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PDBsum entry 1upm

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1upm
Jmol
Contents
Protein chains
(+ 2 more) 467 a.a. *
(+ 2 more) 123 a.a. *
Ligands
CAP ×8
Metals
_CA ×8
Waters ×2788
* Residue conservation analysis
HEADER    LYASE                                   08-OCT-03   1UPM
TITLE     ACTIVATED SPINACH RUBISCO COMPLEXED WITH
TITLE    2 2-CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: L, B, E, H, K, O, R, V;
COMPND   4 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE,
COMPND   5  RUBISCO LARGE SUBUNIT;
COMPND   6 EC: 4.1.1.39;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN;
COMPND   9 CHAIN: S, C, F, I, M, P, T, W;
COMPND  10 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE,
COMPND  11  RUBISCO SMALL SUBUNIT;
COMPND  12 EC: 4.1.1.39;
COMPND  13 OTHER_DETAILS: THE COMPLETE STRUCTURE HAS BEEN SUBMITTED
COMPND  14  AS WELL AS THE MATRIX TRANSFORMATION FOR EACH CHAIN.
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   3 ORGANISM_COMMON: SPINACH;
SOURCE   4 ORGANISM_TAXID: 3562;
SOURCE   5 TISSUE: LEAF;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   8 ORGANISM_COMMON: SPINACH;
SOURCE   9 ORGANISM_TAXID: 3562;
SOURCE  10 ORGAN: LEAF
KEYWDS    LYASE, CARBON-CARBON, OXIDOREDUCTASE, PHOTOSYNTHESIS,
KEYWDS   2 CARBON-DIOXIDE FIXATION LYASE (CARBON-CARBON)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.KARKEHABADI,T.C.TAYLOR,I.ANDERSSON
REVDAT   3   24-FEB-09 1UPM    1       VERSN
REVDAT   2   06-NOV-03 1UPM    1       JRNL
REVDAT   1   14-OCT-03 1UPM    0
JRNL        AUTH   S.KARKEHABADI,T.C.TAYLOR,I.ANDERSSON
JRNL        TITL   CALCIUM SUPPORTS LOOP CLOSURE BUT NOT CATALYSIS IN
JRNL        TITL 2 RUBISCO
JRNL        REF    J.MOL.BIOL.                   V. 334    65 2003
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   14596800
JRNL        DOI    10.1016/J.JMB.2003.09.025
REMARK   2
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.3
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 4
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90
REMARK   3   NUMBER OF REFLECTIONS             : 251201
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.23
REMARK   3   FREE R VALUE                     : 0.20
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 11379
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 37376
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 272
REMARK   3   SOLVENT ATOMS            : 2788
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.408
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.85
REMARK   3    B22 (A**2) : -0.39
REMARK   3    B33 (A**2) : 2.23
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.364
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.210
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.994
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1UPM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  09-OCT-03.
REMARK 100 THE PDBE ID CODE IS EBI-13649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-00
REMARK 200  TEMPERATURE           (KELVIN) : 279.0
REMARK 200  PH                             : 7.80
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9386
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 226289
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0
REMARK 200  DATA REDUNDANCY                : 12.000
REMARK 200  R MERGE                    (I) : 0.08300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.15000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 4000, 0.1 M HEPES PH
REMARK 280  7.8, 10 MM CACL2, 0.2 M NACL, 50 MM NAHCO3, 1MM 2-CABP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      109.80000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      110.47100
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      109.80000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      110.47100
REMARK 290   SMTRY3   4  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: HEXADECAMRIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMRIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, B, E, H, K, O, R, V, S,
REMARK 350                    AND CHAINS: C, F, I, M, P, T, 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 400
REMARK 400 COMPOUND
REMARK 400  RUBISCO CATALYZES THE CARBOXYLATION OF D-RIBULOSE 1,5-
REMARK 400  BISPHOSPHATE AS WELL AS THE OXIDATIVE FRAGMENTATION OF
REMARK 400  PENTOSE SUBSTRATE IN PHOTORESPIRATION. THE PROTEIN IS A
REMARK 400  COMPLEX OF 8 LARGE AND 8 SMALL CHAINS.
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 B     1
REMARK 465     SER 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     MET E     1
REMARK 465     SER E     2
REMARK 465     PRO E     3
REMARK 465     GLN E     4
REMARK 465     THR E     5
REMARK 465     GLU E     6
REMARK 465     THR E     7
REMARK 465     LYS E     8
REMARK 465     MET H     1
REMARK 465     SER H     2
REMARK 465     PRO H     3
REMARK 465     GLN H     4
REMARK 465     THR H     5
REMARK 465     GLU H     6
REMARK 465     THR H     7
REMARK 465     LYS H     8
REMARK 465     MET K     1
REMARK 465     SER K     2
REMARK 465     PRO K     3
REMARK 465     GLN K     4
REMARK 465     THR K     5
REMARK 465     GLU K     6
REMARK 465     THR K     7
REMARK 465     LYS K     8
REMARK 465     MET L     1
REMARK 465     SER L     2
REMARK 465     PRO L     3
REMARK 465     GLN L     4
REMARK 465     THR L     5
REMARK 465     GLU L     6
REMARK 465     THR L     7
REMARK 465     LYS L     8
REMARK 465     MET O     1
REMARK 465     SER O     2
REMARK 465     PRO O     3
REMARK 465     GLN O     4
REMARK 465     THR O     5
REMARK 465     GLU O     6
REMARK 465     THR O     7
REMARK 465     LYS O     8
REMARK 465     MET R     1
REMARK 465     SER 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     MET V     1
REMARK 465     SER 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 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     GLU B  12    CB   CG   CD   OE1  OE2
REMARK 470     GLU E  12    CB   CG   CD   OE1  OE2
REMARK 470     GLU H  12    CB   CG   CD   OE1  OE2
REMARK 470     GLU K  12    CB   CG   CD   OE1  OE2
REMARK 470     GLU L  12    CB   CG   CD   OE1  OE2
REMARK 470     GLU O  12    CB   CG   CD   OE1  OE2
REMARK 470     GLU R  12    CB   CG   CD   OE1  OE2
REMARK 470     GLU V  12    CB   CG   CD   OE1  OE2
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   OD2  ASP K   473  -  O    HOH K  2273              1.71
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   OE1  GLU B   468     NH1  ARG O   439     4456      2.13
REMARK 500   NH1  ARG O   439     OE1  GLU B   468     4556      2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    MET C   1   N     MET C   1   CA      1.399
REMARK 500    PRO R 176   N     PRO R 176   CD      0.119
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    VAL B  69   N   -  CA  -  CB  ANGL. DEV. = -14.9 DEGREES
REMARK 500    ARG B  83   CD  -  NE  -  CZ  ANGL. DEV. =  11.8 DEGREES
REMARK 500    ARG B  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    PRO B 176   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES
REMARK 500    ARG B 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    LEU B 219   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    LEU B 219   CB  -  CG  -  CD1 ANGL. DEV. =  10.2 DEGREES
REMARK 500    CYS B 247   CA  -  CB  -  SG  ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ARG B 253   CD  -  NE  -  CZ  ANGL. DEV. =  10.7 DEGREES
REMARK 500    GLU B 259   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ARG B 285   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    HIS B 294   CB  -  CG  -  ND1 ANGL. DEV. =   8.1 DEGREES
REMARK 500    ARG B 303   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    MET C   1   N   -  CA  -  C   ANGL. DEV. = -16.6 DEGREES
REMARK 500    ARG C  53   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ASP C 105   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    VAL C 110   CA  -  CB  -  CG1 ANGL. DEV. =  10.3 DEGREES
REMARK 500    ARG E  83   CD  -  NE  -  CZ  ANGL. DEV. =  10.7 DEGREES
REMARK 500    PRO E 176   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES
REMARK 500    ARG E 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP E 203   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG E 217   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES
REMARK 500    CYS E 247   CA  -  CB  -  SG  ANGL. DEV. =  -9.2 DEGREES
REMARK 500    ARG E 253   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES
REMARK 500    ARG E 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    HIS E 294   CB  -  CG  -  ND1 ANGL. DEV. =   9.7 DEGREES
REMARK 500    ARG E 303   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES
REMARK 500    ARG E 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP E 397   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP F 105   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG H  83   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES
REMARK 500    ARG H  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG H 167   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG H 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG H 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG H 217   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES
REMARK 500    CYS H 247   CA  -  CB  -  SG  ANGL. DEV. = -10.5 DEGREES
REMARK 500    ARG H 253   CD  -  NE  -  CZ  ANGL. DEV. =  10.3 DEGREES
REMARK 500    HIS H 294   CB  -  CG  -  ND1 ANGL. DEV. =   8.6 DEGREES
REMARK 500    ARG H 350   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG H 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG H 358   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG H 360   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES
REMARK 500    ARG H 360   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    LEU I  33   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES
REMARK 500    ASP I 105   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG K  83   CD  -  NE  -  CZ  ANGL. DEV. =  10.6 DEGREES
