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PDBsum entry 1uwa

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1uwa
Jmol
Contents
Protein chains
(+ 2 more) 465 a.a.
(+ 2 more) 140 a.a.
Ligands
CAP ×8
EDO ×59
Metals
_MG ×8
Waters ×2310
HEADER    LYASE                                   03-FEB-04   1UWA
TITLE     L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, B, E, H, K, O, R, V;
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT, RIBULOSE-1,5 BISPHOSPHATE
COMPND   5  CARBOXYLASE LARGE CHAIN;
COMPND   6 EC: 4.1.1.39;
COMPND   7 MUTATION: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;
COMPND  10 CHAIN: I, C, F, J, P, T, M, W;
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT 1;
COMPND  12 EC: 4.1.1.39
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE   3 ORGANISM_TAXID: 3055;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE   6 ORGANISM_TAXID: 3055
KEYWDS    LYASE, RUBISCO, PHOTOSYNTHESIS, PHOTORESPIRATION,
KEYWDS   2 OXIDOREDUCTASE, MONOOXYGENASE, CARBON DIOXIDE FIXATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KARKEHABADI,T.C.TAYLOR,R.J.SPREITZER,I.ANDERSSON
REVDAT   3   16-JUN-09 1UWA    1       REMARK
REVDAT   2   24-FEB-09 1UWA    1       VERSN
REVDAT   1   12-JAN-05 1UWA    0
JRNL        AUTH   S.KARKEHABADI,T.C.TAYLOR,R.J.SPREITZER,I.ANDERSSON
JRNL        TITL   ALTERED INTERSUBUNIT INTERACTIONS IN CRYSTAL
JRNL        TITL 2 STRUCTURES OF CATALYTICALLY COMPROMISED
JRNL        TITL 3 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE
JRNL        REF    BIOCHEMISTRY                  V.  44   113 2005
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15628851
JRNL        DOI    10.1021/BI047928E
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2
REMARK   3   NUMBER OF REFLECTIONS             : 189087
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172
REMARK   3   R VALUE            (WORKING SET) : 0.171
REMARK   3   FREE R VALUE                     : 0.205
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 10114
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13282
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280
REMARK   3   BIN FREE R VALUE SET COUNT          : 700
REMARK   3   BIN FREE R VALUE                    : 0.2730
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 38016
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 747
REMARK   3   SOLVENT ATOMS            : 2310
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.93
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.73000
REMARK   3    B22 (A**2) : -0.14000
REMARK   3    B33 (A**2) : -1.30000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.30000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.517
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.225
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.259
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 39675 ; 0.012 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 53695 ; 1.235 ; 1.952
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4842 ; 6.004 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5675 ; 0.089 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30556 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 19282 ; 0.195 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  2741 ; 0.133 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     8 ; 0.078 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   127 ; 0.457 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.357 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 24130 ; 1.029 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38687 ; 1.981 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 15545 ; 3.086 ; 6.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15002 ; 4.364 ; 8.000
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B E H K O R V
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     12       A     477      1
REMARK   3           1     B     12       B     477      1
REMARK   3           1     E     12       E     477      1
REMARK   3           1     H     12       H     477      1
REMARK   3           1     K     12       K     477      1
REMARK   3           1     O     12       O     477      1
REMARK   3           1     R     12       R     477      1
REMARK   3           1     V     12       V     477      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    E    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    H    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    K    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    O    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    R    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    V    (A):   3612 ;  0.04 ;  0.05
REMARK   3   TIGHT THERMAL      1    A (A**2):   3612 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):   3612 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    E (A**2):   3612 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    H (A**2):   3612 ;  0.14 ;  0.50
REMARK   3   TIGHT THERMAL      1    K (A**2):   3612 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    O (A**2):   3612 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    R (A**2):   3612 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    V (A**2):   3612 ;  0.13 ;  0.50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : I C F J P T M W
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     I      1       I     140      1
REMARK   3           1     C      1       C     140      1
REMARK   3           1     F      1       F     140      1
REMARK   3           1     J      1       J     140      1
REMARK   3           1     P      1       P     140      1
REMARK   3           1     T      1       T     140      1
REMARK   3           1     M      1       M     140      1
REMARK   3           1     W      1       W     140      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    I    (A):   1120 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    C    (A):   1120 ;  0.05 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    F    (A):   1120 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    J    (A):   1120 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    P    (A):   1120 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    T    (A):   1120 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    M    (A):   1120 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   2    W    (A):   1120 ;  0.04 ;  0.05
REMARK   3   TIGHT THERMAL      2    I (A**2):   1120 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      2    C (A**2):   1120 ;  0.10 ;  0.50
REMARK   3   TIGHT THERMAL      2    F (A**2):   1120 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      2    J (A**2):   1120 ;  0.11 ;  0.50
REMARK   3   TIGHT THERMAL      2    P (A**2):   1120 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      2    T (A**2):   1120 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      2    M (A**2):   1120 ;  0.10 ;  0.50
REMARK   3   TIGHT THERMAL      2    W (A**2):   1120 ;  0.11 ;  0.50
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1UWA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  03-FEB-04.
REMARK 100 THE PDBE ID CODE IS EBI-14497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-MAY-03
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : MAX II
REMARK 200  BEAMLINE                       : I711
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.089
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 264805
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6
REMARK 200  DATA REDUNDANCY                : 22.400
REMARK 200  R MERGE                    (I) : 0.14000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES PH 7.5, 8-12% PEG 4
REMARK 280  50 MM NAHCO3, 5 MM MGCL2, 50 UM 2-CABP, 18 DEG C,
REMARK 280  10-15 MG PROTEIN
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       88.85450
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE:  1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE:  1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 131860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 117680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -432 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, H, I, J
REMARK 350                    AND CHAINS: K, M, O, P, R, T, V, W
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400  ENGINEERED MUTATION LEU 290 PHE IN
REMARK 400  CHAINS A, B, E, H, K, O, R AND V.
REMARK 400
REMARK 400  RUBISCO CATALYZES TWO REACTIONS: THE CARBOXYLATION OF D-
REMARK 400  RIBULOSE 1,5-BISPHOSPHATE, THE PRIMARY EVENT IN
REMARK 400  PHOTOSYNTHETIC CARBON DIOXIDE FIXATION, AS WELL AS THE
REMARK 400  OXIDATIVE FRAGMENTATION OF THE PENTOSE SUBSTRATE IN THE
REMARK 400  PHOTORESPIRATION PROCESS. BOTH REACTIONS OCCUR SIMULTANEOUSLY
REMARK 400  AND IN COMPETITION AT THE SAME ACTIVE SITE.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     VAL A     2
REMARK 465     PRO A     3
REMARK 465     GLN A     4
REMARK 465     THR A     5
REMARK 465     GLU A     6
REMARK 465     THR A     7
REMARK 465     LYS A     8
REMARK 465     ALA A     9
REMARK 465     GLY A    10
REMARK 465     MET B     1
REMARK 465     VAL B     2
REMARK 465     PRO B     3
REMARK 465     GLN B     4
REMARK 465     THR B     5
REMARK 465     GLU B     6
REMARK 465     THR B     7
REMARK 465     LYS B     8
REMARK 465     ALA B     9
REMARK 465     GLY B    10
REMARK 465     MET E     1
REMARK 465     VAL E     2
REMARK 465     PRO E     3
REMARK 465     GLN E     4
REMARK 465     THR E     5
REMARK 465     GLU E     6
REMARK 465     MET H     1
REMARK 465     VAL H     2
REMARK 465     PRO H     3
REMARK 465     GLN H     4
REMARK 465     THR H     5
REMARK 465     GLU H     6
REMARK 465     MET K     1
REMARK 465     VAL K     2
REMARK 465     PRO K     3
REMARK 465     GLN K     4
REMARK 465     THR K     5
REMARK 465     GLU K     6
REMARK 465     MET O     1
REMARK 465     VAL O     2
REMARK 465     PRO O     3
REMARK 465     GLN O     4
REMARK 465     THR O     5
REMARK 465     GLU O     6
REMARK 465     MET R     1
REMARK 465     VAL R     2
REMARK 465     PRO R     3
REMARK 465     GLN R     4
REMARK 465     THR R     5
REMARK 465     GLU R     6
REMARK 465     THR R     7
REMARK 465     LYS R     8
REMARK 465     ALA R     9
REMARK 465     GLY R    10
REMARK 465     MET V     1
REMARK 465     VAL V     2
REMARK 465     PRO V     3
REMARK 465     GLN V     4
REMARK 465     THR V     5
REMARK 465     GLU V     6
REMARK 465     THR V     7
REMARK 465     LYS V     8
REMARK 465     ALA V     9
REMARK 465     GLY V    10
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ASN C 136    CG   OD1  ND2
REMARK 470     LYS C 137    CG   CD   CE   NZ
REMARK 470     ARG F 130    CD   NE   CZ   NH1  NH2
REMARK 470     LYS F 137    CD   CE   NZ
REMARK 470     LYS I 127    CG   CD   CE   NZ
REMARK 470     ARG I 130    CD   NE   CZ   NH1  NH2
REMARK 470     ASN I 136    CG   OD1  ND2
REMARK 470     LYS I 137    CG   CD   CE   NZ
REMARK 470     LYS J 137    CG   CD   CE   NZ
REMARK 470     LYS M 127    CD   CE   NZ
REMARK 470     LYS M 137    CD   CE   NZ
REMARK 470     LYS P 127    CG   CD   CE   NZ
REMARK 470     LYS P 137    CG   CD   CE   NZ
REMARK 470     LYS T 127    CD   CE   NZ
REMARK 470     ARG T 130    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS T 137    CD   CE   NZ
REMARK 470     LYS W 127    CD   CE   NZ
REMARK 470     LYS W 137    CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OG1  THR A   471  -  O    HOH A  2241              2.11
REMARK 500   OG1  THR B   471  -  O    HOH B  2241              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500
