+- -- 0
BEND..... SS
5-TURN.. 3
4-TURN..
..
3-TURN.. . >33<
SUMMARY.. EEETTEEEEE EEE
EXPOSURE. 7843*7866e 799'
101 SEQUENCE. LLSPYSYSTT AVVT
SUMMARY........H~ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIDCE....G~3-HELIX....I~5-HELIX....T~3-,4-r OR 5-TURN....S-BEND....
i
, 1 1 1 , 1 1 1 1 , 1 1 1 1 ~ 1 1 1 1 ~ 1 1 1 ,1 I l l
100 20 0 300 N
...................................................... Q,
1 CPU Hllyly.......:::ym.
.......lllw........ .......lywy......:::w.............. w
N
.................................. ................................
lRBP ........:.......w w ............ymrmw...... ......UwyMYwH...-., ....... ................
....
......
.........................................................
1HIP ...........IIHH..:..HI..H......rn..~~:..:: .........::::......j: ...:.....:... 11-14)
.................................................
156B ~ l m l..............
. . I H H ...........
...........................................................
lCYT ..IIIHWI(R......................... :..........W(II,,,:..H~IWII.M
.............llmllllll
................................................................
.......:..................... :...w.......................... IIUIHHIHH..
.............................................................
....................................
1FDX ..::..........w( .....:......:......... .....::...
.....................................................................
1 FXC ..................................................................................................
L I 1 I I 1 I 1 1 ~ ~ I ~ ~ ~ 1 ~ I ~ I ~
Fig. A l . Strip maps of secondary structure and solvent exposure for 62 proteins. Top line dots: residues with more than three contacting water molecules.
Vertical bars: short, 3-helix; medium, 4-helix (a-helix);long, 5-helix. Dots above baseline: residue has antiparallel /3-bridge partnerb). Dots below baseline:
P-strand has parallel /3-bridge partner(s). The four-letter code is the Protein Data Bank data set identifier (Table AI).
I , r , , , , r , l ' ' ' " ' ' ' ~ 1 I I I I I I I '
N
100 20 0 30 0 Q,
........ ,..... ............................ ..................... w
P
21LN ",.wHyYryI ....... ......::....:.........::...M...... ......yy .....yyyy
......
2GCH 27) 39) -

1ALP
1PTN
............... T
1SGA
.......................
lSB1
lEST
..................................................................
2RCT
ePAP
.................... .......................... ............................
lFAB ..................................
............ HI.:
....................................
lREI
...................................................................... ..............................
3PGfl
................... ."." .......... ....................................
lTIfl ............
..... :...#NHHrm. ......... ?..UyHIk ................:....... ...::::. y .......-.m .::::....... ........::m.
L 1 I I 1 I I I I I 1 I 1 I I 1 I I 1 I I I I I 1 1 I I
Fig. A1. (continued from the preuious page)

.........................................................................................................................
......
3CNR ................. ......... .......................................
......................................................................................................... 40) 50) -
1CRC
1 DFR
1 GPD
.... .....
..:::::.....Y.._l__
...........
4RDH ...........
.....yI......... .....
.... ,.Iyyy) .................. .....+::.
....
.................................................................................................
4LDH ) ....y:.-
........, ....
................................... . .
2GRs ..................................................
. . ...... . .
............................ ........................
...w...w .........E...
.................
2SOD .......*...:................... v,
............................................................................................
1 nBp( ...~..~.*)...~'..... yy....._._..I........____........I..... I.
.......................... ........................................
1 ECD .,- .... .........)." ....yyc..."'.-.
.......................................................................................................................................................
2fWB ---
I I I I 1 1 I 1 1 I I l 1 I I I l I L I I I L L I l N
a
w
Fig. A l . (continued from the previous page) wl
10
Q,
w
Q,
I r r r , I
l " " l " ' ' l " ' ' ~ ' r ' l ~
100 20 0 30 0
.......................................................................................
lLHB . w~ ............
............~ . . ~ . . ........ ~ Hmmylw....... ......vmyywl...... ywIwm.
................................................................................................ 51) -62)
lHBL
1 CRN
...................................
low0 ...................... ......:.::...
:::....::..IIIHH(II
........................ .......
2.5s I ....llHHlHll..................... ..#rm ........
x
3PT I
......................................
1CTX
1nLT ~IlW~.W#wnrrm~
1 NXB
2RDK
................... ......................... ......................... ...............
1 RHO ..................ry*l.........:..........IIy.....::I'
2PRB
L I L 1 I I L I I I ~ ~ l I l ~ ~ I ~ ~ ~ ~ ~
Fig, A l . (continued from the previous p a g e )