REMARK 500    ARG K 167   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    PRO K 176   C   -  N   -  CA  ANGL. DEV. =  12.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     137 ANGLE DEVIATIONS
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 B  10      109.52     51.54
REMARK 500    GLU B  12      151.04    -49.80
REMARK 500    SER B  62      -80.04   -146.22
REMARK 500    THR B  65     -163.96   -123.04
REMARK 500    THR B  75     -166.34   -115.52
REMARK 500    CYS B 172      115.85   -179.89
REMARK 500    PRO B 176      113.86     23.48
REMARK 500    ASN B 207      -94.57   -119.72
REMARK 500    MET B 212      110.81   -164.39
REMARK 500    ALA B 296      133.46    -38.60
REMARK 500    MET B 297      -14.96     91.09
REMARK 500    VAL B 331      -56.04     72.61
REMARK 500    LYS B 356      132.34    -38.91
REMARK 500    ASP B 357       86.10   -159.90
REMARK 500    VAL B 369       54.24     34.90
REMARK 500    GLU C  13     -153.10     64.36
REMARK 500    LEU C  15       -8.06     91.09
REMARK 500    LYS C  71     -128.51     56.66
REMARK 500    SER E  10      109.04     51.50
REMARK 500    GLU E  12      150.05    -48.53
REMARK 500    THR E  26       67.42   -150.92
REMARK 500    SER E  62      -78.04   -148.32
REMARK 500    THR E  65     -159.76   -123.87
REMARK 500    THR E  75     -167.28   -115.37
REMARK 500    CYS E 172      114.40   -177.63
REMARK 500    PRO E 176      113.18     26.00
REMARK 500    ASN E 207     -100.55   -121.50
REMARK 500    MET E 212      102.14   -175.48
REMARK 500    MET E 297      -12.01     86.75
REMARK 500    VAL E 331      -59.12     72.96
REMARK 500    LYS E 356      131.01    -35.57
REMARK 500    ASP E 357       87.52   -159.22
REMARK 500    VAL E 369       52.10     37.82
REMARK 500    GLU F  13     -150.85     58.99
REMARK 500    LEU F  15       -8.85     88.67
REMARK 500    LYS F  71     -121.41     55.59
REMARK 500    SER H  10      108.74     50.49
REMARK 500    SER H  62      -75.57   -148.98
REMARK 500    THR H  65     -162.58   -126.35
REMARK 500    THR H  75     -169.20   -117.89
REMARK 500    CYS H 172      117.70   -177.55
REMARK 500    PRO H 176      113.38     24.94
REMARK 500    ASN H 207      -98.01   -119.98
REMARK 500    MET H 212      109.42   -173.63
REMARK 500    MET H 297      -11.42     92.47
REMARK 500    VAL H 331      -54.72     71.94
REMARK 500    LYS H 356      132.45    -37.57
REMARK 500    ASP H 357       85.50   -160.65
REMARK 500    VAL H 369       53.09     34.53
REMARK 500    TYR I  12       34.90   -141.70
REMARK 500    GLU I  13     -155.16     63.67
REMARK 500    LEU I  15       -8.20     90.82
REMARK 500    LYS I  71     -125.10     56.51
REMARK 500    SER K  10      107.79     51.51
REMARK 500    THR K  26       69.26   -153.67
REMARK 500    SER K  62      -77.87   -146.78
REMARK 500    THR K  65     -157.82   -122.60
REMARK 500    THR K  75     -168.16   -115.95
REMARK 500    ARG K 167      149.90   -171.15
REMARK 500    PRO K 168      151.14    -49.99
REMARK 500    CYS K 172      113.34    176.87
REMARK 500    PRO K 176      119.81     20.09
REMARK 500    ASN K 207      -93.97   -112.59
REMARK 500    MET K 212      108.66   -166.48
REMARK 500    MET K 297      -15.51     89.57
REMARK 500    VAL K 331      -57.97     71.00
REMARK 500    LYS K 356      128.52    -37.89
REMARK 500    ASP K 357       86.97   -157.70
REMARK 500    VAL K 369       53.72     38.47
REMARK 500    SER L  10      109.15     51.17
REMARK 500    THR L  26       62.53   -151.07
REMARK 500    SER L  62      -83.48   -146.61
REMARK 500    THR L  65     -161.36   -120.21
REMARK 500    THR L  75     -165.46   -111.72
REMARK 500    CYS L 172      117.20   -177.98
REMARK 500    PRO L 176      112.33     22.87
REMARK 500    ASN L 207      -96.13   -112.14
REMARK 500    MET L 212      109.97   -167.97
REMARK 500    MET L 297      -14.47     86.98
REMARK 500    VAL L 331      -64.04     74.92
REMARK 500    LYS L 356      128.21    -34.18
REMARK 500    ASP L 357       86.62   -158.01
REMARK 500    VAL L 369       54.32     35.21
REMARK 500    GLU M  13     -150.09     64.14
REMARK 500    LEU M  15      -10.18     94.78
REMARK 500    LYS M  71     -123.04     48.27
REMARK 500    SER O  10      109.55     51.18
REMARK 500    SER O  62      -77.49   -147.46
REMARK 500    THR O  65     -163.67   -120.50
REMARK 500    THR O  75     -163.87   -113.79
REMARK 500    CYS O 172      119.07   -177.51
REMARK 500    PRO O 176      113.85     23.43
REMARK 500    VAL O 206       99.28    -68.98
REMARK 500    ASN O 207      -93.82   -112.84
REMARK 500    MET O 212      116.58   -167.17
REMARK 500    MET O 297      -11.93     85.46
REMARK 500    VAL O 331      -60.87     72.62
REMARK 500    LYS O 356      131.01    -37.50
REMARK 500    ASP O 357       88.08   -157.40
REMARK 500    VAL O 369       54.43     34.88
REMARK 500    GLU P  13     -150.76     62.85
REMARK 500    LEU P  15       -6.54     90.72
REMARK 500    LYS P  71     -129.02     53.25
REMARK 500    SER R  10      109.93     49.80
REMARK 500    THR R  26       66.68   -150.15
REMARK 500    SER R  62      -72.61   -148.19
REMARK 500    THR R  65     -162.66   -123.16
REMARK 500    THR R  75     -169.92   -119.15
REMARK 500    CYS R 172      116.03   -179.57
REMARK 500    ASN R 207      -99.62   -114.07
REMARK 500    MET R 212      109.35   -169.85
REMARK 500    ALA R 296      132.76    -37.01
REMARK 500    MET R 297       -7.34     88.74
REMARK 500    VAL R 331      -58.41     66.07
REMARK 500    LYS R 356      129.47    -37.32
REMARK 500    ASP R 357       89.33   -157.26
REMARK 500    VAL R 369       52.19     36.52
REMARK 500    GLU S  13     -147.54     62.96
REMARK 500    LEU S  15       -4.38     95.57
REMARK 500    LYS S  71     -122.97     48.43
REMARK 500    GLU T  13     -153.33     63.14
REMARK 500    LEU T  15       -7.44     83.49
REMARK 500    LYS T  71     -125.03     57.49
REMARK 500    SER V  10      109.39     50.96
REMARK 500    SER V  62      -79.80   -155.97
REMARK 500    THR V  65     -159.68   -122.89
REMARK 500    THR V  75     -166.43   -113.18
REMARK 500    CYS V 172      118.96   -173.58
REMARK 500    PRO V 176      113.94     22.49
REMARK 500    ASN V 207     -101.10   -119.63
REMARK 500    MET V 212      108.22   -170.54
REMARK 500    MET V 297      -10.20     90.46
REMARK 500    VAL V 331      -58.68     74.01
REMARK 500    LYS V 356      132.53    -36.43
REMARK 500    ASP V 357       87.38   -161.17
REMARK 500    VAL V 369       51.47     37.84
REMARK 500    GLU W  13     -149.50     67.96
REMARK 500    LEU W  15       -8.55     92.61
REMARK 500    LYS W  71     -123.15     55.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 LYS B  175     PRO B  176                  -98.36
REMARK 500 LYS E  175     PRO E  176                 -101.29
REMARK 500 LYS H  175     PRO H  176                  -99.74
REMARK 500 LYS K  175     PRO K  176                  -95.81
REMARK 500 LYS L  175     PRO L  176                  -95.81
REMARK 500 LYS O  175     PRO O  176                 -100.32
REMARK 500 LYS V  175     PRO V  176                  -97.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    LYS R 175         29.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    VAL E 113        23.3      L          L   OUTSIDE RANGE
REMARK 500    VAL E 157        23.8      L          L   OUTSIDE RANGE
REMARK 500    VAL E 377        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL E 428        21.1      L          L   OUTSIDE RANGE
REMARK 500    VAL H 145        22.5      L          L   OUTSIDE RANGE
REMARK 500    VAL K 157        24.0      L          L   OUTSIDE RANGE
REMARK 500    VAL L 189        21.5      L          L   OUTSIDE RANGE
REMARK 500    VAL L 206        24.7      L          L   OUTSIDE RANGE
REMARK 500    VAL T  30        23.6      L          L   OUTSIDE RANGE
REMARK 500    VAL V 346        21.2      L          L   OUTSIDE RANGE
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                              CA B 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B 477   O6
REMARK 620 2 ASP B 203   OD1 100.6
REMARK 620 3 GLU B 204   OE1  99.7  93.6
REMARK 620 4 CAP B 477   O3   74.4 174.9  87.3
REMARK 620 5 KCX B 201   OQ2 156.0  98.1  94.1  86.8
REMARK 620 6 CAP B 477   O2   62.0 115.5 147.2  62.4  96.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA E 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 204   OE1
REMARK 620 2 CAP E 477   O2  147.0
REMARK 620 3 CAP E 477   O3   87.4  62.2
REMARK 620 4 KCX E 201   OQ2  91.9  96.5  83.4
REMARK 620 5 ASP E 203   OD1  88.4 121.5 175.5  98.3
REMARK 620 6 CAP E 477   O6   98.4  63.6  75.7 156.1 103.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA H 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP H 477   O6
REMARK 620 2 ASP H 203   OD1 101.9
REMARK 620 3 GLU H 204   OE1  96.3  91.1
REMARK 620 4 KCX H 201   OQ2 155.6 100.7  92.3
REMARK 620 5 CAP H 477   O2   64.9 119.6 145.9  95.8
REMARK 620 6 CAP H 477   O3   74.5 175.6  86.8  83.2  61.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA K 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX K 201   OQ2
REMARK 620 2 GLU K 204   OE1  95.6
REMARK 620 3 ASP K 203   OD1  98.4  88.7
REMARK 620 4 CAP K 477   O2   96.4 149.1 117.5
REMARK 620 5 CAP K 477   O3   87.2  91.1 174.4  61.3
REMARK 620 6 CAP K 477   O6  157.4 100.7  97.5  61.9  77.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA L 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 204   OE1
REMARK 620 2 CAP L 477   O6  100.6
REMARK 620 3 CAP L 477   O2  148.8  62.9
REMARK 620 4 CAP L 477   O3   90.1  76.4  61.2
REMARK 620 5 ASP L 203   OD1  88.7 100.2 119.0 176.1
REMARK 620 6 KCX L 201   OQ2  92.7 157.0  96.3  85.0  98.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA O 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX O 201   OQ2
REMARK 620 2 ASP O 203   OD1 101.7
REMARK 620 3 GLU O 204   OE1  91.7  93.0
REMARK 620 4 CAP O 477   O3   84.8 173.3  88.2
REMARK 620 5 CAP O 477   O2  100.4 114.5 146.4  62.2
REMARK 620 6 CAP O 477   O6  156.2  99.1  98.4  74.1  60.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA R 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R 203   OD1