REMARK 500   CE   LYS H    14     OE1  GLU R   460     1547      2.00
REMARK 500   OE1  GLU R   460     CE   LYS H    14     1557      2.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP B  33   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP B 160   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG C 138   CD  -  NE  -  CZ  ANGL. DEV. =  13.9 DEGREES
REMARK 500    ARG C 138   NE  -  CZ  -  NH1 ANGL. DEV. = -10.5 DEGREES
REMARK 500    ARG C 138   NE  -  CZ  -  NH2 ANGL. DEV. =  10.2 DEGREES
REMARK 500    ASP E 203   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP H 203   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP H 397   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP M 131   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP O 203   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP R  33   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP R 352   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP V  33   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP V 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP W 131   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  62      -83.43   -143.79
REMARK 500    THR A  75     -166.22   -125.79
REMARK 500    CYS A 172      128.15   -172.12
REMARK 500    ASN A 207      -95.07   -124.30
REMARK 500    MET A 212      109.57   -161.12
REMARK 500    ALA A 296      128.94    -36.81
REMARK 500    MET A 297      -11.86     90.84
REMARK 500    VAL A 331      -53.42     67.20
REMARK 500    ASP A 357       90.93   -161.50
REMARK 500    THR A 406      -57.80   -120.74
REMARK 500    SER B  62      -82.04   -140.28
REMARK 500    THR B  75     -164.53   -123.72
REMARK 500    CYS B 172      127.24   -171.28
REMARK 500    ASN B 207      -97.97   -121.57
REMARK 500    MET B 212      110.53   -161.37
REMARK 500    ALA B 296      128.12    -37.40
REMARK 500    MET B 297      -13.12     91.75
REMARK 500    VAL B 331      -53.48     68.42
REMARK 500    ASP B 357       91.15   -164.34
REMARK 500    GLU C  13     -143.34     60.75
REMARK 500    PHE C  15       -6.41     83.77
REMARK 500    LYS C  77     -125.59     58.27
REMARK 500    SER E  62      -80.28   -142.30
REMARK 500    THR E  65     -168.87   -127.30
REMARK 500    THR E  75     -165.98   -124.06
REMARK 500    CYS E 172      124.45   -172.32
REMARK 500    ASN E 207      -97.30   -121.33
REMARK 500    MET E 212      106.75   -167.07
REMARK 500    TYR E 239       99.94    -68.70
REMARK 500    MET E 297      -13.77     87.63
REMARK 500    VAL E 331      -54.17     69.94
REMARK 500    ASP E 357       88.14   -164.19
REMARK 500    GLU F  13     -140.85     60.24
REMARK 500    PHE F  15       -4.43     83.53
REMARK 500    LYS F  77     -127.14     56.38
REMARK 500    SER H  62      -79.79   -140.58
REMARK 500    THR H  65     -167.28   -127.59
REMARK 500    THR H  75     -163.73   -123.66
REMARK 500    CYS H 172      126.55   -175.15
REMARK 500    ASN H 207      -93.95   -121.05
REMARK 500    MET H 212      108.59   -161.96
REMARK 500    MET H 297      -12.68     86.69
REMARK 500    VAL H 331      -54.61     66.83
REMARK 500    ASP H 357       92.01   -163.41
REMARK 500    GLU I  13     -142.92     60.36
REMARK 500    PHE I  15       -2.47     80.88
REMARK 500    LYS I  77     -125.87     58.32
REMARK 500    PHE J  12       46.74   -140.28
REMARK 500    GLU J  13     -142.92     59.98
REMARK 500    PHE J  15       -3.14     82.98
REMARK 500    LYS J  77     -125.95     59.30
REMARK 500    SER K  62      -78.56   -142.36
REMARK 500    THR K  75     -163.69   -123.72
REMARK 500    CYS K 172      126.99   -171.53
REMARK 500    ASN K 207      -95.45   -119.12
REMARK 500    MET K 212      108.71   -164.22
REMARK 500    MET K 297      -12.93     89.40
REMARK 500    VAL K 331      -53.87     70.48
REMARK 500    ASP K 357       91.30   -162.80
REMARK 500    PHE M  12       47.92   -140.46
REMARK 500    GLU M  13     -139.74     58.52
REMARK 500    PHE M  15       -4.15     81.20
REMARK 500    LYS M  77     -125.46     53.49
REMARK 500    SER O  62      -77.37   -141.86
REMARK 500    THR O  65     -169.37   -126.76
REMARK 500    THR O  75     -165.54   -123.40
REMARK 500    CYS O 172      124.92   -171.67
REMARK 500    ASN O 207      -95.70   -122.75
REMARK 500    MET O 212      105.30   -161.04
REMARK 500    TYR O 239       99.55    -67.48
REMARK 500    MET O 297      -10.88     88.61
REMARK 500    VAL O 331      -52.83     69.62
REMARK 500    ASP O 357       90.10   -162.36
REMARK 500    GLU P  13     -142.58     62.02
REMARK 500    PHE P  15       -6.13     82.66
REMARK 500    LYS P  77     -125.73     56.05
REMARK 500    SER R  62      -81.13   -142.12
REMARK 500    THR R  75     -166.06   -124.36
REMARK 500    CYS R 172      124.27   -170.53
REMARK 500    ASN R 207      -95.19   -122.40
REMARK 500    MET R 212      110.93   -163.58
REMARK 500    ALA R 296      131.89    -37.14
REMARK 500    MET R 297      -14.27     85.75
REMARK 500    VAL R 331      -53.29     67.15
REMARK 500    ASP R 357       91.90   -162.88
REMARK 500    GLU T  13     -143.55     59.94
REMARK 500    PHE T  15       -2.36     83.52
REMARK 500    LYS T  77     -126.58     54.17
REMARK 500    SER V  62      -80.48   -141.87
REMARK 500    THR V  75     -164.08   -124.74
REMARK 500    CYS V 172      125.22   -171.30
REMARK 500    ASN V 207      -95.67   -124.31
REMARK 500    MET V 212      108.94   -163.23
REMARK 500    ALA V 296      129.04    -33.86
REMARK 500    MET V 297      -14.74     88.44
REMARK 500    VAL V 331      -53.86     69.61
REMARK 500    ASP V 357       91.84   -165.27
REMARK 500    GLU W  13     -140.23     58.54
REMARK 500    PHE W  15       -2.69     80.66
REMARK 500    LYS W  77     -124.87     56.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201   OQ2
REMARK 620 2 ASP A 203   OD1  90.3
REMARK 620 3 CAP A 477   O2   97.5 105.5
REMARK 620 4 GLU A 204   OE1  91.8  92.2 159.9
REMARK 620 5 CAP A 477   O3   89.8 177.3  77.1  85.1
REMARK 620 6 CAP A 477   O7  173.9  94.6  77.8  91.5  85.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B 477   O3
REMARK 620 2 KCX B 201   OQ2  85.9
REMARK 620 3 CAP B 477   O2   76.9  96.7
REMARK 620 4 CAP B 477   O7   87.7 172.3  77.7
REMARK 620 5 ASP B 203   OD1 173.7  87.9 105.1  98.6
REMARK 620 6 GLU B 204   OE1  86.8  89.2 162.1  94.7  91.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 203   OD1
REMARK 620 2 CAP E 477   O2  104.2
REMARK 620 3 CAP E 477   O7   94.2  76.0
REMARK 620 4 KCX E 201   OQ2  91.6  96.1 171.1
REMARK 620 5 GLU E 204   OE1  89.5 163.9  94.9  91.8
REMARK 620 6 CAP E 477   O3  176.6  76.8  89.1  85.1  90.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 203   OD1
REMARK 620 2 CAP H 477   O2  104.7
REMARK 620 3 CAP H 477   O7   91.9  75.0
REMARK 620 4 KCX H 201   OQ2  95.1  97.0 170.5
REMARK 620 5 GLU H 204   OE1  93.1 158.1  92.1  93.9
REMARK 620 6 CAP H 477   O3  176.4  76.4  85.0  88.1  85.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG K 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP K 477   O3
REMARK 620 2 KCX K 201   OQ2  83.0
REMARK 620 3 ASP K 203   OD1 174.3  93.8
REMARK 620 4 CAP K 477   O2   77.6  96.2 107.5
REMARK 620 5 GLU K 204   OE1  83.9  88.1  91.3 160.3
REMARK 620 6 CAP K 477   O7   84.2 166.9  99.2  78.2  93.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG O 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX O 201   OQ2
REMARK 620 2 ASP O 203   OD1  87.7
REMARK 620 3 CAP O 477   O2   96.9 101.9
REMARK 620 4 CAP O 477   O3   89.2 176.9  78.4
REMARK 620 5 GLU O 204   OE1  91.8  88.7 166.5  91.5
REMARK 620 6 CAP O 477   O7  173.4  92.1  76.7  91.0  94.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG R 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX R 201   OQ2
REMARK 620 2 ASP R 203   OD1  90.5
REMARK 620 3 GLU R 204   OE1  88.4  89.6
REMARK 620 4 CAP R 477   O2   97.7 108.3 161.0
REMARK 620 5 CAP R 477   O3   84.6 173.3  85.7  77.0
REMARK 620 6 CAP R 477   O7  171.0  97.3  96.0  75.7  87.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG V 476  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP V 477   O2
REMARK 620 2 CAP V 477   O3   76.1
REMARK 620 3 CAP V 477   O7   76.5  86.5
REMARK 620 4 ASP V 203   OD1 106.8 176.7  95.7
REMARK 620 5 GLU V 204   OE1 160.6  86.5  94.2  90.9
REMARK 620 6 KCX V 201   OQ2  95.7  85.8 170.2  92.2  91.5
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG K 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG O 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG R 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG V 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D   9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  10
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  11
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  12
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  13
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  14
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  15
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  16
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  18
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  19
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  20
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  21
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  22
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  23
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  24
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  25
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  26
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  27
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  28
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  29
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  30
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  31
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  32
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  33
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  34
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  35
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  36
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  37
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  38
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  39
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  40
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  41
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  42
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  43
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  44
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  45
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  46
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  47
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  48
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  49
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  50
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  51
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  52
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  53
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  54
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  56
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  57
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  58
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  59
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  61
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D  62
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP K 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP O 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP R 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP V 477
