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PDBsum entry 1rcx

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Top Page protein ligands Protein-protein interface(s) links
Lyase (carbon-carbon) PDB id
1rcx
Jmol
Contents
Protein chains
(+ 2 more) 467 a.a. *
(+ 2 more) 123 a.a. *
Ligands
RUB ×8
Waters ×1768
* Residue conservation analysis
HEADER    LYASE (CARBON-CARBON)                   06-DEC-96   1RCX
TITLE     NON-ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE
TITLE    2 RIBULOSE-1,5-BISPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE;
COMPND   3 CHAIN: L, B, E, H, K, O, R, V;
COMPND   4 SYNONYM: RUBISCO;
COMPND   5 EC: 4.1.1.39;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE;
COMPND   8 CHAIN: S, C, F, I, M, P, T, W;
COMPND   9 SYNONYM: RUBISCO;
COMPND  10 EC: 4.1.1.39
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE   3 ORGANISM_COMMON: SPINACH;
SOURCE   4 ORGANISM_TAXID: 3562;
SOURCE   5 ORGAN: 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)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.C.TAYLOR,I.ANDERSSON
REVDAT   2   24-FEB-09 1RCX    1       VERSN
REVDAT   1   16-JUN-97 1RCX    0
JRNL        AUTH   T.C.TAYLOR,I.ANDERSSON
JRNL        TITL   THE STRUCTURE OF THE COMPLEX BETWEEN RUBISCO AND
JRNL        TITL 2 ITS NATURAL SUBSTRATE RIBULOSE 1,5-BISPHOSPHATE.
JRNL        REF    J.MOL.BIOL.                   V. 265   432 1997
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9034362
JRNL        DOI    10.1006/JMBI.1996.0738
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   I.ANDERSSON
REMARK   1  TITL   LARGE STRUCTURES AT HIGH RESOLUTION: THE 1.6 A
REMARK   1  TITL 2 CRYSTAL STRUCTURE OF SPINACH
REMARK   1  TITL 3 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE
REMARK   1  TITL 4 COMPLEXED WITH 2-CARBOXYARABINITOL BISPHOSPHATE
REMARK   1  REF    J.MOL.BIOL.                   V. 259   160 1996
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 63.0
REMARK   3   NUMBER OF REFLECTIONS             : 143806
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 SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6443
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 16384
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890
REMARK   3   BIN FREE R VALUE                    : 0.3160
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 536
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4682
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 18
REMARK   3   SOLVENT ATOMS            : 221
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.011
REMARK   3   BOND ANGLES            (DEGREES) : 1.94
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.53
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : INDIVIDUAL
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  NCS MODEL : CONSTRAINTS
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : WAT.PARA
REMARK   3  PARAMETER FILE  3  : RUBP.PARA
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : WAT.TOP
REMARK   3  TOPOLOGY FILE  3   : RUBP.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1RCX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : JUL-95
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX9.5
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 149428
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 70.5
REMARK 200  DATA REDUNDANCY                : 6.400
REMARK 200  R MERGE                    (I) : 0.10000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.32800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS WITH PDB
REMARK 200  ENTRY 1RCO
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 25 MM HEPES PH 7.8,
REMARK 280  0.2 M NACL, 20 MM RUBP
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      109.15000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      109.50000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      109.15000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      109.50000
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 300 REMARK:
REMARK 300 THE DEPOSITORS PROVIDED CHAINS L AND S.  THE OTHER CHAINS
REMARK 300 TO MAKE THE COMPLETE ASYMMETRIC UNIT WERE GENERATED BY
REMARK 300 THE PROTEIN DATA BANK USING THE MTRIX TRANSFORMATIONS
REMARK 300 BELOW.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 110020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 116240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -475.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, S, B, C, E, F, H, I, K,
REMARK 350                    AND CHAINS: M, O, P, R, T, V, W
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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 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 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 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 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   CD   GLU H   464     OE1  GLU V   468     3446     1.11
REMARK 500   OE1  GLU H   464     OE1  GLU V   468     3446     1.37
REMARK 500   CA   PHE V   469     O    HOH H   634     3456     1.39
