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PDBsum entry 1rsc

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Top Page protein ligands Protein-protein interface(s) links
Lyase (carbon-carbon) PDB id
1rsc
Jmol
Contents
Protein chains
(+ 2 more) 467 a.a. *
(+ 2 more) 109 a.a. *
Ligands
XBP ×8
Waters ×206
* Residue conservation analysis
HEADER    LYASE (CARBON-CARBON)                   29-MAR-94   1RSC
TITLE     STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE
TITLE    2 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN
TITLE    3 ENZYME AND XYLULOSE BISPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE
COMPND   3 CHAIN);
COMPND   4 CHAIN: A, B, C, D, E, F, G, H;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL
COMPND   9 CHAIN);
COMPND  10 CHAIN: M, I, N, J, O, K, P, L;
COMPND  11 EC: 4.1.1.39;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE   3 ORGANISM_TAXID: 269084;
SOURCE   4 STRAIN: PCC 6301;
SOURCE   5 CELL_LINE: S2;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE   8 ORGANISM_TAXID: 269084;
SOURCE   9 STRAIN: PCC 6301;
SOURCE  10 CELL_LINE: S2
KEYWDS    LYASE (CARBON-CARBON)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.NEWMAN,S.GUTTERIDGE
REVDAT   4   13-JUL-11 1RSC    1       VERSN
REVDAT   3   24-FEB-09 1RSC    1       VERSN
REVDAT   2   01-APR-03 1RSC    1       JRNL
REVDAT   1   08-MAY-95 1RSC    0
JRNL        AUTH   J.NEWMAN,S.GUTTERIDGE
JRNL        TITL   STRUCTURE OF AN EFFECTOR-INDUCED INACTIVATED STATE OF
JRNL        TITL 2 RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE: THE BINARY
JRNL        TITL 3 COMPLEX BETWEEN ENZYME AND XYLULOSE 1,5-BISPHOSPHATE.
JRNL        REF    STRUCTURE                     V.   2   495 1994
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   7922027
JRNL        DOI    10.1016/S0969-2126(00)00050-2
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.NEWMAN,S.GUTTERIDGE
REMARK   1  TITL   THE X-RAY STRUCTURE OF SYNECHOCOCCUS RIBULOSE BISPHOSPHATE
REMARK   1  TITL 2 CARBOXYLASE(SLASH)OXYGENASE ACTIVATE QUATERNARY COMPLEX AT
REMARK   1  TITL 3 2.2 ANGSTROMS RESOLUTION
REMARK   1  REF    J.BIOL.CHEM.                  V. 268 25876 1993
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 2
REMARK   1  AUTH   J.NEWMAN,C.-I.BRANDEN,T.A.JONES
REMARK   1  TITL   STRUCTURE DETERMINATION AND REFINEMENT OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM
REMARK   1  TITL 3 SYNECHOCOCCUS PCC6301
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   548 1993
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.NEWMAN,S.GUTTERIDGE
REMARK   1  TITL   THE PURIFICATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES
REMARK   1  TITL 2 OF RECOMBINANT SYNECHOCOCCUS RIBULOSE-1,5-BISPHOSPHATE
REMARK   1  TITL 3 CARBOXYLASE(SLASH)OXYGENASE FROM E. COLI
REMARK   1  REF    J.BIOL.CHEM.                  V. 265 15154 1990
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.255
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 36496
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 144
REMARK   3   SOLVENT ATOMS            : 206
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) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 0.91
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.62
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.79
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : 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  NCS MODEL : NULL
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1RSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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      112.20000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.15000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.30000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.15000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      112.20000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.30000
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: THERE ARE 7 NON-CRYSTALLOGRAPHIC SYMMETRY OPERATORS, AND
REMARK 300 THESE MUST BE USED TO GENERATE THE ENTIRE L8S8 MOLECULE.
REMARK 300 THE FORMAT OF THE FOLLOWING TRANSFORMATIONS IS FROM X-PLOR,
REMARK 300 THUS THE SYMMETRY RELATED CHAINS ARE GENERATED BY:  R'=R*R
REMARK 300 + T, R = ROTATION MATRIX, T = TRANSLATION.  THESE ARE THE
REMARK 300 ROTATION/TRANSLATION COMPONENTS TO MAP AN LS MONOMER (AM)
REMARK 300 ONTO THE REST OF THE MOLECULE.  THESE MATRICES WERE
REMARK 300 OBTAINED FROM X-PLOR AFTER REFINEMENT OF THE WHOLE L8S8
REMARK 300 920710.
REMARK 300
REMARK 300 MTRIX
REMARK 300  THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300  DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300  VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE
REMARK 300  MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300  YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300  SECOND.