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII
REMARK 900 RELATED ID: 1IR2   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5
REMARK 900  -BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM
REMARK 900  GREEN ALGA,CHLAMYDOMONAS REINHARDTII COMPLEXED
REMARK 900  WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (2-CABP)
REMARK 900 RELATED ID: 1UW9   RELATED DB: PDB
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS
DBREF  1UWA A    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA B    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA E    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA H    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA K    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA O    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA R    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA V    1   475  UNP    P00877   RBL_CHLRE        1    475
DBREF  1UWA I    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  1UWA C    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  1UWA F    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  1UWA J    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  1UWA P    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  1UWA T    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  1UWA M    1   140  UNP    P00873   RBS1_CHLRE      46    185
DBREF  1UWA W    1   140  UNP    P00873   RBS1_CHLRE      46    185
SEQADV 1UWA PRO A   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA PRO B   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA PRO E   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA PRO H   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA PRO K   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA PRO O   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA PRO R   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA PRO V   46  UNP  P00877    LEU    46 CONFLICT
SEQADV 1UWA SER I  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP I  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA SER C  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP C  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA SER F  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP F  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA SER J  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP J  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA SER P  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP P  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA SER T  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP T  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA SER M  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP M  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA SER W  128  UNP  P00873    THR   173 CONFLICT
SEQADV 1UWA TRP W  132  UNP  P00873    PHE   177 CONFLICT
SEQADV 1UWA PHE A  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQADV 1UWA PHE B  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQADV 1UWA PHE E  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQADV 1UWA PHE H  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQADV 1UWA PHE K  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQADV 1UWA PHE O  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQADV 1UWA PHE R  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQADV 1UWA PHE V  290  UNP  P00877    LEU   290 ENGINEERED MUTATION
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 A  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 A  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 B  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 B  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 C  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 C  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 C  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 C  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 C  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 C  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 C  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 C  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 C  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 C  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 C  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 E  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 E  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 F  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 F  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 F  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 F  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 F  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 F  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 F  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 F  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 F  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 F  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 F  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 H  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 H  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 H  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 I  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 I  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 J  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 J  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 J  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 J  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 J  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 J  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 J  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 J  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 J  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 J  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 K  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 K  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 K  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 K  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 K  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 K  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 K  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 K  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 K  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 K  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 K  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 K  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 K  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 K  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 K  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 K  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 K  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 K  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 K  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 K  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 K  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 K  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 K  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 K  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 K  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 K  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 K  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 K  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 K  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 K  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 K  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 K  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 K  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 K  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 K  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 K  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 K  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 M  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 M  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 O  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 O  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 O  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 O  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 O  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 O  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 O  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 O  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 O  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 O  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 O  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 O  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 O  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 O  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 O  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 O  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 O  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 O  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 O  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 O  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 O  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 O  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 O  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 O  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 O  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 O  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 O  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 O  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 O  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 O  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 O  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 O  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 O  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 O  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 O  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 O  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 O  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 P  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 P  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 P  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 P  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 P  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 P  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 P  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 P  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 P  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 P  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 R  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 R  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 R  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 R  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 R  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 R  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 R  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 R  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 R  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 R  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 R  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 R  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 R  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 R  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 