REMARK 500   N    PHE V   469     O    HOH H   634     3456     1.62
REMARK 500   CG   GLU H   464     OE1  GLU V   468     3446     1.85
REMARK 500   C    GLU V   468     O    HOH H   634     3456     1.86
REMARK 500   O    GLU V   468     O    HOH H   634     3456     1.92
REMARK 500   OE2  GLU H   464     OE1  GLU V   468     3446     2.00
REMARK 500   OE2  GLU H   464     CB   GLU V   468     3446     2.01
REMARK 500   OE2  GLU L   338     O    HOH K   619     4455     2.15
REMARK 500   C    PHE V   469     O    HOH H   634     3456     2.18
REMARK 500   NH1  ARG E   439     O    PHE R   469     3445     2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: ACB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: ACE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: ACH
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: ACK
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: ACO
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: ACR
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: ACV
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB L 476
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB B 476
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB E 476
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB H 476
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB K 476
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB O 476
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB R 476
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB V 476
DBREF  1RCX L    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX S    1   123  UNP    P00870   RBS1_SPIOL      58    180
DBREF  1RCX B    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX C    1   123  UNP    P00870   RBS1_SPIOL      58    180
DBREF  1RCX E    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX F    1   123  UNP    P00870   RBS1_SPIOL      58    180
DBREF  1RCX H    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX I    1   123  UNP    P00870   RBS1_SPIOL      58    180
DBREF  1RCX K    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX M    1   123  UNP    P00870   RBS1_SPIOL      58    180
DBREF  1RCX O    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX P    1   123  UNP    P00870   RBS1_SPIOL      58    180
DBREF  1RCX R    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX T    1   123  UNP    P00870   RBS1_SPIOL      58    180
DBREF  1RCX V    1   475  UNP    P00875   RBL_SPIOL        1    475
DBREF  1RCX W    1   123  UNP    P00870   RBS1_SPIOL      58    180
SEQADV 1RCX GLN S    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE S    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU S    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU S    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS S   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU S  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE S  113  UNP  P00870    VAL   170 CONFLICT
SEQADV 1RCX GLN C    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE C    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU C    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU C    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS C   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU C  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE C  113  UNP  P00870    VAL   170 CONFLICT
SEQADV 1RCX GLN F    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE F    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU F    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU F    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS F   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU F  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE F  113  UNP  P00870    VAL   170 CONFLICT
SEQADV 1RCX GLN I    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE I    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU I    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU I    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS I   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU I  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE I  113  UNP  P00870    VAL   170 CONFLICT
SEQADV 1RCX GLN M    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE M    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU M    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU M    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS M   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU M  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE M  113  UNP  P00870    VAL   170 CONFLICT
SEQADV 1RCX GLN P    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE P    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU P    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU P    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS P   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU P  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE P  113  UNP  P00870    VAL   170 CONFLICT