REMARK 620 2 GLU R 204   OE1  94.1
REMARK 620 3 CAP R 477   O6   99.2 101.2
REMARK 620 4 KCX R 201   OQ2  99.2  95.0 154.4
REMARK 620 5 CAP R 477   O2  113.4 148.8  61.4  94.8
REMARK 620 6 CAP R 477   O3  173.7  90.8  75.9  84.3  60.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA V 476  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX V 201   OQ2
REMARK 620 2 ASP V 203   OD1  95.2
REMARK 620 3 GLU V 204   OE1  88.6  87.9
REMARK 620 4 CAP V 477   O2   93.5 121.9 149.7
REMARK 620 5 CAP V 477   O3   80.0 173.9  88.2  62.5
REMARK 620 6 CAP V 477   O6  155.5 106.9 102.6  65.9  78.6
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  CA B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA K 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA L 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA O 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA R 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA V 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP K 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP L 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP O 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP R 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
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: 1AA1   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH
REMARK 900  THE PRODUCT 3-PHOSPHOGLYCERATE
REMARK 900 RELATED ID: 1AUS   RELATED DB: PDB
REMARK 900  ACTIVATED UNLIGANDED SPINACH RUBISCO
REMARK 900 RELATED ID: 1IR1   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF SPINACH RIBULOSE-1,5-
REMARK 900  BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO)
REMARK 900  COMPLEXED WITH CO2, MG2+AND 2-
REMARK 900  CARBOXYARABINITOL-1,5-BISPHOSPHATE
REMARK 900 RELATED ID: 1RBO   RELATED DB: PDB
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH THE
REMARK 900  INHIBITOR 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
REMARK 900 RELATED ID: 1RCO   RELATED DB: PDB
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH THE
REMARK 900  INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-
REMARK 900  BISPHOSPHATE
REMARK 900 RELATED ID: 1RCX   RELATED DB: PDB
REMARK 900  NON-ACTIVATED SPINACH RUBISCO IN COMPLEX
REMARK 900  WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE
REMARK 900 RELATED ID: 1RXO   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH
REMARK 900  ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND
REMARK 900   CALCIUM
REMARK 900 RELATED ID: 1UPP   RELATED DB: PDB
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH 2-
REMARK 900  CARBOXYARABINITOL 2 BISPHOSPHATE AND CALCIUM.
REMARK 900 RELATED ID: 8RUC   RELATED DB: PDB
REMARK 900  ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-
REMARK 900  CARBOXYARABINITOL BISPHOSPHATE
DBREF  1UPM L    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM B    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM E    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM H    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM K    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM O    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM R    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM V    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1UPM S    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPM C    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPM F    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPM I    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPM M    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPM P    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPM T    1   123  UNP    Q43832   RBS2_SPIOL      58    180
DBREF  1UPM W    1   123  UNP    Q43832   RBS2_SPIOL      58    180
SEQADV 1UPM GLN S    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE S    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU S    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU S    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS S   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU S  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE S  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPM GLN C    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE C    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU C    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU C    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS C   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU C  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE C  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPM GLN F    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE F    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU F    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU F    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS F   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU F  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE F  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPM GLN I    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE I    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU I    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU I    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS I   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU I  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE I  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPM GLN M    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE M    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU M    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU M    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS M   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU M  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE M  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPM GLN P    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE P    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU P    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU P    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS P   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU P  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE P  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPM GLN T    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE T    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU T    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU T    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS T   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU T  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE T  113  UNP  Q43832    VAL   170 CONFLICT
SEQADV 1UPM GLN W    2  UNP  Q43832    LYS    59 CONFLICT
SEQADV 1UPM ILE W    6  UNP  Q43832    THR    63 CONFLICT
SEQADV 1UPM LEU W    7  UNP  Q43832    GLN    64 CONFLICT
SEQADV 1UPM LEU W    9  UNP  Q43832    MET    66 CONFLICT
SEQADV 1UPM LYS W   11  UNP  Q43832    ARG    68 CONFLICT
SEQADV 1UPM GLU W  109  UNP  Q43832    GLN   166 CONFLICT
SEQADV 1UPM ILE W  113  UNP  Q43832    VAL   170 CONFLICT
SEQRES   1 B  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 B  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 B  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 B  475  ALA 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 ASN LEU ASP
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 B  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 B  475  LEU 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 VAL ALA
SEQRES  12 B  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 CYS
SEQRES  18 B  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 B  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 B  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 B  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 B  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 B  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 B  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 B  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 B  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 B  475  THR GLU ILE PHE GLY ASP ASP SER VAL 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 VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 B  475  THR ILE ILE ARG GLU ALA THR 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 PRO ALA MET ASP THR VAL
SEQRES   1 C  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 C  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 C  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 C  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 C  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 C  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 C  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 C  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 C  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 C  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 E  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 E  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 E  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 E  475  ALA 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 ASN LEU ASP
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 E  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 E  475  LEU 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 VAL ALA
SEQRES  12 E  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 CYS
SEQRES  18 E  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 E  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 E  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 E  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 E  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 E  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 E  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 E  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 E  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 E  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 E  475  THR GLU ILE PHE GLY ASP ASP SER VAL 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 VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 E  475  THR ILE ILE ARG GLU ALA THR 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 PRO ALA MET ASP THR VAL