R  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 R  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 R  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 R  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 R  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 R  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 R  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 R  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 R  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 R  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 R  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 R  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 R  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 R  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 R  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 R  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 R  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 R  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 R  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 R  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 R  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 R  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 R  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 T  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 T  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 T  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 T  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 T  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 T  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 T  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 T  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 T  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 T  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 T  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES   1 V  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES   2 V  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES   3 V  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES   4 V  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 V  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 V  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 V  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES   8 V  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES   9 V  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 V  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 V  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 V  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES  13 V  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES  14 V  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 V  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 V  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 V  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES  18 V  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 V  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 V  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES  21 V  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 V  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES  23 V  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 V  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 V  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 V  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 V  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES  28 V  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 V  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES  30 V  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 V  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES  32 V  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 V  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES  34 V  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES  35 V  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 V  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 V  475  PHE ASP THR ILE ASP LYS LEU
SEQRES   1 W  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES   2 W  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE
SEQRES   3 W  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES   4 W  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL
SEQRES   5 W  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES   6 W  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES   7 W  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES   8 W  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES   9 W  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES  10 W  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES  11 W  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
MODRES 1UWA HYP A  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP A  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP B  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP B  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP E  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP E  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP H  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP H  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP K  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP K  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP O  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP O  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP R  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP R  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP V  104  PRO  4-HYDROXYPROLINE
MODRES 1UWA HYP V  151  PRO  4-HYDROXYPROLINE
MODRES 1UWA KCX A  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA KCX B  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA KCX E  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA KCX H  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA KCX K  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA KCX O  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA KCX R  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA KCX V  201  LYS  LYSINE NZ- CARBOXYLIC ACID
MODRES 1UWA SMC A  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC A  369  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC B  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC B  369  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC E  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC E  369  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC H  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC H  369  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC K  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC K  369  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC O  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC O  369  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC R  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC R  369  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC V  256  CYS  S- METHYLCYSTEINE
MODRES 1UWA SMC V  369  CYS  S- METHYLCYSTEINE
HET    HYP  A 104       8
HET    HYP  A 151       8
HET    KCX  A 201      12
HET    SMC  A 256       7
HET    SMC  A 369       7
HET    HYP  B 104       8
HET    HYP  B 151       8
HET    KCX  B 201      12
HET    SMC  B 256       7
HET    SMC  B 369       7
HET    HYP  E 104       8
HET    HYP  E 151       8
HET    KCX  E 201      12
HET    SMC  E 256       7
HET    SMC  E 369       7
HET    HYP  H 104       8
HET    HYP  H 151       8
HET    KCX  H 201      12
HET    SMC  H 256       7
HET    SMC  H 369       7
HET    HYP  K 104       8
HET    HYP  K 151       8
HET    KCX  K 201      12
HET    SMC  K 256       7
HET    SMC  K 369       7
HET    HYP  O 104       8
HET    HYP  O 151       8
HET    KCX  O 201      12
HET    SMC  O 256       7
HET    SMC  O 369       7
HET    HYP  R 104       7
HET    HYP  R 151       8
HET    KCX  R 201      12
HET    SMC  R 256       7
HET    SMC  R 369       7
HET    HYP  V 104       8
HET    HYP  V 151       8
HET    KCX  V 201      12
HET    SMC  V 256       7
HET    SMC  V 369       7
HET     MG  A 476       1
HET     MG  B 476       1
HET     MG  E 476       1
HET     MG  H 476       1
HET     MG  K 476       1
HET     MG  O 476       1
HET     MG  R 476       1
HET     MG  V 476       1
HET    CAP  A 477      21
HET    CAP  B 477      21
HET    EDO  D   1       4
HET    EDO  D   2       4
HET    EDO  D   3       4
HET    EDO  D   4       4
HET    EDO  D   5       4
HET    EDO  D   6       4
HET    EDO  D   7       4
HET    EDO  D   8       4
HET    EDO  D   9       4
HET    EDO  D  10       4
HET    EDO  D  11       4
HET    EDO  D  12       4
HET    EDO  D  13       4
HET    EDO  D  14       4
HET    EDO  D  15       4
HET    EDO  D  16       4
HET    EDO  D  18       4
HET    EDO  D  19       4
HET    EDO  D  20       4
HET    EDO  D  21       4
HET    EDO  D  22       4
HET    EDO  D  23       4
HET    EDO  D  24       4
HET    EDO  D  25       4
HET    EDO  D  26       4
HET    EDO  D  27       4
HET    EDO  D  28       4
HET    EDO  D  29       4
HET    EDO  D  30       4
HET    EDO  D  31       4
HET    EDO  D  32       4
HET    EDO  D  33       4
HET    EDO  D  34       4
HET    EDO  D  35       4
HET    EDO  D  36       4
HET    EDO  D  37       4
HET    EDO  D  38       4
HET    EDO  D  39       4
HET    EDO  D  40       4
HET    EDO  D  41       4
HET    EDO  D  42       4
HET    EDO  D  43       4
HET    EDO  D  44       4
HET    EDO  D  45       4
HET    EDO  D  46       4
HET    EDO  D  47       4
HET    EDO  D  48       4
HET    EDO  D  49       4
HET    EDO  D  50       4
HET    EDO  D  51       4
HET    EDO  D  52       4
HET    EDO  D  53       4
HET    EDO  D  54       4
HET    EDO  D  56       4
HET    EDO  D  57       4
HET    EDO  D  58       4
HET    EDO  D  59       4
HET    EDO  D  61       4
HET    EDO  D  62       4
HET    CAP  E 477      21
HET    CAP  H 477      21
HET    CAP  K 477      21
HET    CAP  O 477      21
HET    CAP  R 477      21
HET    CAP  V 477      21
HETNAM     HYP 4-HYDROXYPROLINE
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM     SMC S-METHYLCYSTEINE
HETNAM     HYP 4-HYDROXYPROLINE
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   1  HYP    16(C5 H9 N O3)
FORMUL   1  KCX    8(C7 H14 N2 O4)
FORMUL   1  SMC    16(C4 H9 N O2 S)
FORMUL  17   MG    8(MG 2+)
FORMUL  25  CAP    8(C6 H14 O13 P2)
FORMUL  27  EDO    59(C2 H6 O2)
FORMUL  92  HOH   *2310(H2 O1)
HELIX    1   1 TYR A   20  TYR A   25  1                                   6
HELIX    2   2 PRO A   49  SER A   61  1                                  13
HELIX    3   3 VAL A   69  THR A   75  5                                   7
HELIX    4   4 SER A   76  LYS A   81  1                                   6
HELIX    5   5 HYP A  104  PHE A  108  5                                   5
HELIX    6   6 SER A  112  GLY A  122  1                                  11
HELIX    7   7 ASN A  123  GLY A  126  5                                   4
HELIX    8   8 PRO A  141  LYS A  146  1                                   6
HELIX    9   9 GLY A  154  ASN A  163  1                                  10
HELIX   10  10 SER A  181  GLY A  195  1                                  15
HELIX   11  11 ARG A  213  GLY A  233  1                                  21
HELIX   12  12 THR A  246  GLY A  261  1                                  16
HELIX   13  13 TYR A  269  GLY A  288  1                                  20
HELIX   14  14 MET A  297  ARG A  303  1                                   7
HELIX   15  15 HIS A  310  GLY A  322  1                                  13