SEQADV 1RCX GLN T    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE T    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU T    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU T    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS T   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU T  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE T  113  UNP  P00870    VAL   170 CONFLICT
SEQADV 1RCX GLN W    2  UNP  P00870    LYS    59 CONFLICT
SEQADV 1RCX ILE W    6  UNP  P00870    THR    63 CONFLICT
SEQADV 1RCX LEU W    7  UNP  P00870    GLN    64 CONFLICT
SEQADV 1RCX LEU W    9  UNP  P00870    MET    66 CONFLICT
SEQADV 1RCX LYS W   11  UNP  P00870    ARG    68 CONFLICT
SEQADV 1RCX GLU W  109  UNP  P00870    GLN   166 CONFLICT
SEQADV 1RCX ILE W  113  UNP  P00870    VAL   170 CONFLICT
SEQRES   1 L  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY 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 LYS 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 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 B  475  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY 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 LYS 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 GLY 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 LYS 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 GLY 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 LYS 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 GLY 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 LYS 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 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 GLY 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 LYS 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 GLY 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 LYS 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 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 GLY 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 LYS 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
HET    RUB  L 476      18
HET    RUB  B 476      18
HET    RUB  E 476      18
HET    RUB  H 476      18
HET    RUB  K 476      18
HET    RUB  O 476      18
HET    RUB  R 476      18
HET    RUB  V 476      18
HETNAM     RUB RIBULOSE-1,5-DIPHOSPHATE
FORMUL  17  RUB    8(C5 H12 O11 P2)
FORMUL  25  HOH   *1768(H2 O)
HELIX    1   1 TYR L   20  TYR L   24  5                                   5
HELIX    2   2 PRO L   50  GLU L   60  1                                  11
HELIX    3   3 TRP L   70  LEU L   74  5                                   5
HELIX    4   4 LEU L   77  TYR L   80  1                                   4
HELIX    5   5 LEU L  105  LEU L  107  5                                   3
HELIX    6   6 VAL L  113  ILE L  120  1                                   8
HELIX    7   7 VAL L  124  GLY L  126  5                                   3
HELIX    8   8 VAL L  142  THR L  147  1                                   6
HELIX    9   9 ILE L  155  LEU L  162  1                                   8
HELIX   10  10 ALA L  182  GLY L  195  1                                  14
HELIX   11  11 TRP L  214  THR L  232  1                                  19
HELIX   12  12 CYS L  247  LEU L  260  1                                  14
HELIX   13  13 TYR L  269  GLY L  272  1                                   4
HELIX   14  14 PHE L  274  ASN L  287  1                                  14
HELIX   15  15 HIS L  298  ASP L  302  1                                   5
HELIX   16  16 PHE L  311  SER L  321  1                                  11
HELIX   17  17 ARG L  339  ARG L  350  1                                  12
HELIX   18  18 ARG L  358  ARG L  360  5                                   3
HELIX   19  19 VAL L  384  PHE L  394  5                                  11
HELIX   20  20 GLY L  404  LEU L  407  1                                   4
HELIX   21  21 ASN L  413  ASN L  432  1                                  20
HELIX   22  22 LEU L  437  LYS L  450  1                                  14
HELIX   23  23 PRO L  453  TRP L  462  1                                  10
HELIX   24  24 THR S   23  ASN S   35  1                                  13
HELIX   25  25 PRO S   80  GLU S   93  1                                  14
HELIX   26  26 TYR B   20  TYR B   24  5                                   5
HELIX   27  27 PRO B   50  GLU B   60  1                                  11
HELIX   28  28 TRP B   70  LEU B   74  5                                   5
HELIX   29  29 LEU B   77  TYR B   80  1                                   4
HELIX   30  30 LEU B  105  LEU B  107  5                                   3
HELIX   31  31 VAL B  113  ILE B  120  1                                   8
HELIX   32  32 VAL B  124  GLY B  126  5                                   3
HELIX   33  33 VAL B  142  THR B  147  1                                   6
HELIX   34  34 ILE B  155  LEU B  162  1                                   8
HELIX   35  35 ALA B  182  GLY B  195  1                                  14
HELIX   36  36 TRP B  214  THR B  232  1                                  19
HELIX   37  37 CYS B  247  LEU B  260  1                                  14