For reasons of space it is impossible to cite the tremendous amount of work by the crys-
tallographers on which this paper is based; references for each structure are in the Protein
Data Bank. C. Oefner provided computer graphics software. The Deutsche Forschungs-
gemeinschaft gave financial support to the project Protein Structure Theory.
References
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2. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers,
J. R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977) J Mol. Biol. 112,535-542.
3. Kuntz, I. (1972) J. Am. Chem. SOC. 94,4009-4012.
4. Lewis, P. N., Momany, F. A. & Scheraga, H. A. (1973) Biochim. Biophys. Acta 303,
211-229.
5. Rose, G. D. & Seltzer, J. P. (1977) J. Mol. Biol. 113,153-164.
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Inc., Rockville, Md.
13. Lifson, S., Hagler, A. T. &Dauber, P. (1979) J . Am. Chem. Soc. 101,5111-5121.
14. IUPAC-IUB Commission on Biochemical Nomenclature (1970) J. Bid. Chem. 245,
6489-6497.
15. Rackovsky, S. & Scheraga, H. A. (1978) Macromolecules 11,1168-1174.
16. Shrake, A. & Rupley, J. A. (1973) J . Mol. Biol. 79,351-371.
17. Chothia, C. (1975) Nature 254,304-308.
18. Bode, W., Schwager, P. & Huber, R. (1975) Proceedings of the 10th FEBS Meeting,
Vol. 40, Desnuelle P. & Michelson A. M., Eds., North-Holland, Amsterdam, pp. 3-20.
19. Finney, J. L. (1979) in Water, A Comprehensiue Treatise, Vol. 6, Franks F., Ed., Plenum
Press, New York, p. 93.
20. Brant, D. A,, Miller, W. G, & Flory, P. J. (1967) J. Mol. Biol. 23,47-65.
21. Schellman, C. (1980) in Protein Folding, Jaenicke, R., Ed., Elsevier, Amsterdam, pp.
53-61.
22. Provencher, S. W. & Gloeckner, J. (1981) Biochemistry 20,33-37.
23. Williams, R. W. & Dunker, A. K. (1981) J . Mol. Biol. 152,783-813.
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25. Deisenhofer, J. & Steigemann W. (1975) A C ~Crystallogr.,
Q Sect. B 31,23%250.
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27. Timkovich, R. & Dickerson, R. E. (1976) J. Bid. Chem. 251,4033-4046.
28. Schulz, G. E., Elzinga, M., Marx, F. & Schirmer, R. H. (1974) Nature 250,120-123.
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30. Diamond, R. (1966) A C ~ Crystallogr.,
Q Sect. A 21,253-266.
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R., Ramaseshan, S. & Venkatesan, K., Eds., Indian Academy of Sciences, Bangalore, pp.
13.01-13.23.
33. Dodson, E. J., Isaacs, N. W. & Rollett, J. S. (1976) A C ~ Q Crystallogr., Sect. A 32,
311-315.
34. Jack, A. & Levitt, M. (1978) Acta Crystallogr., Sect. A 34,931-935.
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Q Sect. A 34,791-809.
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Sect. A 33,800-804.
Received December 22,1982

Accepted May 12,1983

Dictionary of Protein Secondary Structure Pattern Recognition

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Dictionary of Protein Secondary Structure Pattern Recognition

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Dictionary of Protein Secondary Structure:

Pattern Recognition of Hydrogen-Bondedand

WOLFGANG KABSCH and CHRISTIAN SANDER, Biophysics

Biopolymers, Vol. 22,2577-2637 (1983)

proach has the advantage of giving assignments when only backbone Ca

The Main Ideas

Hbond(ij)=: [E < -0.5kcal/mole] means: there is an H bond (ij)if

Fig. 2. Elementary patterns used in structure definition

more complicated description of H bonds in terms of one distance and one

Elementary H-Bond Pattern: n-Turn

Elementary H-Bond Pattern: Bridge

Cooperative H-Bond Pattern: Helices

Fig. 5. Stereoviews of secondary structure: illustration of chirality. This short left-handed

Static Solvent Exposure

RESULTS AND DISCUSSION

Ladders per sheet

Hydrogen Bond Type

:L Length of R-Ladder tontiporallel I

H bonds with n = +3,+4,+5 are reported as turns or helices. Most (i,i

is steric hindrance, e g , in an (i,i - 4) helix between the backbone oxygen

Accuracy of H-Bond and Secondary Structure Assignments

give a minimal set of 41 backbone-backbone H bonds. We assign all of

Secondary Structure Size

to a maximum segment length of about 30 A, with parallel &ladders slightly

APPENDIX DICTIONARY OF PROTEIN SECONDARY

136 1.4 DS 491 IECD HEXOGLOBIN (ERYTHROCRUORIN DEOXY)

46 1.5 HK 5 3 1 ICRN CR.438111

- b,??i C c I f , . . are Cys residues labeled by their SS-bond name. !