SEQRES   1 F  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 F  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 F  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 F  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 F  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 F  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 F  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 F  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 F  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 F  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 H  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 H  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 H  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 H  475  ALA 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 ASN LEU ASP
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 H  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 H  475  LEU 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 VAL ALA
SEQRES  12 H  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 CYS
SEQRES  18 H  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 H  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 H  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 H  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 H  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 H  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 H  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 H  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 H  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 H  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 H  475  THR GLU ILE PHE GLY ASP ASP SER VAL 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 VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 H  475  THR ILE ILE ARG GLU ALA THR 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 PRO ALA MET ASP THR VAL
SEQRES   1 I  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 I  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 I  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 I  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 I  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 I  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 I  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 I  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 I  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 I  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 K  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 K  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 K  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 K  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 K  475  ALA 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 ASN LEU ASP
SEQRES   7 K  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 K  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 K  475  LEU 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 VAL ALA
SEQRES  12 K  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 K  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 CYS
SEQRES  18 K  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 K  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 K  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 K  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 K  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 K  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 K  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 K  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 K  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 K  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 K  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 K  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 K  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 K  475  THR GLU ILE PHE GLY ASP ASP SER VAL 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 VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 K  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 K  475  THR ILE ILE ARG GLU ALA THR 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 PRO ALA MET ASP THR VAL
SEQRES   1 L  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 L  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 L  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 L  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 L  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 L  475  TRP THR THR VAL TRP THR ASP GLY LEU THR ASN LEU ASP
SEQRES   7 L  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 L  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 L  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 L  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 L  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA
SEQRES  12 L  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 L  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 L  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 L  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 L  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES  17 L  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 L  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 L  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 L  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 L  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 L  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 L  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 L  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 L  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 L  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 L  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 L  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 L  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 L  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 L  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 L  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 L  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 L  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 L  475  THR ILE ILE ARG GLU ALA THR LYS TRP SER PRO GLU LEU
SEQRES  36 L  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 L  475  PHE PRO ALA MET ASP THR VAL
SEQRES   1 M  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 M  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 M  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 M  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 M  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 M  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 M  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 M  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 M  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 M  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 O  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 O  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 O  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 O  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 O  475  ALA 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 ASN LEU ASP
SEQRES   7 O  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 O  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 O  475  LEU 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 VAL ALA
SEQRES  12 O  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 O  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 CYS
SEQRES  18 O  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 O  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 O  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 O  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 O  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 O  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 O  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 O  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 O  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 O  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 O  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 O  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 O  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 O  475  THR GLU ILE PHE GLY ASP ASP SER VAL 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 VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 O  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 O  475  THR ILE ILE ARG GLU ALA THR 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 PRO ALA MET ASP THR VAL
SEQRES   1 P  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 P  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 P  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 P  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 P  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 P  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 P  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 P  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 P  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 P  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 R  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 R  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 R  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 R  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 R  475  ALA 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 ASN LEU ASP
SEQRES   7 R  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 R  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 R  475  LEU 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 VAL ALA
SEQRES  12 R  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 R  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 CYS