HELIX   38  38 TYR B  269  GLY B  272  1                                   4
HELIX   39  39 PHE B  274  ASN B  287  1                                  14
HELIX   40  40 HIS B  298  ASP B  302  1                                   5
HELIX   41  41 PHE B  311  SER B  321  1                                  11
HELIX   42  42 ARG B  339  ARG B  350  1                                  12
HELIX   43  43 ARG B  358  ARG B  360  5                                   3
HELIX   44  44 VAL B  384  PHE B  394  5                                  11
HELIX   45  45 GLY B  404  LEU B  407  1                                   4
HELIX   46  46 ASN B  413  ASN B  432  1                                  20
HELIX   47  47 LEU B  437  LYS B  450  1                                  14
HELIX   48  48 PRO B  453  TRP B  462  1                                  10
HELIX   49  49 THR C   23  ASN C   35  1                                  13
HELIX   50  50 PRO C   80  GLU C   93  1                                  14
HELIX   51  51 TYR E   20  TYR E   24  5                                   5
HELIX   52  52 PRO E   50  GLU E   60  1                                  11
HELIX   53  53 TRP E   70  LEU E   74  5                                   5
HELIX   54  54 LEU E   77  TYR E   80  1                                   4
HELIX   55  55 LEU E  105  LEU E  107  5                                   3
HELIX   56  56 VAL E  113  ILE E  120  1                                   8
HELIX   57  57 VAL E  124  GLY E  126  5                                   3
HELIX   58  58 VAL E  142  THR E  147  1                                   6
HELIX   59  59 ILE E  155  LEU E  162  1                                   8
HELIX   60  60 ALA E  182  GLY E  195  1                                  14
HELIX   61  61 TRP E  214  THR E  232  1                                  19
HELIX   62  62 CYS E  247  LEU E  260  1                                  14
HELIX   63  63 TYR E  269  GLY E  272  1                                   4
HELIX   64  64 PHE E  274  ASN E  287  1                                  14
HELIX   65  65 HIS E  298  ASP E  302  1                                   5
HELIX   66  66 PHE E  311  SER E  321  1                                  11
HELIX   67  67 ARG E  339  ARG E  350  1                                  12
HELIX   68  68 ARG E  358  ARG E  360  5                                   3
HELIX   69  69 VAL E  384  PHE E  394  5                                  11
HELIX   70  70 GLY E  404  LEU E  407  1                                   4
HELIX   71  71 ASN E  413  ASN E  432  1                                  20
HELIX   72  72 LEU E  437  LYS E  450  1                                  14
HELIX   73  73 PRO E  453  TRP E  462  1                                  10
HELIX   74  74 THR F   23  ASN F   35  1                                  13
HELIX   75  75 PRO F   80  GLU F   93  1                                  14
HELIX   76  76 TYR H   20  TYR H   24  5                                   5
HELIX   77  77 PRO H   50  GLU H   60  1                                  11
HELIX   78  78 TRP H   70  LEU H   74  5                                   5
HELIX   79  79 LEU H   77  TYR H   80  1                                   4
HELIX   80  80 LEU H  105  LEU H  107  5                                   3
HELIX   81  81 VAL H  113  ILE H  120  1                                   8
HELIX   82  82 VAL H  124  GLY H  126  5                                   3
HELIX   83  83 VAL H  142  THR H  147  1                                   6
HELIX   84  84 ILE H  155  LEU H  162  1                                   8
HELIX   85  85 ALA H  182  GLY H  195  1                                  14
HELIX   86  86 TRP H  214  THR H  232  1                                  19
HELIX   87  87 CYS H  247  LEU H  260  1                                  14
HELIX   88  88 TYR H  269  GLY H  272  1                                   4
HELIX   89  89 PHE H  274  ASN H  287  1                                  14
HELIX   90  90 HIS H  298  ASP H  302  1                                   5
HELIX   91  91 PHE H  311  SER H  321  1                                  11
HELIX   92  92 ARG H  339  ARG H  350  1                                  12
HELIX   93  93 ARG H  358  ARG H  360  5                                   3
HELIX   94  94 VAL H  384  PHE H  394  5                                  11
HELIX   95  95 GLY H  404  LEU H  407  1                                   4
HELIX   96  96 ASN H  413  ASN H  432  1                                  20
HELIX   97  97 LEU H  437  LYS H  450  1                                  14
HELIX   98  98 PRO H  453  TRP H  462  1                                  10
HELIX   99  99 THR I   23  ASN I   35  1                                  13
HELIX  100 100 PRO I   80  GLU I   93  1                                  14
HELIX  101 101 TYR K   20  TYR K   24  5                                   5
HELIX  102 102 PRO K   50  GLU K   60  1                                  11
HELIX  103 103 TRP K   70  LEU K   74  5                                   5