HELIX   16  16 GLU A  338  ASP A  351  1                                  14
HELIX   17  17 ARG A  358  GLY A  361  5                                   4
HELIX   18  18 HIS A  383  TRP A  385  5                                   3
HELIX   19  19 HIS A  386  GLY A  395  1                                  10
HELIX   20  20 GLY A  403  GLY A  408  1                                   6
HELIX   21  21 GLY A  412  GLU A  433  1                                  22
HELIX   22  22 ASP A  436  LYS A  463  1                                  28
HELIX   23  23 TYR B   20  TYR B   25  1                                   6
HELIX   24  24 PRO B   49  SER B   61  1                                  13
HELIX   25  25 VAL B   69  THR B   75  5                                   7
HELIX   26  26 SER B   76  LYS B   81  1                                   6
HELIX   27  27 HYP B  104  PHE B  108  5                                   5
HELIX   28  28 SER B  112  GLY B  122  1                                  11
HELIX   29  29 ASN B  123  GLY B  126  5                                   4
HELIX   30  30 PRO B  141  LYS B  146  1                                   6
HELIX   31  31 GLY B  154  ASN B  163  1                                  10
HELIX   32  32 SER B  181  GLY B  195  1                                  15
HELIX   33  33 ARG B  213  GLY B  233  1                                  21
HELIX   34  34 THR B  246  LEU B  260  1                                  15
HELIX   35  35 TYR B  269  GLY B  288  1                                  20
HELIX   36  36 MET B  297  ARG B  303  1                                   7
HELIX   37  37 HIS B  310  GLY B  322  1                                  13
HELIX   38  38 GLU B  338  ASP B  351  1                                  14
HELIX   39  39 ARG B  358  GLY B  361  5                                   4
HELIX   40  40 HIS B  383  TRP B  385  5                                   3
HELIX   41  41 HIS B  386  GLY B  395  1                                  10
HELIX   42  42 GLY B  403  GLY B  408  1                                   6
HELIX   43  43 GLY B  412  GLU B  433  1                                  22
HELIX   44  44 ASP B  436  LYS B  463  1                                  28
HELIX   45  45 THR C   22  ASN C   36  1                                  15
HELIX   46  46 GLU C   46  ALA C   50  5                                   5
HELIX   47  47 ASN C   54  PHE C   60  5                                   7
HELIX   48  48 ASP C   85  PHE C  100  1                                  16
HELIX   49  49 PRO C  134  ARG C  138  5                                   5
HELIX   50  50 TYR E   20  TYR E   25  1                                   6
HELIX   51  51 PRO E   49  SER E   61  1                                  13
HELIX   52  52 VAL E   69  THR E   75  5                                   7
HELIX   53  53 SER E   76  LYS E   81  1                                   6
HELIX   54  54 HYP E  104  PHE E  108  5                                   5
HELIX   55  55 SER E  112  GLY E  122  1                                  11
HELIX   56  56 ASN E  123  GLY E  126  5                                   4
HELIX   57  57 PRO E  141  LYS E  146  1                                   6
HELIX   58  58 GLY E  154  ASN E  163  1                                  10
HELIX   59  59 SER E  181  GLY E  195  1                                  15
HELIX   60  60 ARG E  213  GLY E  233  1                                  21
HELIX   61  61 THR E  246  LEU E  260  1                                  15
HELIX   62  62 TYR E  269  GLY E  288  1                                  20
HELIX   63  63 MET E  297  ARG E  303  1                                   7
HELIX   64  64 HIS E  310  GLY E  322  1                                  13
HELIX   65  65 GLU E  338  ASP E  351  1                                  14
HELIX   66  66 ARG E  358  GLY E  361  5                                   4
HELIX   67  67 HIS E  383  TRP E  385  5                                   3
HELIX   68  68 HIS E  386  GLY E  395  1                                  10
HELIX   69  69 GLY E  403  GLY E  408  1                                   6
HELIX   70  70 GLY E  412  GLU E  433  1                                  22
HELIX   71  71 ASP E  436  LYS E  463  1                                  28
HELIX   72  72 THR F   22  GLY F   37  1                                  16
HELIX   73  73 GLU F   46  ALA F   50  5                                   5
HELIX   74  74 ASN F   54  PHE F   60  5                                   7
HELIX   75  75 ASP F   85  PHE F  100  1                                  16
HELIX   76  76 PRO F  134  ARG F  138  5                                   5
HELIX   77  77 TYR H   20  TYR H   25  1                                   6
HELIX   78  78 PRO H   49  SER H   61  1                                  13
HELIX   79  79 VAL H   69  THR H   75  5                                   7
HELIX   80  80 SER H   76  LYS H   81  1                                   6
HELIX   81  81 HYP H  104  PHE H  108  5                                   5
HELIX   82  82 SER H  112  GLY H  122  1                                  11
HELIX   83  83 ASN H  123  GLY H  126  5                                   4
HELIX   84  84 PRO H  141  LYS H  146  1                                   6
HELIX   85  85 GLY H  154  ASN H  163  1                                  10
HELIX   86  86 SER H  181  GLY H  195  1                                  15
HELIX   87  87 ARG H  213  GLY H  233  1                                  21
HELIX   88  88 THR H  246  GLY H  261  1                                  16
HELIX   89  89 TYR H  269  GLY H  288  1                                  20
HELIX   90  90 MET H  297  ARG H  303  1                                   7
HELIX   91  91 HIS H  310  GLY H  322  1                                  13
HELIX   92  92 GLU H  338  ASP H  351  1                                  14
HELIX   93  93 ARG H  358  GLY H  361  5                                   4
HELIX   94  94 HIS H  383  TRP H  385  5                                   3
HELIX   95  95 HIS H  386  GLY H  395  1                                  10
HELIX   96  96 GLY H  403  GLY H  408  1                                   6
HELIX   97  97 GLY H  412  GLU H  433  1                                  22
HELIX   98  98 ASP H  436  LYS H  463  1                                  28
HELIX   99  99 THR I   22  ASN I   36  1                                  15
HELIX  100 100 GLU I   46  ALA I   50  5                                   5
HELIX  101 101 ASN I   54  PHE I   60  5                                   7
HELIX  102 102 ASP I   85  PHE I  100  1                                  16
HELIX  103 103 PRO I  134  ARG I  138  5                                   5
HELIX  104 104 THR J   22  ASN J   36  1                                  15
HELIX  105 105 GLU J   46  ALA J   50  5                                   5
HELIX  106 106 ASN J   54  PHE J   60  5                                   7
HELIX  107 107 ASP J   85  PHE J  100  1                                  16
HELIX  108 108 PRO J  134  ARG J  138  5                                   5
HELIX  109 109 TYR K   20  TYR K   25  1                                   6
HELIX  110 110 PRO K   49  SER K   61  1                                  13
HELIX  111 111 VAL K   69  THR K   75  5                                   7
HELIX  112 112 SER K   76  LYS K   81  1                                   6
HELIX  113 113 HYP K  104  PHE K  108  5                                   5
HELIX  114 114 SER K  112  GLY K  122  1                                  11
HELIX  115 115 ASN K  123  GLY K  126  5                                   4
HELIX  116 116 PRO K  141  LYS K  146  1                                   6
HELIX  117 117 GLY K  154  ASN K  163  1                                  10
HELIX  118 118 SER K  181  GLY K  195  1                                  15
HELIX  119 119 ARG K  213  GLY K  233  1                                  21
HELIX  120 120 THR K  246  GLY K  261  1                                  16
HELIX  121 121 TYR K  269  GLY K  288  1                                  20
HELIX  122 122 MET K  297  ARG K  303  1                                   7
HELIX  123 123 HIS K  310  GLY K  322  1                                  13
HELIX  124 124 GLU K  338  ASP K  351  1                                  14
HELIX  125 125 HIS K  383  TRP K  385  5                                   3
HELIX  126 126 HIS K  386  GLY K  395  1                                  10
HELIX  127 127 GLY K  403  GLY K  408  1                                   6
HELIX  128 128 GLY K  412  GLU K  433  1                                  22
HELIX  129 129 ASP K  436  LYS K  463  1                                  28
HELIX  130 130 THR M   22  ASN M   36  1                                  15
HELIX  131 131 GLU M   46  ALA M   50  5                                   5
HELIX  132 132 ASN M   54  PHE M   60  5                                   7
HELIX  133 133 ASP M   85  PHE M  100  1                                  16
HELIX  134 134 PRO M  134  ARG M  138  5                                   5
HELIX  135 135 TYR O   20  TYR O   25  1                                   6
HELIX  136 136 PRO O   49  SER O   61  1                                  13
HELIX  137 137 VAL O   69  THR O   75  5                                   7
HELIX  138 138 SER O   76  LYS O   81  1                                   6
HELIX  139 139 HYP O  104  PHE O  108  5                                   5
HELIX  140 140 SER O  112  GLY O  122  1                                  11
HELIX  141 141 ASN O  123  GLY O  126  5                                   4
HELIX  142 142 PRO O  141  LYS O  146  1                                   6
HELIX  143 143 GLY O  154  ASN O  163  1                                  10
HELIX  144 144 SER O  181  GLY O  195  1                                  15
HELIX  145 145 ARG O  213  GLY O  233  1                                  21
HELIX  146 146 THR O  246  LEU O  260  1                                  15
HELIX  147 147 TYR O  269  GLY O  288  1                                  20
HELIX  148 148 MET O  297  ARG O  303  1                                   7
HELIX  149 149 HIS O  310  GLY O  322  1                                  13
HELIX  150 150 GLU O  338  ASP O  351  1                                  14
HELIX  151 151 ARG O  358  GLY O  361  5                                   4
HELIX  152 152 HIS O  383  TRP O  385  5                                   3
HELIX  153 153 HIS O  386  GLY O  395  1                                  10
HELIX  154 154 GLY O  403  GLY O  408  1                                   6
HELIX  155 155 GLY O  412  GLU O  433  1                                  22
HELIX  156 156 ASP O  436  LYS O  463  1                                  28
HELIX  157 157 THR P   22  ASN P   36  1                                  15
HELIX  158 158 GLU P   46  ALA P   50  5                                   5
HELIX  159 159 ASN P   54  PHE P   60  5                                   7
HELIX  160 160 ASP P   85  PHE P  100  1                                  16
HELIX  161 161 PRO P  134  ARG P  138  5                                   5
HELIX  162 162 TYR R   20  TYR R   25  1                                   6
HELIX  163 163 PRO R   49  SER R   61  1                                  13
HELIX  164 164 VAL R   69  THR R   75  5                                   7
HELIX  165 165 SER R   76  LYS R   81  1                                   6
HELIX  166 166 HYP R  104  PHE R  108  5                                   5
HELIX  167 167 SER R  112  GLY R  122  1                                  11