SEQRES  18 R  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 R  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 R  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 R  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 R  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 R  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 R  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 R  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 R  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 R  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 R  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 R  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 R  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 R  475  THR GLU ILE PHE GLY ASP ASP SER VAL 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 VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 R  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 R  475  THR ILE ILE ARG GLU ALA THR 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 PRO ALA MET ASP THR VAL
SEQRES   1 S  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 S  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 S  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 S  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 S  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 S  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 S  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 S  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 S  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 S  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 T  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 T  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 T  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 T  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 T  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 T  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 T  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 T  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 T  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 T  123  TYR LYS PRO ALA GLY TYR
SEQRES   1 V  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLU PHE
SEQRES   2 V  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 V  475  PRO GLU TYR GLU THR LEU ASP THR ASP ILE LEU ALA ALA
SEQRES   4 V  475  PHE ARG VAL SER PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 V  475  ALA 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 ASN LEU ASP
SEQRES   7 V  475  ARG TYR LYS GLY ARG CYS TYR HIS ILE GLU PRO VAL ALA
SEQRES   8 V  475  GLY GLU GLU ASN GLN TYR ILE CYS TYR VAL ALA TYR PRO
SEQRES   9 V  475  LEU 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 VAL ALA
SEQRES  12 V  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 V  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO 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 CYS
SEQRES  18 V  475  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 V  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 V  475  GLU ASP MET MET LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 V  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 V  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 V  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 V  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 V  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 V  475  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 V  475  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 V  475  ASP TYR THR GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 V  475  THR GLN SER TRP VAL SER THR PRO GLY VAL LEU PRO VAL
SEQRES  30 V  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 V  475  THR GLU ILE PHE GLY ASP ASP SER VAL 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 VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 V  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 V  475  THR ILE ILE ARG GLU ALA THR 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 PRO ALA MET ASP THR VAL
SEQRES   1 W  123  MET GLN VAL TRP PRO ILE LEU ASN LEU LYS LYS TYR GLU
SEQRES   2 W  123  THR LEU SER TYR LEU PRO PRO LEU THR THR ASP GLN LEU
SEQRES   3 W  123  ALA ARG GLN VAL ASP TYR LEU LEU ASN ASN LYS TRP VAL
SEQRES   4 W  123  PRO CYS LEU GLU PHE GLU THR ASP HIS GLY PHE VAL TYR
SEQRES   5 W  123  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 W  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 W  123  ASP PRO ALA GLN VAL LEU ASN GLU LEU GLU GLU CYS LYS
SEQRES   8 W  123  LYS GLU TYR PRO ASN ALA PHE ILE ARG ILE ILE GLY PHE
SEQRES   9 W  123  ASP SER ASN ARG GLU VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 W  123  TYR LYS PRO ALA GLY TYR
MODRES 1UPM KCX L  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPM KCX B  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPM KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPM KCX H  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPM KCX K  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPM KCX O  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPM KCX R  201  LYS  LYSINE NZ-CARBOXYLIC ACID
MODRES 1UPM KCX V  201  LYS  LYSINE NZ-CARBOXYLIC ACID
HET    KCX  B 201      12
HET    KCX  E 201      12
HET    KCX  H 201      12
HET    KCX  K 201      12
HET    KCX  L 201      12
HET    KCX  O 201      12
HET    KCX  R 201      12
HET    KCX  V 201      12
HET     CA  B 476       1
HET     CA  E 476       1
HET     CA  H 476       1
HET     CA  K 476       1
HET     CA  L 476       1
HET     CA  O 476       1
HET     CA  R 476       1
HET     CA  V 476       1
HET    CAP  B 477      21
HET    CAP  E 477      21
HET    CAP  H 477      21
HET    CAP  K 477      21
HET    CAP  L 477      21
HET    CAP  O 477      21
HET    CAP  R 477      21
HET    CAP  V 477      21
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM      CA CALCIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
FORMUL   1  KCX    8(C7 H14 N2 O4)
FORMUL  17   CA    8(CA 2+)
FORMUL  25  CAP    8(C6 H14 O13 P2)
FORMUL  33  HOH   *2788(H2 O1)
HELIX    1   1 TYR B   20  TYR B   25  1                                   6
HELIX    2   2 PRO B   49  SER B   61  1                                  13
HELIX    3   3 VAL B   69  THR B   75  5                                   7
HELIX    4   4 ASN B   76  LYS B   81  1                                   6
HELIX    5   5 PRO B  104  PHE B  108  5                                   5
HELIX    6   6 SER B  112  VAL B  121  1                                  10
HELIX    7   7 ASN B  123  GLY B  126  5                                   4
HELIX    8   8 PRO B  141  LYS B  146  1                                   6
HELIX    9   9 GLY B  154  ASN B  163  1                                  10
HELIX   10  10 SER B  181  GLY B  195  1                                  15
HELIX   11  11 ARG B  213  GLY B  233  1                                  21
HELIX   12  12 THR B  246  GLY B  261  1                                  16
HELIX   13  13 TYR B  269  GLY B  288  1                                  20
HELIX   14  14 MET B  297  ARG B  303  1                                   7
HELIX   15  15 HIS B  310  GLY B  322  1                                  13
HELIX   16  16 GLU B  338  ASP B  351  1                                  14
HELIX   17  17 ARG B  358  GLY B  361  5                                   4
HELIX   18  18 HIS B  383  TRP B  385  5                                   3
HELIX   19  19 HIS B  386  GLY B  395  1                                  10
HELIX   20  20 GLY B  403  GLY B  408  1                                   6
HELIX   21  21 GLY B  412  GLU B  433  1                                  22
HELIX   22  22 ASP B  436  LYS B  450  1                                  15
HELIX   23  23 SER B  452  LYS B  463  1                                  12
HELIX   24  24 THR C   22  ASN C   36  1                                  15
HELIX   25  25 ASP C   79  TYR C   94  1                                  16
HELIX   26  26 TYR E   20  TYR E   25  1                                   6
HELIX   27  27 PRO E   49  SER E   61  1                                  13
HELIX   28  28 VAL E   69  THR E   75  5                                   7
HELIX   29  29 ASN E   76  LYS E   81  1                                   6
HELIX   30  30 PRO E  104  PHE E  108  5                                   5
HELIX   31  31 SER E  112  GLY E  122  1                                  11
HELIX   32  32 ASN E  123  GLY E  126  5                                   4
HELIX   33  33 PRO E  141  LYS E  146  1                                   6
HELIX   34  34 GLY E  154  ASN E  163  1                                  10
HELIX   35  35 SER E  181  GLY E  195  1                                  15
HELIX   36  36 ARG E  213  GLY E  233  1                                  21
HELIX   37  37 THR E  246  GLY E  261  1                                  16
HELIX   38  38 TYR E  269  GLY E  288  1                                  20
HELIX   39  39 MET E  297  ARG E  303  1                                   7
HELIX   40  40 HIS E  310  GLY E  322  1                                  13
HELIX   41  41 GLU E  338  ASP E  351  1                                  14
HELIX   42  42 ARG E  358  GLY E  361  5                                   4
HELIX   43  43 HIS E  383  TRP E  385  5                                   3
HELIX   44  44 HIS E  386  GLY E  395  1                                  10
HELIX   45  45 GLY E  403  GLY E  408  1                                   6
HELIX   46  46 GLY E  412  GLU E  433  1                                  22
HELIX   47  47 ASP E  436  LYS E  450  1                                  15
HELIX   48  48 SER E  452  LYS E  463  1                                  12
HELIX   49  49 THR F   22  ASN F   36  1                                  15
HELIX   50  50 ASP F   79  TYR F   94  1                                  16
HELIX   51  51 TYR H   20  TYR H   25  1                                   6
HELIX   52  52 PRO H   49  SER H   61  1                                  13