HELIX  104 104 LEU K   77  TYR K   80  1                                   4
HELIX  105 105 LEU K  105  LEU K  107  5                                   3
HELIX  106 106 VAL K  113  ILE K  120  1                                   8
HELIX  107 107 VAL K  124  GLY K  126  5                                   3
HELIX  108 108 VAL K  142  THR K  147  1                                   6
HELIX  109 109 ILE K  155  LEU K  162  1                                   8
HELIX  110 110 ALA K  182  GLY K  195  1                                  14
HELIX  111 111 TRP K  214  THR K  232  1                                  19
HELIX  112 112 CYS K  247  LEU K  260  1                                  14
HELIX  113 113 TYR K  269  GLY K  272  1                                   4
HELIX  114 114 PHE K  274  ASN K  287  1                                  14
HELIX  115 115 HIS K  298  ASP K  302  1                                   5
HELIX  116 116 PHE K  311  SER K  321  1                                  11
HELIX  117 117 ARG K  339  ARG K  350  1                                  12
HELIX  118 118 ARG K  358  ARG K  360  5                                   3
HELIX  119 119 VAL K  384  PHE K  394  5                                  11
HELIX  120 120 GLY K  404  LEU K  407  1                                   4
HELIX  121 121 ASN K  413  ASN K  432  1                                  20
HELIX  122 122 LEU K  437  LYS K  450  1                                  14
HELIX  123 123 PRO K  453  TRP K  462  1                                  10
HELIX  124 124 THR M   23  ASN M   35  1                                  13
HELIX  125 125 PRO M   80  GLU M   93  1                                  14
HELIX  126 126 TYR O   20  TYR O   24  5                                   5
HELIX  127 127 PRO O   50  GLU O   60  1                                  11
HELIX  128 128 TRP O   70  LEU O   74  5                                   5
HELIX  129 129 LEU O   77  TYR O   80  1                                   4
HELIX  130 130 LEU O  105  LEU O  107  5                                   3
HELIX  131 131 VAL O  113  ILE O  120  1                                   8
HELIX  132 132 VAL O  124  GLY O  126  5                                   3
HELIX  133 133 VAL O  142  THR O  147  1                                   6
HELIX  134 134 ILE O  155  LEU O  162  1                                   8
HELIX  135 135 ALA O  182  GLY O  195  1                                  14
HELIX  136 136 TRP O  214  THR O  232  1                                  19
HELIX  137 137 CYS O  247  LEU O  260  1                                  14
HELIX  138 138 TYR O  269  GLY O  272  1                                   4
HELIX  139 139 PHE O  274  ASN O  287  1                                  14
HELIX  140 140 HIS O  298  ASP O  302  1                                   5
HELIX  141 141 PHE O  311  SER O  321  1                                  11
HELIX  142 142 ARG O  339  ARG O  350  1                                  12
HELIX  143 143 ARG O  358  ARG O  360  5                                   3
HELIX  144 144 VAL O  384  PHE O  394  5                                  11
HELIX  145 145 GLY O  404  LEU O  407  1                                   4
HELIX  146 146 ASN O  413  ASN O  432  1                                  20
HELIX  147 147 LEU O  437  LYS O  450  1                                  14
HELIX  148 148 PRO O  453  TRP O  462  1                                  10
HELIX  149 149 THR P   23  ASN P   35  1                                  13
HELIX  150 150 PRO P   80  GLU P   93  1                                  14
HELIX  151 151 TYR R   20  TYR R   24  5                                   5
HELIX  152 152 PRO R   50  GLU R   60  1                                  11
HELIX  153 153 TRP R   70  LEU R   74  5                                   5
HELIX  154 154 LEU R   77  TYR R   80  1                                   4
HELIX  155 155 LEU R  105  LEU R  107  5                                   3
HELIX  156 156 VAL R  113  ILE R  120  1                                   8
HELIX  157 157 VAL R  124  GLY R  126  5                                   3
HELIX  158 158 VAL R  142  THR R  147  1                                   6
HELIX  159 159 ILE R  155  LEU R  162  1                                   8
HELIX  160 160 ALA R  182  GLY R  195  1                                  14
HELIX  161 161 TRP R  214  THR R  232  1                                  19
HELIX  162 162 CYS R  247  LEU R  260  1                                  14
HELIX  163 163 TYR R  269  GLY R  272  1                                   4
HELIX  164 164 PHE R  274  ASN R  287  1                                  14
HELIX  165 165 HIS R  298  ASP R  302  1                                   5
HELIX  166 166 PHE R  311  SER R  321  1                                  11
HELIX  167 167 ARG R  339  ARG R  350  1                                  12
HELIX  168 168 ARG R  358  ARG R  360  5                                   3
HELIX  169 169 VAL R  384  PHE R  394  5                                  11
HELIX  170 170 GLY R  404  LEU R  407  1                                   4