HELIX  168 168 ASN R  123  GLY R  126  5                                   4
HELIX  169 169 PRO R  141  LYS R  146  1                                   6
HELIX  170 170 GLY R  154  ASN R  163  1                                  10
HELIX  171 171 SER R  181  GLY R  195  1                                  15
HELIX  172 172 ARG R  213  GLY R  233  1                                  21
HELIX  173 173 THR R  246  GLY R  261  1                                  16
HELIX  174 174 TYR R  269  GLY R  288  1                                  20
HELIX  175 175 MET R  297  ARG R  303  1                                   7
HELIX  176 176 HIS R  310  GLY R  322  1                                  13
HELIX  177 177 GLU R  338  ASP R  351  1                                  14
HELIX  178 178 ARG R  358  GLY R  361  5                                   4
HELIX  179 179 HIS R  383  TRP R  385  5                                   3
HELIX  180 180 HIS R  386  GLY R  395  1                                  10
HELIX  181 181 GLY R  403  GLY R  408  1                                   6
HELIX  182 182 GLY R  412  GLU R  433  1                                  22
HELIX  183 183 ASP R  436  LYS R  463  1                                  28
HELIX  184 184 THR T   22  GLY T   37  1                                  16
HELIX  185 185 GLU T   46  ALA T   50  5                                   5
HELIX  186 186 ASN T   54  PHE T   60  5                                   7
HELIX  187 187 ASP T   85  PHE T  100  1                                  16
HELIX  188 188 PRO T  134  ARG T  138  5                                   5
HELIX  189 189 TYR V   20  TYR V   25  1                                   6
HELIX  190 190 PRO V   49  SER V   61  1                                  13
HELIX  191 191 VAL V   69  THR V   75  5                                   7
HELIX  192 192 SER V   76  LYS V   81  1                                   6
HELIX  193 193 HYP V  104  PHE V  108  5                                   5
HELIX  194 194 SER V  112  GLY V  122  1                                  11
HELIX  195 195 ASN V  123  GLY V  126  5                                   4
HELIX  196 196 PRO V  141  LYS V  146  1                                   6
HELIX  197 197 GLY V  154  ASN V  163  1                                  10
HELIX  198 198 SER V  181  GLY V  195  1                                  15
HELIX  199 199 ARG V  213  GLY V  233  1                                  21
HELIX  200 200 THR V  246  GLY V  261  1                                  16
HELIX  201 201 TYR V  269  GLY V  288  1                                  20
HELIX  202 202 MET V  297  ARG V  303  1                                   7
HELIX  203 203 HIS V  310  GLY V  322  1                                  13
HELIX  204 204 GLU V  338  ASP V  351  1                                  14
HELIX  205 205 ARG V  358  GLY V  361  5                                   4
HELIX  206 206 HIS V  383  TRP V  385  5                                   3
HELIX  207 207 HIS V  386  GLY V  395  1                                  10
HELIX  208 208 GLY V  403  GLY V  408  1                                   6
HELIX  209 209 GLY V  412  GLU V  433  1                                  22
HELIX  210 210 ASP V  436  LYS V  463  1                                  28
HELIX  211 211 THR W   22  ASN W   36  1                                  15
HELIX  212 212 GLU W   46  ALA W   50  5                                   5
HELIX  213 213 ASN W   54  PHE W   60  5                                   7
HELIX  214 214 ASP W   85  PHE W  100  1                                  16
HELIX  215 215 PRO W  134  ARG W  138  5                                   5
SHEET    1  AA 5 ARG A  83  PRO A  89  0
SHEET    2  AA 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  ARG A 131   O  THR A  43
SHEET    5  AA 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135
SHEET    1  AB 8 LEU A 169  GLY A 171  0
SHEET    2  AB 8 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171
SHEET    3  AB 8 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399
SHEET    4  AB 8 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377
SHEET    5  AB 8 PHE A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327
SHEET    6  AB 8 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292
SHEET    7  AB 8 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266
SHEET    8  AB 8 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239
SHEET    1  AC 2 TYR A 353  VAL A 354  0
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354
SHEET    1  BA 5 ARG B  83  PRO B  89  0
SHEET    2  BA 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88
SHEET    3  BA 5 ILE B  36  PRO B  44 -1  O  ILE B  36   N  TYR B 103
SHEET    4  BA 5 LEU B 130  ARG B 139 -1  N  ARG B 131   O  THR B  43
SHEET    5  BA 5 GLY B 308  ILE B 309  1  O  GLY B 308   N  LEU B 135
SHEET    1  BB 8 LEU B 169  GLY B 171  0
SHEET    2  BB 8 CYS B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171
SHEET    3  BB 8 MET B 375  SER B 379  1  O  PRO B 376   N  CYS B 399
SHEET    4  BB 8 HIS B 325  HIS B 327  1  O  LEU B 326   N  VAL B 377
SHEET    5  BB 8 PHE B 290  HIS B 294  1  O  ILE B 293   N  HIS B 327
SHEET    6  BB 8 ILE B 264  ASP B 268  1  O  ILE B 265   N  HIS B 292
SHEET    7  BB 8 GLY B 237  ASN B 241  1  O  LEU B 240   N  MET B 266
SHEET    8  BB 8 PHE B 199  KCX B 201  1  O  THR B 200   N  TYR B 239
SHEET    1  BC 2 TYR B 353  VAL B 354  0
SHEET    2  BC 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  VAL B 354
SHEET    1  CA 4 THR C  74  TRP C  76  0
SHEET    2  CA 4 ILE C  39  ALA C  45 -1  O  LEU C  42   N  TRP C  76
SHEET    3  CA 4 TYR C 104  ASP C 111 -1  O  TYR C 104   N  ALA C  45
SHEET    4  CA 4 VAL C 116  GLN C 124 -1  O  VAL C 116   N  ASP C 111
SHEET    1  EA 5 ARG E  83  PRO E  89  0
SHEET    2  EA 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  ARG E 131   O  THR E  43
SHEET    5  EA 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135
SHEET    1  EB 8 LEU E 169  GLY E 171  0
SHEET    2  EB 8 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171
SHEET    3  EB 8 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377
SHEET    5  EB 8 PHE E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327
SHEET    6  EB 8 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292
SHEET    7  EB 8 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266
SHEET    8  EB 8 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239
SHEET    1  EC 2 TYR E 353  VAL E 354  0
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354
SHEET    1  FA 4 THR F  74  TRP F  76  0
SHEET    2  FA 4 ILE F  39  ALA F  45 -1  O  LEU F  42   N  TRP F  76
SHEET    3  FA 4 TYR F 104  ASP F 111 -1  O  TYR F 104   N  ALA F  45
SHEET    4  FA 4 VAL F 116  GLN F 124 -1  O  VAL F 116   N  ASP F 111
SHEET    1  HA 5 ARG H  83  PRO H  89  0
SHEET    2  HA 5 TYR H  97  TYR H 103 -1  O  ILE H  98   N  GLU H  88
SHEET    3  HA 5 ILE H  36  PRO H  44 -1  O  ILE H  36   N  TYR H 103
SHEET    4  HA 5 LEU H 130  ARG H 139 -1  N  ARG H 131   O  THR H  43
SHEET    5  HA 5 GLY H 308  ILE H 309  1  O  GLY H 308   N  LEU H 135
SHEET    1  HB 8 LEU H 169  GLY H 171  0
SHEET    2  HB 8 CYS H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171
SHEET    3  HB 8 MET H 375  SER H 379  1  O  PRO H 376   N  CYS H 399
SHEET    4  HB 8 HIS H 325  HIS H 327  1  O  LEU H 326   N  VAL H 377
SHEET    5  HB 8 PHE H 290  HIS H 294  1  O  ILE H 293   N  HIS H 327
SHEET    6  HB 8 ILE H 264  ASP H 268  1  O  ILE H 265   N  HIS H 292
SHEET    7  HB 8 GLY H 237  ASN H 241  1  O  LEU H 240   N  MET H 266
SHEET    8  HB 8 PHE H 199  KCX H 201  1  O  THR H 200   N  TYR H 239
SHEET    1  HC 2 TYR H 353  VAL H 354  0
SHEET    2  HC 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  VAL H 354
SHEET    1  IA 4 THR I  74  TRP I  76  0
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111
SHEET    1  JA 4 THR J  74  TRP J  76  0
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  76
SHEET    3  JA 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45
SHEET    4  JA 4 VAL J 116  GLN J 124 -1  O  VAL J 116   N  ASP J 111
SHEET    1  KA 5 ARG K  83  PRO K  89  0
SHEET    2  KA 5 TYR K  97  TYR K 103 -1  O  ILE K  98   N  GLU K  88
SHEET    3  KA 5 ILE K  36  PRO K  44 -1  O  ILE K  36   N  TYR K 103
SHEET    4  KA 5 LEU K 130  ARG K 139 -1  N  ARG K 131   O  THR K  43
SHEET    5  KA 5 GLY K 308  ILE K 309  1  O  GLY K 308   N  LEU K 135
SHEET    1  KB 8 LEU K 169  GLY K 171  0
SHEET    2  KB 8 CYS K 399  GLN K 401  1  O  LEU K 400   N  GLY K 171
SHEET    3  KB 8 MET K 375  SER K 379  1  O  PRO K 376   N  CYS K 399
SHEET    4  KB 8 HIS K 325  HIS K 327  1  O  LEU K 326   N  VAL K 377
SHEET    5  KB 8 PHE K 290  HIS K 294  1  O  ILE K 293   N  HIS K 327
SHEET    6  KB 8 ILE K 264  ASP K 268  1  O  ILE K 265   N  HIS K 292
SHEET    7  KB 8 GLY K 237  ASN K 241  1  O  LEU K 240   N  MET K 266
SHEET    8  KB 8 PHE K 199  KCX K 201  1  O  THR K 200   N  TYR K 239
SHEET    1  KC 2 TYR K 353  VAL K 354  0
SHEET    2  KC 2 GLN K 366  ASP K 367 -1  O  GLN K 366   N  VAL K 354
SHEET    1  MA 4 THR M  74  TRP M  76  0
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111
SHEET    1  OA 5 ARG O  83  PRO O  89  0
SHEET    2  OA 5 TYR O  97  TYR O 103 -1  O  ILE O  98   N  GLU O  88
SHEET    3  OA 5 ILE O  36  PRO O  44 -1  O  ILE O  36   N  TYR O 103
SHEET    4  OA 5 LEU O 130  ARG O 139 -1  N  ARG O 131   O  THR O  43
SHEET    5  OA 5 GLY O 308  ILE O 309  1  O  GLY O 308   N  LEU O 135
SHEET    1  OB 8 LEU O 169  GLY O 171  0
SHEET    2  OB 8 CYS O 399  GLN O 401  1  O  LEU O 400   N  GLY O 171
SHEET    3  OB 8 MET O 375  SER O 379  1  O  PRO O 376   N  CYS O 399
SHEET    4  OB 8 HIS O 325  HIS O 327  1  O  LEU O 326   N  VAL O 377
SHEET    5  OB 8 PHE O 290  HIS O 294  1  O  ILE O 293   N  HIS O 327
SHEET    6  OB 8 ILE O 264  ASP O 268  1  O  ILE O 265   N  HIS O 292
SHEET    7  OB 8 GLY O 237  ASN O 241  1  O  LEU O 240   N  MET O 266
SHEET    8  OB 8 PHE O 199  KCX O 201  1  O  THR O 200   N  TYR O 239
SHEET    1  OC 2 TYR O 353  VAL O 354  0
SHEET    2  OC 2 GLN O 366  ASP O 367 -1  O  GLN O 366   N  VAL O 354
SHEET    1  PA 4 THR P  74  TRP P  76  0
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  76
SHEET    3  PA 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45
SHEET    4  PA 4 VAL P 116  GLN P 124 -1  O  VAL P 116   N  ASP P 111
SHEET    1  RA 5 ARG R  83  PRO R  89  0
SHEET    2  RA 5 TYR R  97  TYR R 103 -1  O  ILE R  98   N  GLU R  88
SHEET    3  RA 5 ILE R  36  PRO R  44 -1  O  ILE R  36   N  TYR R 103
SHEET    4  RA 5 LEU R 130  ARG R 139 -1  N  ARG R 131   O  THR R  43
SHEET    5  RA 5 GLY R 308  ILE R 309  1  O  GLY R 308   N  LEU R 135
SHEET    1  RB 8 LEU R 169  GLY R 171  0
SHEET    2  RB 8 CYS R 399  GLN R 401  1  O  LEU R 400   N  GLY R 171
SHEET    3  RB 8 MET R 375  SER R 379  1  O  PRO R 376   N  CYS R 399
SHEET    4  RB 8 HIS R 325  HIS R 327  1  O  LEU R 326   N  VAL R 377
SHEET    5  RB 8 PHE R 290  HIS R 294  1  O  ILE R 293   N  HIS R 327
SHEET    6  RB 8 ILE R 264  ASP R 268  1  O  ILE R 265   N  HIS R 292
SHEET    7  RB 8 GLY R 237  ASN R 241  1  O  LEU R 240   N  MET R 266
SHEET    8  RB 8 PHE R 199  KCX R 201  1  O  THR R 200   N  TYR R 239
SHEET    1  RC 2 TYR R 353  VAL R 354  0
SHEET    2  RC 2 GLN R 366  ASP R 367 -1  O  GLN R 366   N  VAL R 354
SHEET    1  TA 4 THR T  74  TRP T  76  0
SHEET    2  TA 4 ILE T  39  ALA T  45 -1  O  LEU T  42   N  TRP T  76
SHEET    3  TA 4 TYR T 104  ASP T 111 -1  O  TYR T 104   N  ALA T  45
SHEET    4  TA 4 VAL T 116  GLN T 124 -1  O  VAL T 116   N  ASP T 111
SHEET    1  VA 5 ARG V  83  PRO V  89  0
SHEET    2  VA 5 TYR V  97  TYR V 103 -1  O  ILE V  98   N  GLU V  88