HELIX   53  53 VAL H   69  THR H   75  5                                   7
HELIX   54  54 ASN H   76  LYS H   81  1                                   6
HELIX   55  55 PRO H  104  PHE H  108  5                                   5
HELIX   56  56 SER H  112  GLY H  122  1                                  11
HELIX   57  57 ASN H  123  GLY H  126  5                                   4
HELIX   58  58 PRO H  141  LYS H  146  1                                   6
HELIX   59  59 GLY H  154  ASN H  163  1                                  10
HELIX   60  60 SER H  181  GLY H  195  1                                  15
HELIX   61  61 ARG H  213  GLY H  233  1                                  21
HELIX   62  62 THR H  246  GLY H  261  1                                  16
HELIX   63  63 TYR H  269  GLY H  288  1                                  20
HELIX   64  64 MET H  297  ARG H  303  1                                   7
HELIX   65  65 HIS H  310  GLY H  322  1                                  13
HELIX   66  66 GLU H  338  ASP H  351  1                                  14
HELIX   67  67 ARG H  358  GLY H  361  5                                   4
HELIX   68  68 HIS H  383  TRP H  385  5                                   3
HELIX   69  69 HIS H  386  GLY H  395  1                                  10
HELIX   70  70 GLY H  403  GLY H  408  1                                   6
HELIX   71  71 GLY H  412  GLU H  433  1                                  22
HELIX   72  72 ASP H  436  LYS H  450  1                                  15
HELIX   73  73 SER H  452  LYS H  463  1                                  12
HELIX   74  74 THR I   22  ASN I   36  1                                  15
HELIX   75  75 ASP I   79  TYR I   94  1                                  16
HELIX   76  76 TYR K   20  TYR K   25  1                                   6
HELIX   77  77 PRO K   49  SER K   61  1                                  13
HELIX   78  78 VAL K   69  THR K   75  5                                   7
HELIX   79  79 ASN K   76  LYS K   81  1                                   6
HELIX   80  80 PRO K  104  PHE K  108  5                                   5
HELIX   81  81 SER K  112  VAL K  121  1                                  10
HELIX   82  82 ASN K  123  GLY K  126  5                                   4
HELIX   83  83 PRO K  141  LYS K  146  1                                   6
HELIX   84  84 GLY K  154  ASN K  163  1                                  10
HELIX   85  85 SER K  181  ARG K  194  1                                  14
HELIX   86  86 ARG K  213  GLY K  233  1                                  21
HELIX   87  87 THR K  246  GLY K  261  1                                  16
HELIX   88  88 TYR K  269  GLY K  288  1                                  20
HELIX   89  89 MET K  297  ARG K  303  1                                   7
HELIX   90  90 HIS K  310  GLY K  322  1                                  13
HELIX   91  91 GLU K  338  ASP K  351  1                                  14
HELIX   92  92 ARG K  358  GLY K  361  5                                   4
HELIX   93  93 HIS K  383  TRP K  385  5                                   3
HELIX   94  94 HIS K  386  GLY K  395  1                                  10
HELIX   95  95 GLY K  403  GLY K  408  1                                   6
HELIX   96  96 GLY K  412  GLU K  433  1                                  22
HELIX   97  97 ASP K  436  LYS K  450  1                                  15
HELIX   98  98 SER K  452  LYS K  463  1                                  12
HELIX   99  99 TYR L   20  TYR L   25  1                                   6
HELIX  100 100 PRO L   49  SER L   61  1                                  13
HELIX  101 101 VAL L   69  THR L   75  5                                   7
HELIX  102 102 ASN L   76  LYS L   81  1                                   6
HELIX  103 103 PRO L  104  PHE L  108  5                                   5
HELIX  104 104 SER L  112  VAL L  121  1                                  10
HELIX  105 105 ASN L  123  GLY L  126  5                                   4
HELIX  106 106 PRO L  141  LYS L  146  1                                   6
HELIX  107 107 GLY L  154  ASN L  163  1                                  10
HELIX  108 108 SER L  181  ARG L  194  1                                  14
HELIX  109 109 ARG L  213  GLY L  233  1                                  21
HELIX  110 110 THR L  246  GLY L  261  1                                  16
HELIX  111 111 TYR L  269  GLY L  288  1                                  20
HELIX  112 112 MET L  297  ARG L  303  1                                   7
HELIX  113 113 HIS L  310  GLY L  322  1                                  13
HELIX  114 114 GLU L  338  ASP L  351  1                                  14
HELIX  115 115 ARG L  358  GLY L  361  5                                   4
HELIX  116 116 HIS L  383  TRP L  385  5                                   3
HELIX  117 117 HIS L  386  GLY L  395  1                                  10
HELIX  118 118 GLY L  403  GLY L  408  1                                   6
HELIX  119 119 GLY L  412  GLU L  433  1                                  22
HELIX  120 120 ASP L  436  LYS L  450  1                                  15
HELIX  121 121 SER L  452  LYS L  463  1                                  12
HELIX  122 122 THR M   22  ASN M   36  1                                  15
HELIX  123 123 ASP M   79  TYR M   94  1                                  16
HELIX  124 124 TYR O   20  TYR O   25  1                                   6
HELIX  125 125 PRO O   49  SER O   61  1                                  13
HELIX  126 126 VAL O   69  THR O   75  5                                   7
HELIX  127 127 ASN O   76  LYS O   81  1                                   6
HELIX  128 128 PRO O  104  PHE O  108  5                                   5
HELIX  129 129 SER O  112  VAL O  121  1                                  10
HELIX  130 130 ASN O  123  GLY O  126  5                                   4
HELIX  131 131 PRO O  141  LYS O  146  1                                   6
HELIX  132 132 GLY O  154  ASN O  163  1                                  10
HELIX  133 133 SER O  181  GLY O  195  1                                  15
HELIX  134 134 ARG O  213  GLY O  233  1                                  21
HELIX  135 135 THR O  246  GLY O  261  1                                  16
HELIX  136 136 TYR O  269  GLY O  288  1                                  20
HELIX  137 137 MET O  297  ARG O  303  1                                   7
HELIX  138 138 HIS O  310  GLY O  322  1                                  13
HELIX  139 139 GLU O  338  ASP O  351  1                                  14
HELIX  140 140 ARG O  358  GLY O  361  5                                   4
HELIX  141 141 HIS O  383  TRP O  385  5                                   3
HELIX  142 142 HIS O  386  GLY O  395  1                                  10
HELIX  143 143 GLY O  403  GLY O  408  1                                   6
HELIX  144 144 GLY O  412  GLU O  433  1                                  22
HELIX  145 145 ASP O  436  THR O  449  1                                  14
HELIX  146 146 SER O  452  LYS O  463  1                                  12
HELIX  147 147 THR P   22  ASN P   36  1                                  15
HELIX  148 148 ASP P   79  TYR P   94  1                                  16
HELIX  149 149 TYR R   20  TYR R   25  1                                   6
HELIX  150 150 PRO R   49  SER R   61  1                                  13
HELIX  151 151 VAL R   69  THR R   75  5                                   7
HELIX  152 152 ASN R   76  LYS R   81  1                                   6
HELIX  153 153 PRO R  104  PHE R  108  5                                   5
HELIX  154 154 SER R  112  VAL R  121  1                                  10
HELIX  155 155 ASN R  123  GLY R  126  5                                   4
HELIX  156 156 PRO R  141  LYS R  146  1                                   6
HELIX  157 157 GLY R  154  ASN R  163  1                                  10
HELIX  158 158 SER R  181  ARG R  194  1                                  14
HELIX  159 159 ARG R  213  GLY R  233  1                                  21
HELIX  160 160 THR R  246  GLY R  261  1                                  16
HELIX  161 161 TYR R  269  GLY R  288  1                                  20
HELIX  162 162 MET R  297  ARG R  303  1                                   7
HELIX  163 163 HIS R  310  GLY R  322  1                                  13
HELIX  164 164 GLU R  338  ASP R  351  1                                  14
HELIX  165 165 ARG R  358  GLY R  361  5                                   4
HELIX  166 166 HIS R  383  TRP R  385  5                                   3
HELIX  167 167 HIS R  386  GLY R  395  1                                  10
HELIX  168 168 GLY R  403  GLY R  408  1                                   6
HELIX  169 169 GLY R  412  GLU R  433  1                                  22
HELIX  170 170 ASP R  436  LYS R  450  1                                  15
HELIX  171 171 SER R  452  LYS R  463  1                                  12
HELIX  172 172 THR S   22  ASN S   36  1                                  15
HELIX  173 173 ASP S   79  TYR S   94  1                                  16
HELIX  174 174 THR T   22  ASN T   36  1                                  15
HELIX  175 175 ASP T   79  TYR T   94  1                                  16
HELIX  176 176 TYR V   20  TYR V   25  1                                   6
HELIX  177 177 PRO V   49  SER V   61  1                                  13
HELIX  178 178 VAL V   69  THR V   75  5                                   7
HELIX  179 179 ASN V   76  LYS V   81  1                                   6
HELIX  180 180 PRO V  104  PHE V  108  5                                   5
HELIX  181 181 SER V  112  GLY V  122  1                                  11
HELIX  182 182 ASN V  123  GLY V  126  5                                   4
HELIX  183 183 PRO V  141  LYS V  146  1                                   6
HELIX  184 184 GLY V  154  ASN V  163  1                                  10