HELIX  171 171 ASN R  413  ASN R  432  1                                  20
HELIX  172 172 LEU R  437  LYS R  450  1                                  14
HELIX  173 173 PRO R  453  TRP R  462  1                                  10
HELIX  174 174 THR T   23  ASN T   35  1                                  13
HELIX  175 175 PRO T   80  GLU T   93  1                                  14
HELIX  176 176 TYR V   20  TYR V   24  5                                   5
HELIX  177 177 PRO V   50  GLU V   60  1                                  11
HELIX  178 178 TRP V   70  LEU V   74  5                                   5
HELIX  179 179 LEU V   77  TYR V   80  1                                   4
HELIX  180 180 LEU V  105  LEU V  107  5                                   3
HELIX  181 181 VAL V  113  ILE V  120  1                                   8
HELIX  182 182 VAL V  124  GLY V  126  5                                   3
HELIX  183 183 VAL V  142  THR V  147  1                                   6
HELIX  184 184 ILE V  155  LEU V  162  1                                   8
HELIX  185 185 ALA V  182  GLY V  195  1                                  14
HELIX  186 186 TRP V  214  THR V  232  1                                  19
HELIX  187 187 CYS V  247  LEU V  260  1                                  14
HELIX  188 188 TYR V  269  GLY V  272  1                                   4
HELIX  189 189 PHE V  274  ASN V  287  1                                  14
HELIX  190 190 HIS V  298  ASP V  302  1                                   5
HELIX  191 191 PHE V  311  SER V  321  1                                  11
HELIX  192 192 ARG V  339  ARG V  350  1                                  12
HELIX  193 193 ARG V  358  ARG V  360  5                                   3
HELIX  194 194 VAL V  384  PHE V  394  5                                  11
HELIX  195 195 GLY V  404  LEU V  407  1                                   4
HELIX  196 196 ASN V  413  ASN V  432  1                                  20
HELIX  197 197 LEU V  437  LYS V  450  1                                  14
HELIX  198 198 PRO V  453  TRP V  462  1                                  10
HELIX  199 199 THR W   23  ASN W   35  1                                  13
HELIX  200 200 PRO W   80  GLU W   93  1                                  14
SHEET    1   A 4 ALA L 132  ARG L 139  0
SHEET    2   A 4 ILE L  36  SER L  43 -1  N  SER L  43   O  ALA L 132
SHEET    3   A 4 TYR L  97  TYR L 103 -1  N  TYR L 103   O  ILE L  36
SHEET    4   A 4 ARG L  83  PRO L  89 -1  N  GLU L  88   O  ILE L  98
SHEET    1   B 4 LEU L 169  GLY L 171  0
SHEET    2   B 4 SER L 398  GLN L 401  1  N  LEU L 400   O  LEU L 169
SHEET    3   B 4 LEU L 375  SER L 379  1  N  PRO L 376   O  VAL L 399
SHEET    4   B 4 HIS L 325  HIS L 327  1  N  ILE L 326   O  LEU L 375
SHEET    1   C 2 PHE L 199  LYS L 201  0
SHEET    2   C 2 GLY L 237  TYR L 239  1  N  GLY L 237   O  THR L 200
SHEET    1   D 2 ILE L 264  ASP L 268  0
SHEET    2   D 2 LEU L 290  HIS L 294  1  N  LEU L 290   O  VAL L 265
SHEET    1   E 4 THR S  68  TRP S  70  0
SHEET    2   E 4 VAL S  39  GLU S  45 -1  N  PHE S  44   O  THR S  68
SHEET    3   E 4 PHE S  98  PHE S 104 -1  N  PHE S 104   O  VAL S  39
SHEET    4   E 4 ILE S 113  TYR S 118 -1  N  TYR S 118   O  ILE S  99
SHEET    1   F 4 ALA B 132  ARG B 139  0
SHEET    2   F 4 ILE B  36  SER B  43 -1  N  SER B  43   O  ALA B 132
SHEET    3   F 4 TYR B  97  TYR B 103 -1  N  TYR B 103   O  ILE B  36
SHEET    4   F 4 ARG B  83  PRO B  89 -1  N  GLU B  88   O  ILE B  98
SHEET    1   G 4 LEU B 169  GLY B 171  0
SHEET    2   G 4 SER B 398  GLN B 401  1  N  LEU B 400   O  LEU B 169
SHEET    3   G 4 LEU B 375  SER B 379  1  N  PRO B 376   O  VAL B 399
SHEET    4   G 4 HIS B 325  HIS B 327  1  N  ILE B 326   O  LEU B 375
SHEET    1   H 2 PHE B 199  LYS B 201  0
SHEET    2   H 2 GLY B 237  TYR B 239  1  N  GLY B 237   O  THR B 200
SHEET    1   I 2 ILE B 264  ASP B 268  0
SHEET    2   I 2 LEU B 290  HIS B 294  1  N  LEU B 290   O  VAL B 265
SHEET    1   J 4 THR C  68  TRP C  70  0
SHEET    2   J 4 VAL C  39  GLU C  45 -1  N  PHE C  44   O  THR C  68
SHEET    3   J 4 PHE C  98  PHE C 104 -1  N  PHE C 104   O  VAL C  39
SHEET    4   J 4 ILE C 113  TYR C 118 -1  N  TYR C 118   O  ILE C  99
SHEET    1   K 4 ALA E 132  ARG E 139  0
SHEET    2   K 4 ILE E  36  SER E  43 -1  N  SER E  43   O  ALA E 132
SHEET    3   K 4 TYR E  97  TYR E 103 -1  N  TYR E 103   O  ILE E  36
SHEET    4   K 4 ARG E  83  PRO E  89 -1  N  GLU E  88   O  ILE E  98
SHEET    1   L 4 LEU E 169  GLY E 171  0
SHEET    2   L 4 SER E 398  GLN E 401  1  N  LEU E 400   O  LEU E 169
SHEET    3   L 4 LEU E 375  SER E 379  1  N  PRO E 376   O  VAL E 399
SHEET    4   L 4 HIS E 325  HIS E 327  1  N  ILE E 326   O  LEU E 375
SHEET    1   M 2 PHE E 199  LYS E 201  0
SHEET    2   M 2 GLY E 237  TYR E 239  1  N  GLY E 237   O  THR E 200
SHEET    1   N 2 ILE E 264  ASP E 268  0
SHEET    2   N 2 LEU E 290  HIS E 294  1  N  LEU E 290   O  VAL E 265
SHEET    1   O 4 THR F  68  TRP F  70  0
SHEET    2   O 4 VAL F  39  GLU F  45 -1  N  PHE F  44   O  THR F  68