SHEET    3  VA 5 ILE V  36  PRO V  44 -1  O  ILE V  36   N  TYR V 103
SHEET    4  VA 5 LEU V 130  ARG V 139 -1  N  ARG V 131   O  THR V  43
SHEET    5  VA 5 GLY V 308  ILE V 309  1  O  GLY V 308   N  LEU V 135
SHEET    1  VB 8 LEU V 169  GLY V 171  0
SHEET    2  VB 8 CYS V 399  GLN V 401  1  O  LEU V 400   N  GLY V 171
SHEET    3  VB 8 MET V 375  SER V 379  1  O  PRO V 376   N  CYS V 399
SHEET    4  VB 8 HIS V 325  HIS V 327  1  O  LEU V 326   N  VAL V 377
SHEET    5  VB 8 PHE V 290  HIS V 294  1  O  ILE V 293   N  HIS V 327
SHEET    6  VB 8 ILE V 264  ASP V 268  1  O  ILE V 265   N  HIS V 292
SHEET    7  VB 8 GLY V 237  ASN V 241  1  O  LEU V 240   N  MET V 266
SHEET    8  VB 8 PHE V 199  KCX V 201  1  O  THR V 200   N  TYR V 239
SHEET    1  VC 2 TYR V 353  VAL V 354  0
SHEET    2  VC 2 GLN V 366  ASP V 367 -1  O  GLN V 366   N  VAL V 354
SHEET    1  WA 4 THR W  74  TRP W  76  0
SHEET    2  WA 4 ILE W  39  ALA W  45 -1  O  LEU W  42   N  TRP W  76
SHEET    3  WA 4 TYR W 104  ASP W 111 -1  O  TYR W 104   N  ALA W  45
SHEET    4  WA 4 VAL W 116  GLN W 124 -1  O  VAL W 116   N  ASP W 111
SSBOND   1 CYS A  247    CYS O  247                          1555   1555  2.04
SSBOND   2 CYS A  449    CYS A  459                          1555   1555  2.07
SSBOND   3 CYS B  247    CYS E  247                          1555   1555  2.05
SSBOND   4 CYS B  449    CYS B  459                          1555   1555  2.07
SSBOND   5 CYS E  449    CYS E  459                          1555   1555  2.06
SSBOND   6 CYS H  247    CYS V  247                          1555   1555  2.04
SSBOND   7 CYS H  449    CYS H  459                          1555   1555  2.04
SSBOND   8 CYS K  247    CYS R  247                          1555   1555  2.04
SSBOND   9 CYS K  449    CYS K  459                          1555   1555  2.06
SSBOND  10 CYS O  449    CYS O  459                          1555   1555  2.06
SSBOND  11 CYS R  449    CYS R  459                          1555   1555  2.07
SSBOND  12 CYS V  449    CYS V  459                          1555   1555  2.06
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.33
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.33
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.33
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.34
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33
LINK        MG    MG A 476                 OQ2 KCX A 201     1555   1555  2.03
LINK        MG    MG A 476                 OD1 ASP A 203     1555   1555  1.92
LINK        MG    MG A 476                 O2  CAP A 477     1555   1555  2.19
LINK        MG    MG A 476                 OE1 GLU A 204     1555   1555  2.06
LINK        MG    MG A 476                 O3  CAP A 477     1555   1555  2.09
LINK        MG    MG A 476                 O7  CAP A 477     1555   1555  2.16
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.34
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.33
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.33
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.32
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.34
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.34
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.34
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.33
LINK        MG    MG B 476                 O3  CAP B 477     1555   1555  2.13
LINK        MG    MG B 476                 OQ2 KCX B 201     1555   1555  2.08
LINK        MG    MG B 476                 O2  CAP B 477     1555   1555  2.24
LINK        MG    MG B 476                 O7  CAP B 477     1555   1555  2.08
LINK        MG    MG B 476                 OD1 ASP B 203     1555   1555  1.94
LINK        MG    MG B 476                 OE1 GLU B 204     1555   1555  2.06
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.34
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.34
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.33
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.34
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.32
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.34
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.33
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.34
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.34
LINK        MG    MG E 476                 OQ2 KCX E 201     1555   1555  1.97
LINK        MG    MG E 476                 O7  CAP E 477     1555   1555  2.12
LINK        MG    MG E 476                 O2  CAP E 477     1555   1555  2.18
LINK        MG    MG E 476                 OD1 ASP E 203     1555   1555  1.99
LINK        MG    MG E 476                 OE1 GLU E 204     1555   1555  2.06
LINK        MG    MG E 476                 O3  CAP E 477     1555   1555  2.05
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.33
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.33
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.34
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.33
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.33
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.33
LINK         C   SMC H 256                 N   ALA H 257     1555   1555  1.33
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.33
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.34
LINK        MG    MG H 476                 OD1 ASP H 203     1555   1555  1.93
LINK        MG    MG H 476                 OQ2 KCX H 201     1555   1555  1.88
LINK        MG    MG H 476                 O7  CAP H 477     1555   1555  2.21
LINK        MG    MG H 476                 O2  CAP H 477     1555   1555  2.17
LINK        MG    MG H 476                 OE1 GLU H 204     1555   1555  2.05
LINK        MG    MG H 476                 O3  CAP H 477     1555   1555  2.14
LINK         C   TYR K 103                 N   HYP K 104     1555   1555  1.33
LINK         C   HYP K 104                 N   ILE K 105     1555   1555  1.33
LINK         C   GLY K 150                 N   HYP K 151     1555   1555  1.33
LINK         C   HYP K 151                 N   PRO K 152     1555   1555  1.34
LINK         C   THR K 200                 N   KCX K 201     1555   1555  1.32
LINK         C   KCX K 201                 N   ASP K 202     1555   1555  1.33
LINK         C   VAL K 255                 N   SMC K 256     1555   1555  1.33
LINK         C   SMC K 256                 N   ALA K 257     1555   1555  1.33
LINK         C   TRP K 368                 N   SMC K 369     1555   1555  1.34
LINK         C   SMC K 369                 N   SER K 370     1555   1555  1.34
LINK        MG    MG K 476                 OQ2 KCX K 201     1555   1555  2.02
LINK        MG    MG K 476                 O7  CAP K 477     1555   1555  2.15
LINK        MG    MG K 476                 OE1 GLU K 204     1555   1555  2.11
LINK        MG    MG K 476                 O2  CAP K 477     1555   1555  2.18
LINK        MG    MG K 476                 OD1 ASP K 203     1555   1555  1.88
LINK        MG    MG K 476                 O3  CAP K 477     1555   1555  2.23
LINK         C   TYR O 103                 N   HYP O 104     1555   1555  1.33
LINK         C   HYP O 104                 N   ILE O 105     1555   1555  1.34
LINK         C   GLY O 150                 N   HYP O 151     1555   1555  1.33
LINK         C   HYP O 151                 N   PRO O 152     1555   1555  1.33
LINK         C   THR O 200                 N   KCX O 201     1555   1555  1.33
LINK         C   KCX O 201                 N   ASP O 202     1555   1555  1.33
LINK         C   VAL O 255                 N   SMC O 256     1555   1555  1.33
LINK         C   SMC O 256                 N   ALA O 257     1555   1555  1.34
LINK         C   TRP O 368                 N   SMC O 369     1555   1555  1.33
LINK         C   SMC O 369                 N   SER O 370     1555   1555  1.33
LINK        MG    MG O 476                 O7  CAP O 477     1555   1555  2.11
LINK        MG    MG O 476                 OE1 GLU O 204     1555   1555  2.08
LINK        MG    MG O 476                 O3  CAP O 477     1555   1555  1.99
LINK        MG    MG O 476                 O2  CAP O 477     1555   1555  2.22
LINK        MG    MG O 476                 OQ2 KCX O 201     1555   1555  2.03
LINK        MG    MG O 476                 OD1 ASP O 203     1555   1555  2.05
LINK         C   TYR R 103                 N   HYP R 104     1555   1555  1.33
LINK         C   HYP R 104                 N   ILE R 105     1555   1555  1.33
LINK         C   GLY R 150                 N   HYP R 151     1555   1555  1.33
LINK         C   HYP R 151                 N   PRO R 152     1555   1555  1.33
LINK         C   THR R 200                 N   KCX R 201     1555   1555  1.33
LINK         C   KCX R 201                 N   ASP R 202     1555   1555  1.34
LINK         C   VAL R 255                 N   SMC R 256     1555   1555  1.34
LINK         C   SMC R 256                 N   ALA R 257     1555   1555  1.33
LINK         C   TRP R 368                 N   SMC R 369     1555   1555  1.34
LINK         C   SMC R 369                 N   SER R 370     1555   1555  1.33
LINK        MG    MG R 476                 O7  CAP R 477     1555   1555  2.09
LINK        MG    MG R 476                 O3  CAP R 477     1555   1555  2.16
LINK        MG    MG R 476                 O2  CAP R 477     1555   1555  2.12
LINK        MG    MG R 476                 OE1 GLU R 204     1555   1555  2.10
LINK        MG    MG R 476                 OD1 ASP R 203     1555   1555  1.89
LINK        MG    MG R 476                 OQ2 KCX R 201     1555   1555  2.03
LINK         C   TYR V 103                 N   HYP V 104     1555   1555  1.33
LINK         C   HYP V 104                 N   ILE V 105     1555   1555  1.33
LINK         C   GLY V 150                 N   HYP V 151     1555   1555  1.33
LINK         C   HYP V 151                 N   PRO V 152     1555   1555  1.33
LINK         C   THR V 200                 N   KCX V 201     1555   1555  1.32
LINK         C   KCX V 201                 N   ASP V 202     1555   1555  1.33
LINK         C   VAL V 255                 N   SMC V 256     1555   1555  1.33
LINK         C   SMC V 256                 N   ALA V 257     1555   1555  1.33
LINK         C   TRP V 368                 N   SMC V 369     1555   1555  1.33
LINK         C   SMC V 369                 N   SER V 370     1555   1555  1.34
LINK        MG    MG V 476                 O3  CAP V 477     1555   1555  2.13
LINK        MG    MG V 476                 O7  CAP V 477     1555   1555  2.14
LINK        MG    MG V 476                 OD1 ASP V 203     1555   1555  1.94
LINK        MG    MG V 476                 OE1 GLU V 204     1555   1555  2.07
LINK        MG    MG V 476                 OQ2 KCX V 201     1555   1555  2.05
LINK        MG    MG V 476                 O2  CAP V 477     1555   1555  2.22
CISPEP   1 LYS A  175    PRO A  176          0        -0.04
CISPEP   2 LYS B  175    PRO B  176          0         1.82
CISPEP   3 LYS E  175    PRO E  176          0        -3.87
CISPEP   4 LYS H  175    PRO H  176          0        -1.29
CISPEP   5 LYS K  175    PRO K  176          0        -2.26
CISPEP   6 LYS O  175    PRO O  176          0        -4.28
CISPEP   7 LYS R  175    PRO R  176          0        -3.32
CISPEP   8 LYS V  175    PRO V  176          0        -3.97
SITE     1 AC1  4 KCX A 201  ASP A 203  GLU A 204  CAP A 477
SITE     1 AC2  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204
SITE     2 AC2  5 CAP B 477
SITE     1 AC3  4 KCX E 201  ASP E 203  GLU E 204  CAP E 477
SITE     1 AC4  4 KCX H 201  ASP H 203  GLU H 204  CAP H 477
SITE     1 AC5  4 KCX K 201  ASP K 203  GLU K 204  CAP K 477
SITE     1 AC6  4 KCX O 201  ASP O 203  GLU O 204  CAP O 477