HELIX  185 185 SER V  181  GLY V  195  1                                  15
HELIX  186 186 ARG V  213  GLY V  233  1                                  21
HELIX  187 187 THR V  246  GLY V  261  1                                  16
HELIX  188 188 TYR V  269  GLY V  288  1                                  20
HELIX  189 189 MET V  297  ARG V  303  1                                   7
HELIX  190 190 HIS V  310  GLY V  322  1                                  13
HELIX  191 191 GLU V  338  ASP V  351  1                                  14
HELIX  192 192 ARG V  358  GLY V  361  5                                   4
HELIX  193 193 HIS V  383  TRP V  385  5                                   3
HELIX  194 194 HIS V  386  GLY V  395  1                                  10
HELIX  195 195 GLY V  403  GLY V  408  1                                   6
HELIX  196 196 GLY V  412  GLU V  433  1                                  22
HELIX  197 197 ASP V  436  LYS V  450  1                                  15
HELIX  198 198 SER V  452  LYS V  463  1                                  12
HELIX  199 199 THR W   22  ASN W   36  1                                  15
HELIX  200 200 ASP W   79  TYR W   94  1                                  16
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  SER B  43
SHEET    5  BA 5 GLY B 308  MET 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 VAL B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171
SHEET    3  BB 8 LEU B 375  SER B 379  1  O  PRO B 376   N  VAL B 399
SHEET    4  BB 8 HIS B 325  HIS B 327  1  O  ILE B 326   N  VAL B 377
SHEET    5  BB 8 LEU 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  VAL 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  THR B 354  0
SHEET    2  BC 2 GLN B 366  SER B 367 -1  O  GLN B 366   N  THR B 354
SHEET    1  CA 4 THR C  68  TRP C  70  0
SHEET    2  CA 4 VAL C  39  GLU C  45 -1  O  LEU C  42   N  TRP C  70
SHEET    3  CA 4 PHE C  98  ASP C 105 -1  O  PHE C  98   N  GLU C  45
SHEET    4  CA 4 VAL C 110  TYR C 118 -1  O  VAL C 110   N  ASP C 105
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  SER E  43
SHEET    5  EA 5 GLY E 308  MET 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 VAL E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171
SHEET    3  EB 8 LEU E 375  SER E 379  1  O  PRO E 376   N  VAL E 399
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  ILE E 326   N  VAL E 377
SHEET    5  EB 8 LEU 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  VAL 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  THR E 354  0
SHEET    2  EC 2 GLN E 366  SER E 367 -1  O  GLN E 366   N  THR E 354
SHEET    1  FA 4 THR F  68  TRP F  70  0
SHEET    2  FA 4 VAL F  39  GLU F  45 -1  O  LEU F  42   N  TRP F  70
SHEET    3  FA 4 PHE F  98  ASP F 105 -1  O  PHE F  98   N  GLU F  45
SHEET    4  FA 4 VAL F 110  TYR F 118 -1  O  VAL F 110   N  ASP F 105
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  SER H  43
SHEET    5  HA 5 GLY H 308  MET 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 VAL H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171
SHEET    3  HB 8 LEU H 375  SER H 379  1  O  PRO H 376   N  VAL H 399
SHEET    4  HB 8 HIS H 325  HIS H 327  1  O  ILE H 326   N  VAL H 377
SHEET    5  HB 8 LEU 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  VAL 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  THR H 354  0
SHEET    2  HC 2 GLN H 366  SER H 367 -1  O  GLN H 366   N  THR H 354
SHEET    1  IA 4 THR I  68  TRP I  70  0
SHEET    2  IA 4 VAL I  39  GLU I  45 -1  O  LEU I  42   N  TRP I  70
SHEET    3  IA 4 PHE I  98  ASP I 105 -1  O  PHE I  98   N  GLU I  45
SHEET    4  IA 4 VAL I 110  TYR I 118 -1  O  VAL I 110   N  ASP I 105
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  SER K  43
SHEET    5  KA 5 GLY K 308  MET 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 VAL K 399  GLN K 401  1  O  LEU K 400   N  GLY K 171
SHEET    3  KB 8 LEU K 375  SER K 379  1  O  PRO K 376   N  VAL K 399
SHEET    4  KB 8 HIS K 325  HIS K 327  1  O  ILE K 326   N  VAL K 377
SHEET    5  KB 8 LEU 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  VAL 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  THR K 354  0
SHEET    2  KC 2 GLN K 366  SER K 367 -1  O  GLN K 366   N  THR K 354
SHEET    1  LA 5 ARG L  83  PRO L  89  0
SHEET    2  LA 5 TYR L  97  TYR L 103 -1  O  ILE L  98   N  GLU L  88
SHEET    3  LA 5 ILE L  36  PRO L  44 -1  O  ILE L  36   N  TYR L 103
SHEET    4  LA 5 LEU L 130  ARG L 139 -1  N  ARG L 131   O  SER L  43
SHEET    5  LA 5 GLY L 308  MET L 309  1  O  GLY L 308   N  LEU L 135
SHEET    1  LB 8 LEU L 169  GLY L 171  0
SHEET    2  LB 8 VAL L 399  GLN L 401  1  O  LEU L 400   N  GLY L 171
SHEET    3  LB 8 LEU L 375  SER L 379  1  O  PRO L 376   N  VAL L 399
SHEET    4  LB 8 HIS L 325  HIS L 327  1  O  ILE L 326   N  VAL L 377
SHEET    5  LB 8 LEU L 290  HIS L 294  1  O  ILE L 293   N  HIS L 327
SHEET    6  LB 8 ILE L 264  ASP L 268  1  O  VAL L 265   N  HIS L 292
SHEET    7  LB 8 GLY L 237  ASN L 241  1  O  LEU L 240   N  MET L 266
SHEET    8  LB 8 PHE L 199  KCX L 201  1  O  THR L 200   N  TYR L 239
SHEET    1  LC 2 TYR L 353  THR L 354  0
SHEET    2  LC 2 GLN L 366  SER L 367 -1  O  GLN L 366   N  THR L 354
SHEET    1  MA 4 THR M  68  MET M  69  0
SHEET    2  MA 4 VAL M  39  GLU M  45 -1  O  PHE M  44   N  THR M  68
SHEET    3  MA 4 PHE M  98  ASP M 105 -1  O  PHE M  98   N  GLU M  45
SHEET    4  MA 4 VAL M 110  TYR M 118 -1  O  VAL M 110   N  ASP M 105
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  SER O  43
SHEET    5  OA 5 GLY O 308  MET 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 VAL O 399  GLN O 401  1  O  LEU O 400   N  GLY O 171
SHEET    3  OB 8 LEU O 375  SER O 379  1  O  PRO O 376   N  VAL O 399
SHEET    4  OB 8 HIS O 325  HIS O 327  1  O  ILE O 326   N  VAL O 377
SHEET    5  OB 8 LEU 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  VAL 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  THR O 354  0
SHEET    2  OC 2 GLN O 366  SER O 367 -1  O  GLN O 366   N  THR O 354
SHEET    1  PA 4 THR P  68  TRP P  70  0
SHEET    2  PA 4 VAL P  39  GLU P  45 -1  O  LEU P  42   N  TRP P  70
SHEET    3  PA 4 PHE P  98  ASP P 105 -1  O  PHE P  98   N  GLU P  45
SHEET    4  PA 4 VAL P 110  TYR P 118 -1  O  VAL P 110   N  ASP P 105
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  SER R  43
SHEET    5  RA 5 GLY R 308  MET 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 VAL R 399  GLN R 401  1  O  LEU R 400   N  GLY R 171
SHEET    3  RB 8 LEU R 375  SER R 379  1  O  PRO R 376   N  VAL R 399
SHEET    4  RB 8 HIS R 325  HIS R 327  1  O  ILE R 326   N  VAL R 377
SHEET    5  RB 8 LEU 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  VAL 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  THR R 354  0
SHEET    2  RC 2 GLN R 366  SER R 367 -1  O  GLN R 366   N  THR R 354
SHEET    1  SA 4 THR S  68  TRP S  70  0
SHEET    2  SA 4 VAL S  39  GLU S  45 -1  O  LEU S  42   N  TRP S  70
SHEET    3  SA 4 PHE S  98  ASP S 105 -1  O  PHE S  98   N  GLU S  45
SHEET    4  SA 4 VAL S 110  TYR S 118 -1  O  VAL S 110   N  ASP S 105
SHEET    1  TA 4 THR T  68  TRP T  70  0
SHEET    2  TA 4 VAL T  39  GLU T  45 -1  O  LEU T  42   N  TRP T  70
SHEET    3  TA 4 PHE T  98  ASP T 105 -1  O  PHE T  98   N  GLU T  45
SHEET    4  TA 4 VAL T 110  TYR T 118 -1  O  VAL T 110   N  ASP T 105
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  SER V  43
SHEET    5  VA 5 GLY V 308  MET 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 VAL V 399  GLN V 401  1  O  LEU V 400   N  GLY V 171
SHEET    3  VB 8 LEU V 375  SER V 379  1  O  PRO V 376   N  VAL V 399
SHEET    4  VB 8 HIS V 325  HIS V 327  1  O  ILE V 326   N  VAL V 377
SHEET    5  VB 8 LEU 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  VAL 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  THR V 354  0
SHEET    2  VC 2 GLN V 366  SER V 367 -1  O  GLN V 366   N  THR V 354
SHEET    1  WA 4 THR W  68  TRP W  70  0
SHEET    2  WA 4 VAL W  39  GLU W  45 -1  O  LEU W  42   N  TRP W  70
SHEET    3  WA 4 PHE W  98  ASP W 105 -1  O  PHE W  98   N  GLU W  45
SHEET    4  WA 4 VAL W 110  TYR W 118 -1  O  VAL W 110   N  ASP W 105
SSBOND   1 CYS B  247    CYS L  247                          1555   1555  2.57
SSBOND   2 CYS E  247    CYS H  247                          1555   1555  2.61
SSBOND   3 CYS K  247    CYS O  247                          1555   1555  2.50
SSBOND   4 CYS R  247    CYS V  247                          1555   1555  2.65
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.32
LINK        CA    CA B 476                 O6  CAP B 477     1555   1555  2.70
LINK        CA    CA B 476                 OD1 ASP B 203     1555   1555  2.68
LINK        CA    CA B 476                 OE1 GLU B 204     1555   1555  2.59
LINK        CA    CA B 476                 O3  CAP B 477     1555   1555  2.79
LINK        CA    CA B 476                 OQ2 KCX B 201     1555   1555  2.65
LINK        CA    CA B 476                 O2  CAP B 477     1555   1555  2.77
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.31
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.34
LINK        CA    CA E 476                 OE1 GLU E 204     1555   1555  2.54
LINK        CA    CA E 476                 O2  CAP E 477     1555   1555  2.74
LINK        CA    CA E 476                 O3  CAP E 477     1555   1555  2.79
LINK        CA    CA E 476                 OQ2 KCX E 201     1555   1555  2.70
LINK        CA    CA E 476                 OD1 ASP E 203     1555   1555  2.69
LINK        CA    CA E 476                 O6  CAP E 477     1555   1555  2.73
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.34
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.33
LINK        CA    CA H 476                 O6  CAP H 477     1555   1555  2.72
LINK        CA    CA H 476                 OD1 ASP H 203     1555   1555  2.68
LINK        CA    CA H 476                 OE1 GLU H 204     1555   1555  2.54
LINK        CA    CA H 476                 OQ2 KCX H 201     1555   1555  2.69
LINK        CA    CA H 476                 O2  CAP H 477     1555   1555  2.76