SHEET    3   O 4 PHE F  98  PHE F 104 -1  N  PHE F 104   O  VAL F  39
SHEET    4   O 4 ILE F 113  TYR F 118 -1  N  TYR F 118   O  ILE F  99
SHEET    1   P 4 ALA H 132  ARG H 139  0
SHEET    2   P 4 ILE H  36  SER H  43 -1  N  SER H  43   O  ALA H 132
SHEET    3   P 4 TYR H  97  TYR H 103 -1  N  TYR H 103   O  ILE H  36
SHEET    4   P 4 ARG H  83  PRO H  89 -1  N  GLU H  88   O  ILE H  98
SHEET    1   Q 4 LEU H 169  GLY H 171  0
SHEET    2   Q 4 SER H 398  GLN H 401  1  N  LEU H 400   O  LEU H 169
SHEET    3   Q 4 LEU H 375  SER H 379  1  N  PRO H 376   O  VAL H 399
SHEET    4   Q 4 HIS H 325  HIS H 327  1  N  ILE H 326   O  LEU H 375
SHEET    1   R 2 PHE H 199  LYS H 201  0
SHEET    2   R 2 GLY H 237  TYR H 239  1  N  GLY H 237   O  THR H 200
SHEET    1   S 2 ILE H 264  ASP H 268  0
SHEET    2   S 2 LEU H 290  HIS H 294  1  N  LEU H 290   O  VAL H 265
SHEET    1   T 4 THR I  68  TRP I  70  0
SHEET    2   T 4 VAL I  39  GLU I  45 -1  N  PHE I  44   O  THR I  68
SHEET    3   T 4 PHE I  98  PHE I 104 -1  N  PHE I 104   O  VAL I  39
SHEET    4   T 4 ILE I 113  TYR I 118 -1  N  TYR I 118   O  ILE I  99
SHEET    1   U 4 ALA K 132  ARG K 139  0
SHEET    2   U 4 ILE K  36  SER K  43 -1  N  SER K  43   O  ALA K 132
SHEET    3   U 4 TYR K  97  TYR K 103 -1  N  TYR K 103   O  ILE K  36
SHEET    4   U 4 ARG K  83  PRO K  89 -1  N  GLU K  88   O  ILE K  98
SHEET    1   V 4 LEU K 169  GLY K 171  0
SHEET    2   V 4 SER K 398  GLN K 401  1  N  LEU K 400   O  LEU K 169
SHEET    3   V 4 LEU K 375  SER K 379  1  N  PRO K 376   O  VAL K 399
SHEET    4   V 4 HIS K 325  HIS K 327  1  N  ILE K 326   O  LEU K 375
SHEET    1   W 2 PHE K 199  LYS K 201  0
SHEET    2   W 2 GLY K 237  TYR K 239  1  N  GLY K 237   O  THR K 200
SHEET    1   X 2 ILE K 264  ASP K 268  0
SHEET    2   X 2 LEU K 290  HIS K 294  1  N  LEU K 290   O  VAL K 265
SHEET    1   Y 4 THR M  68  TRP M  70  0
SHEET    2   Y 4 VAL M  39  GLU M  45 -1  N  PHE M  44   O  THR M  68
SHEET    3   Y 4 PHE M  98  PHE M 104 -1  N  PHE M 104   O  VAL M  39
SHEET    4   Y 4 ILE M 113  TYR M 118 -1  N  TYR M 118   O  ILE M  99
SHEET    1   Z 4 ALA O 132  ARG O 139  0
SHEET    2   Z 4 ILE O  36  SER O  43 -1  N  SER O  43   O  ALA O 132
SHEET    3   Z 4 TYR O  97  TYR O 103 -1  N  TYR O 103   O  ILE O  36
SHEET    4   Z 4 ARG O  83  PRO O  89 -1  N  GLU O  88   O  ILE O  98
SHEET    1  AA 4 LEU O 169  GLY O 171  0
SHEET    2  AA 4 SER O 398  GLN O 401  1  N  LEU O 400   O  LEU O 169
SHEET    3  AA 4 LEU O 375  SER O 379  1  N  PRO O 376   O  VAL O 399
SHEET    4  AA 4 HIS O 325  HIS O 327  1  N  ILE O 326   O  LEU O 375
SHEET    1  BB 2 PHE O 199  LYS O 201  0
SHEET    2  BB 2 GLY O 237  TYR O 239  1  N  GLY O 237   O  THR O 200
SHEET    1  CC 2 ILE O 264  ASP O 268  0
SHEET    2  CC 2 LEU O 290  HIS O 294  1  N  LEU O 290   O  VAL O 265
SHEET    1  DD 4 THR P  68  TRP P  70  0
SHEET    2  DD 4 VAL P  39  GLU P  45 -1  N  PHE P  44   O  THR P  68
SHEET    3  DD 4 PHE P  98  PHE P 104 -1  N  PHE P 104   O  VAL P  39
SHEET    4  DD 4 ILE P 113  TYR P 118 -1  N  TYR P 118   O  ILE P  99
SHEET    1  EE 4 ALA R 132  ARG R 139  0
SHEET    2  EE 4 ILE R  36  SER R  43 -1  N  SER R  43   O  ALA R 132
SHEET    3  EE 4 TYR R  97  TYR R 103 -1  N  TYR R 103   O  ILE R  36
SHEET    4  EE 4 ARG R  83  PRO R  89 -1  N  GLU R  88   O  ILE R  98
SHEET    1  FF 4 LEU R 169  GLY R 171  0
SHEET    2  FF 4 SER R 398  GLN R 401  1  N  LEU R 400   O  LEU R 169
SHEET    3  FF 4 LEU R 375  SER R 379  1  N  PRO R 376   O  VAL R 399
SHEET    4  FF 4 HIS R 325  HIS R 327  1  N  ILE R 326   O  LEU R 375
SHEET    1  GG 2 PHE R 199  LYS R 201  0
SHEET    2  GG 2 GLY R 237  TYR R 239  1  N  GLY R 237   O  THR R 200
SHEET    1  HH 2 ILE R 264  ASP R 268  0
SHEET    2  HH 2 LEU R 290  HIS R 294  1  N  LEU R 290   O  VAL R 265
SHEET    1  II 4 THR T  68  TRP T  70  0
SHEET    2  II 4 VAL T  39  GLU T  45 -1  N  PHE T  44   O  THR T  68
SHEET    3  II 4 PHE T  98  PHE T 104 -1  N  PHE T 104   O  VAL T  39
SHEET    4  II 4 ILE T 113  TYR T 118 -1  N  TYR T 118   O  ILE T  99
SHEET    1  JJ 4 ALA V 132  ARG V 139  0
SHEET    2  JJ 4 ILE V  36  SER V  43 -1  N  SER V  43   O  ALA V 132
SHEET    3  JJ 4 TYR V  97  TYR V 103 -1  N  TYR V 103   O  ILE V  36
SHEET    4  JJ 4 ARG V  83  PRO V  89 -1  N  GLU V  88   O  ILE V  98
SHEET    1  KK 4 LEU V 169  GLY V 171  0
SHEET    2  KK 4 SER V 398  GLN V 401  1  N  LEU V 400   O  LEU V 169
SHEET    3  KK 4 LEU V 375  SER V 379  1  N  PRO V 376   O  VAL V 399
SHEET    4  KK 4 HIS V 325  HIS V 327  1  N  ILE V 326   O  LEU V 375
SHEET    1  LL 2 PHE V 199  LYS V 201  0
SHEET    2  LL 2 GLY V 237  TYR V 239  1  N  GLY V 237   O  THR V 200
SHEET    1  MM 2 ILE V 264  ASP V 268  0
SHEET    2  MM 2 LEU V 290  HIS V 294  1  N  LEU V 290   O  VAL V 265
SHEET    1  NN 4 THR W  68  TRP W  70  0
SHEET    2  NN 4 VAL W  39  GLU W  45 -1  N  PHE W  44   O  THR W  68
SHEET    3  NN 4 PHE W  98  PHE W 104 -1  N  PHE W 104   O  VAL W  39
SHEET    4  NN 4 ILE W 113  TYR W 118 -1  N  TYR W 118   O  ILE W  99
SSBOND   1 CYS L  247    CYS B  247                          1555   1555  2.27