SITE     1 AC7  5 LYS R 177  KCX R 201  ASP R 203  GLU R 204
SITE     2 AC7  5 CAP R 477
SITE     1 AC8  4 KCX V 201  ASP V 203  GLU V 204  CAP V 477
SITE     1 AC9 28 THR A 173  LYS A 175  LYS A 177  KCX A 201
SITE     2 AC9 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295
SITE     3 AC9 28 HIS A 327  LYS A 334  LEU A 335  SER A 379
SITE     4 AC9 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404
SITE     5 AC9 28  MG A 476  HOH A2155  HOH A2202  HOH A2203
SITE     6 AC9 28 HOH A2215  HOH A2244  HOH A2245  GLU O  60
SITE     7 AC9 28 THR O  65  TRP O  66  ASN O 123  HOH O2057
SITE     1 BC1 29 THR B 173  LYS B 175  LYS B 177  KCX B 201
SITE     2 BC1 29 ASP B 203  GLU B 204  HIS B 294  ARG B 295
SITE     3 BC1 29 HIS B 327  LYS B 334  LEU B 335  SER B 379
SITE     4 BC1 29 GLY B 380  GLY B 381  GLY B 403  GLY B 404
SITE     5 BC1 29  MG B 476  HOH B2148  HOH B2150  HOH B2208
SITE     6 BC1 29 HOH B2245  HOH B2246  HOH B2247  GLU E  60
SITE     7 BC1 29 THR E  65  TRP E  66  ASN E 123  HOH E2042
SITE     8 BC1 29 HOH E2083
SITE     1 BC2  9 TYR A  24  GLY A  64  THR A  68  VAL A  69
SITE     2 BC2  9 ASP A  72  LEU A  77  HOH A2032  HOH D2001
SITE     3 BC2  9 HOH D2002
SITE     1 BC3  7 LYS A  18  THR A  65  TRP A  66  THR A  67
SITE     2 BC3  7 THR A  68  HOH A2013  HOH A2032
SITE     1 BC4  1 GLU A  52
SITE     1 BC5  5 HIS A 298  ASP A 302  ASP A 473  HOH A2153
SITE     2 BC5  5 HOH D2003
SITE     1 BC6  9 TYR B  24  GLY B  64  THR B  68  VAL B  69
SITE     2 BC6  9 ASP B  72  LEU B  77  HOH B2039  HOH D2004
SITE     3 BC6  9 HOH D2005
SITE     1 BC7  6 LYS B  18  THR B  65  THR B  67  THR B  68
SITE     2 BC7  6 HOH B2013  HOH D2004
SITE     1 BC8  2 GLU B  52  HOH D2006
SITE     1 BC9  5 LYS B 466  PHE B 467  GLU B 468  PHE B 469
SITE     2 BC9  5 HOH D2007
SITE     1 CC1  5 ARG B 295  GLU B 336  PHE B 345  ASP B 473
SITE     2 CC1  5 HOH B2168
SITE     1 CC2  8 HOH D2008  TYR E  24  GLY E  64  THR E  68
SITE     2 CC2  8 VAL E  69  ASP E  72  HOH E2043  HOH E2044
SITE     1 CC3  8 GLY E  16  LYS E  18  THR E  65  TRP E  66
SITE     2 CC3  8 THR E  67  THR E  68  HOH E2017  HOH E2043
SITE     1 CC4  4 HOH D2006  LYS E 466  GLU E 468  PHE E 469
SITE     1 CC5  4 HOH D2009  HOH D2010  ARG E 295  ASP E 473
SITE     1 CC6  7 TYR A 226  ALA A 230  HOH D2011  HOH D2012
SITE     2 CC6  7 LYS F  49  GLU F  55  ASP F  69
SITE     1 CC7  4 GLY F  37  TRP F  38  ILE F  39  GLY F  82
SITE     1 CC8  4 HOH D2014  HOH D2015  LEU H 270  LEU V 270
SITE     1 CC9  7 HOH D2016  VAL H  17  LYS H  18  TRP H  66
SITE     2 CC9  7 THR H  67  THR H  68  HOH H2021
SITE     1 DC1  2 HOH D2017  GLU H  52
SITE     1 DC2  4 HOH D2019  LYS H 466  GLU H 468  PHE H 469
SITE     1 DC3  4 HOH D2020  ARG H 295  GLU H 336  ASP H 473
SITE     1 DC4  8 EDO D  23  HOH D2021  HOH D2023  TYR K  24
SITE     2 DC4  8 THR K  68  VAL K  69  ASP K  72  HOH K2037
SITE     1 DC5  9 EDO D  22  HOH D2022  HOH D2023  VAL K  17
SITE     2 DC5  9 LYS K  18  THR K  65  TRP K  66  THR K  67
SITE     3 DC5  9 THR K  68
SITE     1 DC6  5 GLY P  37  TRP P  38  ILE P  39  GLY P  82
SITE     2 DC6  5 CYS P  83
SITE     1 DC7  9 EDO D  26  HOH D2026  TYR O  24  GLY O  64
SITE     2 DC7  9 THR O  68  VAL O  69  ASP O  72  HOH O2024
SITE     3 DC7  9 HOH O2027
SITE     1 DC8  8 EDO D  25  HOH D2026  LYS O  18  THR O  65
SITE     2 DC8  8 TRP O  66  THR O  67  THR O  68  HOH O2010
SITE     1 DC9  3 PHE A 469  HOH D2043  GLU O  52
SITE     1 EC1  5 HOH D2030  LYS O 466  PHE O 467  GLU O 468
SITE     2 EC1  5 PHE O 469
SITE     1 EC2  5 TYR B 226  LYS T  49  GLU T  55  SER T  56
SITE     2 EC2  5 ASP T  69
SITE     1 EC3  4 HOH D2032  LEU K 270  LEU R 270  HOH R2134
SITE     1 EC4  4 LEU B 270  HOH D2033  HOH D2034  LEU E 270
SITE     1 EC5  4 LEU A 270  HOH A2142  HOH D2035  LEU O 270
SITE     1 EC6  7 HOH D2036  LYS R  18  THR R  65  TRP R  66
SITE     2 EC6  7 THR R  67  THR R  68  HOH R2011
SITE     1 EC7  1 GLU R  52
SITE     1 EC8  5 HOH D2037  LYS R 466  PHE R 467  GLU R 468
SITE     2 EC8  5 PHE R 469
SITE     1 EC9  9 HOH D2038  HOH D2039  TYR V  24  GLY V  64
SITE     2 EC9  9 THR V  68  VAL V  69  ASP V  72  LEU V  77
SITE     3 EC9  9 HOH V2025
SITE     1 FC1  8 HOH D2039  GLY V  16  VAL V  17  LYS V  18
SITE     2 FC1  8 THR V  65  THR V  67  THR V  68  HOH V2006
SITE     1 FC2  1 GLU V  52
SITE     1 FC3  6 HOH D2040  LYS V 466  PHE V 467  GLU V 468
SITE     2 FC3  6 PHE V 469  HOH V2207
SITE     1 FC4  5 HOH D2041  GLY V 337  GLU V 338  VAL V 341
SITE     2 FC4  5 ASP V 473
SITE     1 FC5  4 GLY J  37  TRP J  38  ILE J  39  GLY J  82
SITE     1 FC6  4 ALA A  11  HOH D2042  GLY M  37  ARG M  84
SITE     1 FC7  6 GLY T  37  TRP T  38  ILE T  39  PHE T  81
SITE     2 FC7  6 GLY T  82  CYS T  83
SITE     1 FC8  5 LYS A 466  GLU A 468  PHE A 469  HOH D2043
SITE     2 FC8  5 HOH D2044
SITE     1 FC9  3 HOH D2037  TYR K  20  GLU K  52
SITE     1 GC1  4 HOH D2045  LYS K 466  GLU K 468  PHE K 469
SITE     1 GC2  3 GLU K 336  ASP K 473  HOH K2146
SITE     1 GC3  3 HOH D2007  GLU E  52  ALA E 129
SITE     1 GC4  6 HOH D2046  LYS I  49  GLU I  55  HOH I2031
SITE     2 GC4  6 TYR K 226  ALA K 230
SITE     1 GC5  5 GLY I  37  TRP I  38  ILE I  39  PHE I  81
SITE     2 GC5  5 GLY I  82
SITE     1 GC6  5 HOH D2047  LYS P  49  GLU P  55  HOH P2035
SITE     2 GC6  5 TYR V 226
SITE     1 GC7  4 ALA B  11  HOH D2048  HOH D2049  ARG W  84
SITE     1 GC8  8 HOH D2050  TYR H  24  THR H  68  VAL H  69
SITE     2 GC8  8 ASP H  72  LEU H  77  HOH H2021  HOH H2023
SITE     1 GC9  8 HOH D2036  HOH D2051  TYR R  24  GLY R  64
SITE     2 GC9  8 THR R  68  VAL R  69  ASP R  72  HOH R2031
SITE     1 HC1  5 HOH D2052  ARG R 295  GLU R 336  ASP R 473
SITE     2 HC1  5 HOH R2160
SITE     1 HC2  6 ARG O 295  GLU O 336  PHE O 345  ASP O 473
SITE     2 HC2  6 HOH O2167  HOH O2170
SITE     1 HC3  8 LYS C  49  GLU C  55  SER C  56  ASP C  69
SITE     2 HC3  8 HOH C2025  HOH D2053  TYR H 226  LYS H 227
SITE     1 HC4  3 GLY C  37  TRP C  38  GLY C  82
SITE     1 HC5  5 LYS J  49  GLU J  55  HOH J2028  TYR R 226
SITE     2 HC5  5 ALA R 230
SITE     1 HC6  4 LYS M  49  GLU M  55  HOH M2031  TYR O 226
SITE     1 HC7 30 GLU B  60  THR B  65  TRP B  66  ASN B 123
SITE     2 HC7 30 HOH B2037  HOH B2077  THR E 173  LYS E 175
SITE     3 HC7 30 LYS E 177  KCX E 201  ASP E 203  GLU E 204
SITE     4 HC7 30 HIS E 294  ARG E 295  HIS E 327  LYS E 334
SITE     5 HC7 30 LEU E 335  SER E 379  GLY E 380  GLY E 381
SITE     6 HC7 30 GLY E 403  GLY E 404   MG E 476  HOH E2116
SITE     7 HC7 30 HOH E2171  HOH E2209  HOH E2245  HOH E2246
SITE     8 HC7 30 HOH E2247  HOH E2248
SITE     1 HC8 30 THR H 173  LYS H 175  LYS H 177  KCX H 201
SITE     2 HC8 30 ASP H 203  GLU H 204  HIS H 294  ARG H 295
SITE     3 HC8 30 HIS H 327  LYS H 334  LEU H 335  SER H 379
SITE     4 HC8 30 GLY H 380  GLY H 381  GLY H 403  GLY H 404
SITE     5 HC8 30  MG H 476  HOH H2121  HOH H2152  HOH H2162
SITE     6 HC8 30 HOH H2187  HOH H2188  HOH H2189  GLU V  60
SITE     7 HC8 30 THR V  65  TRP V  66  ASN V 123  HOH V2019
SITE     8 HC8 30 HOH V2020  HOH V2048
SITE     1 HC9 30 THR K 173  LYS K 175  LYS K 177  KCX K 201
SITE     2 HC9 30 ASP K 203  GLU K 204  HIS K 294  ARG K 295
SITE     3 HC9 30 HIS K 327  LYS K 334  LEU K 335  SER K 379
SITE     4 HC9 30 GLY K 380  GLY K 381  GLY K 403  GLY K 404
SITE     5 HC9 30  MG K 476  HOH K2188  HOH K2234  HOH K2235
SITE     6 HC9 30 HOH K2236  HOH K2237  HOH K2238  GLU R  60
SITE     7 HC9 30 THR R  65  TRP R  66  ASN R 123  HOH R2027
SITE     8 HC9 30 HOH R2028  HOH R2067
SITE     1 IC1 30 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 IC1 30 HOH A2030  THR O 173  LYS O 175  LYS O 177
SITE     3 IC1 30 KCX O 201  ASP O 203  GLU O 204  HIS O 294
SITE     4 IC1 30 ARG O 295  HIS O 327  LYS O 334  LEU O 335
SITE     5 IC1 30 SER O 379  GLY O 380  GLY O 381  GLY O 403
SITE     6 IC1 30 GLY O 404   MG O 476  HOH O2091  HOH O2094
SITE     7 IC1 30 HOH O2150  HOH O2152  HOH O2190  HOH O2202
SITE     8 IC1 30 HOH O2227  HOH O2228
SITE     1 IC2 28 GLU K  60  THR K  65  TRP K  66  ASN K 123
SITE     2 IC2 28 HOH K2064  THR R 173  LYS R 175  LYS R 177
SITE     3 IC2 28 KCX R 201  ASP R 203  GLU R 204  HIS R 294
SITE     4 IC2 28 ARG R 295  HIS R 327  LYS R 334  LEU R 335
SITE     5 IC2 28 SER R 379  GLY R 380  GLY R 381  GLY R 403
SITE     6 IC2 28 GLY R 404   MG R 476  HOH R2187  HOH R2211
SITE     7 IC2 28 HOH R2212  HOH R2213  HOH R2214  HOH R2215
SITE     1 IC3 28 GLU H  60  THR H  65  TRP H  66  ASN H 123
SITE     2 IC3 28 THR V 173  LYS V 175  LYS V 177  KCX V 201
SITE     3 IC3 28 ASP V 203  GLU V 204  HIS V 294  ARG V 295
SITE     4 IC3 28 HIS V 327  LYS V 334  LEU V 335  SER V 379
SITE     5 IC3 28 GLY V 380  GLY V 381  GLY V 403  GLY V 404
SITE     6 IC3 28  MG V 476  HOH V2127  HOH V2129  HOH V2162
SITE     7 IC3 28 HOH V2174  HOH V2212  HOH V2213  HOH V2214
CRYST1  120.983  177.709  122.663  90.00 117.70  90.00 P 1 21 1     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.008266  0.000000  0.004340        0.00000
SCALE2      0.000000  0.005627  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009208        0.00000
MTRIX1   1  0.491200  0.001218 -0.871000       64.53000    1
MTRIX2   1  0.000868 -1.000000 -0.000908      168.89999    1
MTRIX3   1 -0.871000 -0.000310 -0.491200      110.60000    1
MTRIX1   2  0.093650 -0.777400 -0.622000      101.10000    1
MTRIX2   2  0.285900  0.619400 -0.731100      100.30000    1
MTRIX3   2  0.953700 -0.109300  0.280000       89.83000    1
MTRIX1   3 -0.781000 -0.286900 -0.554800       36.42000    1
MTRIX2   3 -0.288900 -0.621500  0.728200       68.55000    1
MTRIX3   3 -0.553700  0.729000  0.402400      -21.40000    1
MTRIX1   4  0.098360  0.285000  0.953500     -123.80000    1
MTRIX2   4 -0.776900  0.620800 -0.105400       25.49000    1
MTRIX3   4 -0.621900 -0.730300  0.282500      110.80000    1
MTRIX1   5  0.491400  0.001234 -0.870900       64.54000    1
MTRIX2   5  0.002343 -1.000000 -0.000094      168.89999    1
MTRIX3   5 -0.870900 -0.001995 -0.491400      110.80000    1
MTRIX1   6  0.586100  0.778600  0.224100      -93.05000    1
MTRIX2   6  0.778400 -0.617900  0.111300      142.30000    1
MTRIX3   6  0.225100  0.109300 -0.968200      164.00000    1
MTRIX1   7 -0.685000  0.489000  0.540100     -121.10000    1
MTRIX2   7  0.488400 -0.242100  0.838400       42.44000    1
MTRIX3   7  0.540700  0.838000 -0.073000       32.16000    1
MTRIX1   8 -0.805800 -0.490400  0.331900      -22.92000    1
MTRIX2   8 -0.491500  0.241100 -0.836900      125.90000    1
MTRIX3   8  0.330400 -0.837500 -0.435300      200.50000    1
MTRIX1   9  0.093620 -0.779200 -0.619800      101.00000    1
MTRIX2   9  0.281600  0.617800 -0.734200      100.80000    1
MTRIX3   9  0.955000 -0.105800  0.277300       89.87000    1
MTRIX1  10 -0.781100 -0.279600 -0.558300       35.92000    1
MTRIX2  10 -0.290500 -0.628700  0.721300       69.74000    1
MTRIX3  10 -0.552700  0.725600  0.409800      -21.51000    1
MTRIX1  11  0.102300  0.279300  0.954700     -123.50000    1
MTRIX2  11 -0.772200  0.627400 -0.100800       24.66000    1
MTRIX3  11 -0.627100 -0.726900  0.279800      110.80000    1
MTRIX1  12  0.584300  0.780300  0.223000      -93.19000    1
MTRIX2  12  0.778900 -0.616300  0.115800      141.89999    1
MTRIX3  12  0.227800  0.106000 -0.967900      164.39999    1
MTRIX1  13 -0.681400  0.494200  0.539900     -121.50000    1
MTRIX2  13  0.491500 -0.237700  0.837800       42.23000    1
MTRIX3  13  0.542300  0.836300 -0.080920       33.21000    1
MTRIX1  14 -0.803900 -0.493700  0.331800      -22.65000    1
MTRIX2  14 -0.492200  0.238900 -0.837100      126.10000    1
MTRIX3  14  0.334000 -0.836200 -0.435000      200.60001    1
      
PROCHECK
Go to PROCHECK summary
 References