LINK        CA    CA H 476                 O3  CAP H 477     1555   1555  2.74
LINK         C   THR K 200                 N   KCX K 201     1555   1555  1.32
LINK         C   KCX K 201                 N   ASP K 202     1555   1555  1.32
LINK        CA    CA K 476                 O6  CAP K 477     1555   1555  2.73
LINK        CA    CA K 476                 O2  CAP K 477     1555   1555  2.76
LINK        CA    CA K 476                 OD1 ASP K 203     1555   1555  2.76
LINK        CA    CA K 476                 O3  CAP K 477     1555   1555  2.71
LINK        CA    CA K 476                 OE1 GLU K 204     1555   1555  2.49
LINK        CA    CA K 476                 OQ2 KCX K 201     1555   1555  2.65
LINK         C   THR L 200                 N   KCX L 201     1555   1555  1.33
LINK         C   KCX L 201                 N   ASP L 202     1555   1555  1.33
LINK        CA    CA L 476                 O6  CAP L 477     1555   1555  2.71
LINK        CA    CA L 476                 OE1 GLU L 204     1555   1555  2.53
LINK        CA    CA L 476                 O2  CAP L 477     1555   1555  2.72
LINK        CA    CA L 476                 O3  CAP L 477     1555   1555  2.76
LINK        CA    CA L 476                 OD1 ASP L 203     1555   1555  2.72
LINK        CA    CA L 476                 OQ2 KCX L 201     1555   1555  2.65
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        CA    CA O 476                 O2  CAP O 477     1555   1555  2.79
LINK        CA    CA O 476                 O6  CAP O 477     1555   1555  2.77
LINK        CA    CA O 476                 O3  CAP O 477     1555   1555  2.75
LINK        CA    CA O 476                 OQ2 KCX O 201     1555   1555  2.65
LINK        CA    CA O 476                 OD1 ASP O 203     1555   1555  2.71
LINK        CA    CA O 476                 OE1 GLU O 204     1555   1555  2.53
LINK         C   THR R 200                 N   KCX R 201     1555   1555  1.32
LINK         C   KCX R 201                 N   ASP R 202     1555   1555  1.33
LINK        CA    CA R 476                 O3  CAP R 477     1555   1555  2.77
LINK        CA    CA R 476                 OD1 ASP R 203     1555   1555  2.69
LINK        CA    CA R 476                 OE1 GLU R 204     1555   1555  2.49
LINK        CA    CA R 476                 O6  CAP R 477     1555   1555  2.72
LINK        CA    CA R 476                 OQ2 KCX R 201     1555   1555  2.71
LINK        CA    CA R 476                 O2  CAP R 477     1555   1555  2.84
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        CA    CA V 476                 OD1 ASP V 203     1555   1555  2.76
LINK        CA    CA V 476                 OE1 GLU V 204     1555   1555  2.56
LINK        CA    CA V 476                 O2  CAP V 477     1555   1555  2.73
LINK        CA    CA V 476                 O3  CAP V 477     1555   1555  2.80
LINK        CA    CA V 476                 O6  CAP V 477     1555   1555  2.64
LINK        CA    CA V 476                 OQ2 KCX V 201     1555   1555  2.75
CISPEP   1 LYS R  175    PRO R  176          0        22.30
SITE     1 AC1  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204
SITE     2 AC1  5 CAP B 477
SITE     1 AC2  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204
SITE     2 AC2  5 CAP E 477
SITE     1 AC3  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204
SITE     2 AC3  5 CAP H 477
SITE     1 AC4  5 LYS K 177  KCX K 201  ASP K 203  GLU K 204
SITE     2 AC4  5 CAP K 477
SITE     1 AC5  5 LYS L 177  KCX L 201  ASP L 203  GLU L 204
SITE     2 AC5  5 CAP L 477
SITE     1 AC6  5 LYS O 177  KCX O 201  ASP O 203  GLU O 204
SITE     2 AC6  5 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  5 LYS V 177  KCX V 201  ASP V 203  GLU V 204
SITE     2 AC8  5 CAP V 477
SITE     1 AC9 26 THR B 173  LYS B 175  LYS B 177  KCX B 201
SITE     2 AC9 26 HIS B 294  ARG B 295  HIS B 327  LYS B 334
SITE     3 AC9 26 LEU B 335  SER B 379  GLY B 380  GLY B 381
SITE     4 AC9 26 GLY B 403  GLY B 404   CA B 476  HOH B2119
SITE     5 AC9 26 HOH B2222  HOH B2259  HOH B2260  HOH B2261
SITE     6 AC9 26 HOH B2262  HOH B2263  GLU L  60  THR L  65
SITE     7 AC9 26 TRP L  66  ASN L 123
SITE     1 BC1 27 THR E 173  LYS E 175  LYS E 177  KCX E 201
SITE     2 BC1 27 GLU E 204  HIS E 294  ARG E 295  HIS E 327
SITE     3 BC1 27 LYS E 334  LEU E 335  SER E 379  GLY E 380
SITE     4 BC1 27 GLY E 381  GLY E 403  GLY E 404   CA E 476
SITE     5 BC1 27 HOH E2110  HOH E2180  HOH E2226  HOH E2228
SITE     6 BC1 27 HOH E2295  HOH E2296  HOH E2297  GLU H  60
SITE     7 BC1 27 THR H  65  TRP H  66  ASN H 123
SITE     1 BC2 28 GLU E  60  THR E  65  TRP E  66  ASN E 123
SITE     2 BC2 28 HOH E2040  THR H 173  LYS H 175  LYS H 177
SITE     3 BC2 28 KCX H 201  GLU H 204  HIS H 294  ARG H 295
SITE     4 BC2 28 HIS H 327  LYS H 334  LEU H 335  SER H 379
SITE     5 BC2 28 GLY H 380  GLY H 381  GLY H 403  GLY H 404
SITE     6 BC2 28  CA H 476  HOH H2112  HOH H2168  HOH H2211
SITE     7 BC2 28 HOH H2212  HOH H2221  HOH H2245  HOH H2246
SITE     1 BC3 26 THR K 173  LYS K 175  LYS K 177  KCX K 201
SITE     2 BC3 26 HIS K 294  ARG K 295  HIS K 327  LYS K 334
SITE     3 BC3 26 LEU K 335  SER K 379  GLY K 380  GLY K 381
SITE     4 BC3 26 GLY K 403  GLY K 404   CA K 476  HOH K2112
SITE     5 BC3 26 HOH K2170  HOH K2220  HOH K2221  HOH K2276
SITE     6 BC3 26 HOH K2277  HOH K2278  GLU O  60  THR O  65
SITE     7 BC3 26 TRP O  66  ASN O 123
SITE     1 BC4 26 GLU B  60  THR B  65  TRP B  66  ASN B 123
SITE     2 BC4 26 THR L 173  LYS L 175  LYS L 177  KCX L 201
SITE     3 BC4 26 HIS L 294  ARG L 295  HIS L 327  LYS L 334
SITE     4 BC4 26 LEU L 335  SER L 379  GLY L 380  GLY L 381
SITE     5 BC4 26 GLY L 403  GLY L 404   CA L 476  HOH L2123
SITE     6 BC4 26 HOH L2185  HOH L2188  HOH L2305  HOH L2306
SITE     7 BC4 26 HOH L2307  HOH L2308
SITE     1 BC5 27 GLU K  60  THR K  65  TRP K  66  ASN K 123
SITE     2 BC5 27 THR O 173  LYS O 175  LYS O 177  KCX O 201
SITE     3 BC5 27 GLU O 204  HIS O 294  ARG O 295  HIS O 327
SITE     4 BC5 27 LYS O 334  LEU O 335  SER O 379  GLY O 380
SITE     5 BC5 27 GLY O 381  GLY O 403  GLY O 404   CA O 476
SITE     6 BC5 27 HOH O2117  HOH O2220  HOH O2229  HOH O2258
SITE     7 BC5 27 HOH O2259  HOH O2260  HOH O2261
SITE     1 BC6 26 THR R 173  LYS R 175  LYS R 177  KCX R 201
SITE     2 BC6 26 HIS R 294  ARG R 295  HIS R 327  LYS R 334
SITE     3 BC6 26 LEU R 335  SER R 379  GLY R 380  GLY R 381
SITE     4 BC6 26 GLY R 403  GLY R 404   CA R 476  HOH R2115
SITE     5 BC6 26 HOH R2177  HOH R2179  HOH R2227  HOH R2289
SITE     6 BC6 26 HOH R2290  GLU V  60  THR V  65  TRP V  66
SITE     7 BC6 26 ASN V 123  HOH V2093
SITE     1 BC7 27 GLU R  60  THR R  65  TRP R  66  ASN R 123
SITE     2 BC7 27 HOH R2044  THR V 173  LYS V 175  LYS V 177
SITE     3 BC7 27 KCX V 201  HIS V 294  ARG V 295  HIS V 327
SITE     4 BC7 27 LYS V 334  LEU V 335  SER V 379  GLY V 380
SITE     5 BC7 27 GLY V 381  GLY V 403  GLY V 404   CA V 476
SITE     6 BC7 27 HOH V2121  HOH V2182  HOH V2235  HOH V2271
SITE     7 BC7 27 HOH V2272  HOH V2273  HOH V2274
CRYST1  219.600  220.942  116.984  90.00  90.00  90.00 P 21 21 2    32
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      0.004554  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004526  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008548        0.00000
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1
MTRIX1   2  0.975400  0.163100  0.148500      -13.16000    1
MTRIX2   2  0.163100 -0.986500  0.011940      102.70000    1
MTRIX3   2  0.148400  0.012580 -0.988800       62.17000    1
MTRIX1   3  0.004226  0.999900 -0.015700      -97.89000    1
MTRIX2   3 -0.992400  0.002264 -0.122900        0.58250    1
MTRIX3   3 -0.122900  0.016100  0.992300       -6.76200    1
MTRIX1   4 -0.175700  0.978100  0.111800     -109.50000    1
MTRIX2   4  0.978300  0.160900  0.130400       86.07000    1
MTRIX3   4  0.109500  0.132200 -0.985100       54.33000    1
MTRIX1   5 -0.991000  0.006136 -0.134000      -97.71000    1
MTRIX2   5  0.008826 -0.993800 -0.110800       98.66000    1
MTRIX3   5 -0.133800 -0.111000  0.984800       -1.16100    1
MTRIX1   6 -0.985200 -0.171600 -0.003444      -92.57000    1
MTRIX2   6 -0.171100  0.980300  0.098620      -10.56000    1
MTRIX3   6 -0.013550  0.097740 -0.995100       50.11000    1
MTRIX1   7  0.006028 -0.991600 -0.129000        0.42450    1
MTRIX2   7  0.999900  0.004664  0.010880       97.93000    1
MTRIX3   7 -0.010180 -0.129100  0.991600        5.86700    1
MTRIX1   8  0.167600 -0.985600  0.023930        4.10300    1
MTRIX2   8 -0.985600 -0.168100 -0.020770        6.25200    1
MTRIX3   8  0.024490 -0.020100 -0.999500       57.76000    1
MTRIX1   9  1.000000  0.000000  0.000000        0.00000    1
MTRIX2   9  0.000000  1.000000  0.000000        0.00000    1
MTRIX3   9  0.000000  0.000000  1.000000        0.00000    1
MTRIX1  10  0.974100  0.173200  0.145300      -13.53000    1
MTRIX2  10  0.172200 -0.984900  0.019820      103.00000    1
MTRIX3  10  0.146600  0.005719 -0.989200       62.35000    1
MTRIX1  11  0.011180  0.999800 -0.013370      -97.55000    1
MTRIX2  11 -0.991700  0.009374 -0.128300        0.46830    1
MTRIX3  11 -0.128200  0.014690  0.991600       -6.96400    1
MTRIX1  12 -0.181000  0.977400  0.109500     -109.70000    1
MTRIX2  12  0.976800  0.165700  0.135800       85.63000    1
MTRIX3  12  0.114600  0.131500 -0.984700       54.59000    1
MTRIX1  13 -0.991200  0.007847 -0.132200      -97.83000    1
MTRIX2  13  0.007278 -0.993500 -0.113500       98.65000    1
MTRIX3  13 -0.132200 -0.113500  0.984700       -0.92360    1
MTRIX1  14 -0.983200 -0.182300 -0.008580      -91.68000    1
MTRIX2  14 -0.182200  0.977500  0.106300      -11.13000    1
MTRIX3  14 -0.010990  0.106100 -0.994300       49.72000    1
MTRIX1  15 -0.002603 -0.992000 -0.126000        0.00952    1
MTRIX2  15  1.000000 -0.003150  0.004136       98.62000    1
MTRIX3  15 -0.004500 -0.126000  0.992000        5.93800    1
MTRIX1  16  0.169700 -0.985200  0.023030        4.25300    1
MTRIX2  16 -0.985200 -0.170100 -0.019800        6.39600    1
MTRIX3  16  0.023430 -0.019330 -0.999500       57.64000    1
      
PROCHECK
Go to PROCHECK summary
 References