SSBOND   2 CYS E  247    CYS H  247                          1555   1555  2.26
SSBOND   3 CYS K  247    CYS O  247                          1555   1555  2.26
SSBOND   4 CYS R  247    CYS V  247                          1555   1555  2.23
CISPEP   1 LYS L  175    PRO L  176          0        -0.67
CISPEP   2 LYS B  175    PRO B  176          0        -0.71
CISPEP   3 LYS E  175    PRO E  176          0        -0.61
CISPEP   4 LYS H  175    PRO H  176          0        -0.68
CISPEP   5 LYS K  175    PRO K  176          0        -0.67
CISPEP   6 LYS O  175    PRO O  176          0        -0.56
CISPEP   7 LYS R  175    PRO R  176          0        -0.68
CISPEP   8 LYS V  175    PRO V  176          0        -0.76
SITE     1 ACL  3 LYS L 201  ASP L 203  GLU L 204
SITE     1 ACB  3 LYS B 201  ASP B 203  GLU B 204
SITE     1 ACE  3 LYS E 201  ASP E 203  GLU E 204
SITE     1 ACH  3 LYS H 201  ASP H 203  GLU H 204
SITE     1 ACK  3 LYS K 201  ASP K 203  GLU K 204
SITE     1 ACO  3 LYS O 201  ASP O 203  GLU O 204
SITE     1 ACR  3 LYS R 201  ASP R 203  GLU R 204
SITE     1 ACV  3 LYS V 201  ASP V 203  GLU V 204
SITE     1 AC1 20 THR B  65  TRP B  66  ASN B 123  HOH B 484
SITE     2 AC1 20 THR L 173  LYS L 175  LYS L 201  GLU L 204
SITE     3 AC1 20 HIS L 294  ARG L 295  HIS L 327  LYS L 334
SITE     4 AC1 20 LEU L 335  SER L 379  GLY L 380  GLY L 381
SITE     5 AC1 20 GLY L 403  GLY L 404  HOH L 505  HOH L 583
SITE     1 AC2 20 THR B 173  LYS B 175  LYS B 201  GLU B 204
SITE     2 AC2 20 HIS B 294  ARG B 295  HIS B 327  LYS B 334
SITE     3 AC2 20 LEU B 335  SER B 379  GLY B 380  GLY B 381
SITE     4 AC2 20 GLY B 403  GLY B 404  HOH B 514  HOH B 593
SITE     5 AC2 20 THR L  65  TRP L  66  ASN L 123  HOH L 633
SITE     1 AC3 20 THR E 173  LYS E 175  LYS E 201  GLU E 204
SITE     2 AC3 20 HIS E 294  ARG E 295  HIS E 327  LYS E 334
SITE     3 AC3 20 LEU E 335  SER E 379  GLY E 380  GLY E 381
SITE     4 AC3 20 GLY E 403  GLY E 404  HOH E 510  HOH E 588
SITE     5 AC3 20 THR H  65  TRP H  66  ASN H 123  HOH H 495
SITE     1 AC4 20 THR E  65  TRP E  66  ASN E 123  HOH E 639
SITE     2 AC4 20 THR H 173  LYS H 175  LYS H 201  GLU H 204
SITE     3 AC4 20 HIS H 294  ARG H 295  HIS H 327  LYS H 334
SITE     4 AC4 20 LEU H 335  SER H 379  GLY H 380  GLY H 381
SITE     5 AC4 20 GLY H 403  GLY H 404  HOH H 525  HOH H 603
SITE     1 AC5 20 THR K 173  LYS K 175  LYS K 201  GLU K 204
SITE     2 AC5 20 HIS K 294  ARG K 295  HIS K 327  LYS K 334
SITE     3 AC5 20 LEU K 335  SER K 379  GLY K 380  GLY K 381
SITE     4 AC5 20 GLY K 403  GLY K 404  HOH K 509  HOH K 588
SITE     5 AC5 20 THR O  65  TRP O  66  ASN O 123  HOH O1104
SITE     1 AC6 20 THR K  65  TRP K  66  ASN K 123  HOH K 639
SITE     2 AC6 20 THR O 173  LYS O 175  LYS O 201  GLU O 204
SITE     3 AC6 20 HIS O 294  ARG O 295  HIS O 327  LYS O 334
SITE     4 AC6 20 LEU O 335  SER O 379  GLY O 380  GLY O 381
SITE     5 AC6 20 GLY O 403  GLY O 404  HOH O1152  HOH O1263
SITE     1 AC7 20 THR R 173  LYS R 175  LYS R 201  GLU R 204
SITE     2 AC7 20 HIS R 294  ARG R 295  HIS R 327  LYS R 334
SITE     3 AC7 20 LEU R 335  SER R 379  GLY R 380  GLY R 381
SITE     4 AC7 20 GLY R 403  GLY R 404  HOH R 518  HOH R 596
SITE     5 AC7 20 THR V  65  TRP V  66  ASN V 123  HOH V 497
SITE     1 AC8 20 THR R  65  TRP R  66  ASN R 123  HOH R 646
SITE     2 AC8 20 THR V 173  LYS V 175  LYS V 201  GLU V 204
SITE     3 AC8 20 HIS V 294  ARG V 295  HIS V 327  LYS V 334
SITE     4 AC8 20 LEU V 335  SER V 379  GLY V 380  GLY V 381
SITE     5 AC8 20 GLY V 403  GLY V 404  HOH V 527  HOH V 605
CRYST1  218.300  219.000  113.500  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      0.004581  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004566  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008811        0.00000
MTRIX1   1  0.965620  0.218860  0.140279      -15.94210    1
MTRIX2   1  0.218875 -0.975630  0.015511      104.27010    1
MTRIX3   1  0.140255  0.015726 -0.989991       60.63140    1
MTRIX1   2  0.002938 -0.993493 -0.113853       -0.05200    1
MTRIX2   2  0.999828  0.000836  0.018505       97.29790    1
MTRIX3   2 -0.018289 -0.113888  0.993325        4.69870    1
MTRIX1   3 -0.229902  0.968377  0.096907     -110.50110    1
MTRIX2   3  0.968338  0.217659  0.122252       82.59150    1
MTRIX3   3  0.097293  0.121945 -0.987757       53.35540    1
MTRIX1   4 -0.991742  0.008038 -0.127996      -97.20890    1
MTRIX2   4  0.004456 -0.995271 -0.097031       97.49640    1
MTRIX3   4 -0.128171 -0.096800  0.987017       -1.47760    1
MTRIX1   5 -0.974164 -0.225620 -0.009962      -88.49370    1
MTRIX2   5 -0.225691  0.970978  0.079157      -12.08780    1
MTRIX3   5 -0.008186  0.079361 -0.996812       50.29280    1
MTRIX1   6  0.005318  0.999912 -0.012176      -97.08730    1
MTRIX2   6 -0.993416  0.003889 -0.114498        0.36010    1
MTRIX3   6 -0.114440  0.012705  0.993349       -6.14950    1
MTRIX1   7  0.223928 -0.973976  0.035028        6.21510    1
MTRIX2   7 -0.974117 -0.224809 -0.023603        9.71160    1
MTRIX3   7  0.030863 -0.028836 -0.999108       57.50370    1
      
PROCHECK
Go to PROCHECK summary
 References