2) lABP L-ARABINOSE-BINDING PROTEIN (BACTERIAL: ESCHERICHIA COLI).....................................................lABP

8) 155C CYTCCHROME C 550 [ELECTRON TRANSPORT] (PARACOCCUS DENITRIFICANSI.. ............................................. 155C

13) 2RXN R U B R E D O X I N ( O X I D I Z E D , F E ( I I 1 ) ) [ E L E C T R O N T R A N S P O R T ] ( C L O S T R I D I U M P A T E U R I A N u n ) . . ................ ...... .2RXN

141 1 A Z U A Z U R I N [ E L E C T R O N T R A N S P O R T , C O P P E R B I N D I N G ] (PSEUDOMONAS AERUGINOSA)..........................................lAZU

SHEET.. .. BBBB BB BBBB

1 P P T A V I A N P A N C R E A T I C P O L Y P E P T I D E [HORMONE] [ T U R K E Y P A N C R E A S : M E L E A G R I S G A L L O P A V O ) . ................................ lPPT

1 I N S I N S U L I N ( A AND B C H A I N ) [HORMONEI I P I G : SUS S C R C F A I .......................................................... .1INS

SUMMARY........H=ALPHA-HELIX....E~BETA-STRAND..~~B~BETA-BRIDGE....G-J-HELIX....I=5-HELIX....T~3 -,4-, OR 5-TURN....S=BEND....

20) lLZM LYSOZYME [O-GLYCOLSYL HYDROLASE] [BACTERIOPHAGE T 4 ) . ,

lSNS STAPHYLOCOCCAL NUCLEASE ICWPLEX) [PHOSPHORIC DIESTER ( D N A ) HYDROLASE] (STAPHYLOCOCCUS AUREUS)

SHEET.... AAAAA BBBB B B B B B B

SHEET.. .. DDG G BBB I1 I I11 J K LL

SU~MARY ........H~ALPHA-HELIX....E~BETA-STRAND....B~BETA-BRIDGE....G~3-HELIX....I=5-HELIX....T~3 -,4-, OR 5-TURN....S=BEND.. ..

SHEET.. .. P KKK KKK PJ

26) l A P P A C I D PROTEINASE, PENICILLOPEPSIN [HYDROIASE: PROTEINASE] (FUNGUS: PENICILLIUM JANTHINELLUM] ...,.......,.......lAPP

3-TURN.. . >33< >33< >33< >33 < >33< >33< >33<

SHEET.. .. cccc cc c ccc C A BBBBB BBBBB E B BBB F G GGGG

SHEET.. .. I BBB B BBBB IE

27) ZTLN THERMOLYSIN [HYDROLASE: NEUTRAL METALLO-PROTEINASE] (BACILLUS THERMOPROTEOLYTICUS)............................ZTLN

SHEET.. .. CCC B B BBBBB 888 BBBB BBBBB A B BBBBB BBB

SHEET.... CCCC CCC C C CC C CC CC CCCC E CCC D CCC C C E cc ccc BS

SUMMARY. ....... H-ALPHA-HELIX. ...E-BETA-STRAND ....B~BETA-BRIDGE....G~3-HELIX....I-5-HELIX....T=3 -,4-, OR 5-TURN....S-BEND....

SHEET.... EEEEEC C C CC cc cccc C E EEE EE C CC F F CCC BB

SHEET.. .. B B BBB B G G H H BBBBB

SHEET.. .. E AAAA AAAAA AA AAAAA AAA AA AAAAAA A B A AAAAA

SHEET.... B c cc cccc ccc DDDDD D CCC CC CCC CCCCC DDDD DD DDDD

SHEET..,. DD EEEEE F F EEEE EEEE GGGGGGG GG GGG G GGG EEEE EEEE E G v1

SHEET.... GGGGGGG GG G GGFF H I J JJJJJI J H KKKK J JJ JJ J J J J J

SUMMARY........H=ALPHA-HELIX....E=BETA-STRAND....B=BETA-BRIDGE....G=3-HELIX....I=5-HELIX....T=3 -,4-, OR 5-TURN....S=BEND....

37) l R E I BENCE-JONES IMMUNOGLOBULIN VARIABLE PORTION ( R E 1 1 (HUMAN). .................................................... 1REI

SHEET.. .. AAAAAAA AA AAAAA

SHEET.. . BB BB BBBBB BBBBBBB A AAAA BB BB A AAAAA CC BB BBBBBBBB

SHEET.. , . AA A BBBBBBBB B BBBB BBBBBBB BB B BB BB

SHEET.. .. BBBBB BBBB C C BB

43) lGPD D-GYCERALDEHYDE-3-PHOSPHATE DEHYDRCGENASE [OXIDOREDUCTASE: ALDEHYDE/DONR,NAD/ACCPTR] (LDBSTER: HIMARUS AMERICAlGPD