REMARK 300
REMARK 300              APPLIED TO           TRANSFORMED TO
REMARK 300     MTRIX  CHAIN  RESIDUES        CHAIN  RESIDUES
REMARK 300       1      A     9 - 475         B      9 - 475
REMARK 300       1      M     2 -  51         I      2 -  51
REMARK 300       1      M    59 - 122         I     59 - 122
REMARK 300       2      A     9 - 475         C      9 - 475
REMARK 300       2      M     2 -  51         N      2 -  51
REMARK 300       2      M    59 - 122         N     59 - 122
REMARK 300       3      A     9 - 475         D      9 - 475
REMARK 300       3      M     2 -  51         J      2 -  51
REMARK 300       3      M    59 - 122         J     59 - 122
REMARK 300       4      A     9 - 475         E      9 - 475
REMARK 300       4      M     2 -  51         O      2 -  51
REMARK 300       4      M    59 - 122         O     59 - 122
REMARK 300       5      A     9 - 475         F      9 - 475
REMARK 300       5      M     2 -  51         F      2 -  51
REMARK 300       5      M    59 - 122         F     59 - 122
REMARK 300       6      A     9 - 475         G      9 - 475
REMARK 300       6      M     2 -  51         P      2 -  51
REMARK 300       6      M    59 - 122         P     59 - 122
REMARK 300       7      A     9 - 475         H      9 - 475
REMARK 300       7      M     2 -  51         L      2 -  51
REMARK 300       7      M    59 - 122         L     59 - 122
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 APPLY THE FOLLOWING TO CHAINS: A, M, B, I, C, N, D, J, E,
REMARK 350                    AND CHAINS: O, F, K, G, P, H, L
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 A     4
REMARK 465     PRO A     5
REMARK 465     LYS A     6
REMARK 465     THR A     7
REMARK 465     GLN A     8
REMARK 465     MET M     1
REMARK 465     TYR M   123
REMARK 465     MET B     4
REMARK 465     PRO B     5
REMARK 465     LYS B     6
REMARK 465     THR B     7
REMARK 465     GLN B     8
REMARK 465     MET I     1
REMARK 465     TYR I   123
REMARK 465     MET C     4
REMARK 465     PRO C     5
REMARK 465     LYS C     6
REMARK 465     THR C     7
REMARK 465     GLN C     8
REMARK 465     MET N     1
REMARK 465     TYR N   123
REMARK 465     MET D     4
REMARK 465     PRO D     5
REMARK 465     LYS D     6
REMARK 465     THR D     7
REMARK 465     GLN D     8
REMARK 465     MET J     1
REMARK 465     TYR J   123
REMARK 465     MET E     4
REMARK 465     PRO E     5
REMARK 465     LYS E     6
REMARK 465     THR E     7
REMARK 465     GLN E     8
REMARK 465     MET O     1
REMARK 465     TYR O   123
REMARK 465     MET F     4
REMARK 465     PRO F     5
REMARK 465     LYS F     6
REMARK 465     THR F     7
REMARK 465     GLN F     8
REMARK 465     MET K     1
REMARK 465     TYR K   123
REMARK 465     MET G     4
REMARK 465     PRO G     5
REMARK 465     LYS G     6
REMARK 465     THR G     7
REMARK 465     GLN G     8
REMARK 465     MET P     1
REMARK 465     TYR P   123
REMARK 465     MET H     4
REMARK 465     PRO H     5
REMARK 465     LYS H     6
REMARK 465     THR H     7
REMARK 465     GLN H     8
REMARK 465     MET L     1
REMARK 465     TYR L   123
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     GLN A  91    CG   CD   OE1  NE2
REMARK 470     ASP M  76    CG   OD1  OD2
REMARK 470     LYS M  78    CG   CD   CE   NZ
REMARK 470     SER M  79    OG
REMARK 470     GLN B  91    CG   CD   OE1  NE2
REMARK 470     ASP I  76    CG   OD1  OD2
REMARK 470     LYS I  78    CG   CD   CE   NZ
REMARK 470     SER I  79    OG
REMARK 470     GLN C  91    CG   CD   OE1  NE2
REMARK 470     ASP N  76    CG   OD1  OD2
REMARK 470     LYS N  78    CG   CD   CE   NZ
REMARK 470     SER N  79    OG
REMARK 470     GLN D  91    CG   CD   OE1  NE2
REMARK 470     ASP J  76    CG   OD1  OD2
REMARK 470     LYS J  78    CG   CD   CE   NZ
REMARK 470     SER J  79    OG
REMARK 470     GLN E  91    CG   CD   OE1  NE2
REMARK 470     ASP O  76    CG   OD1  OD2
REMARK 470     LYS O  78    CG   CD   CE   NZ
REMARK 470     SER O  79    OG
REMARK 470     GLN F  91    CG   CD   OE1  NE2
REMARK 470     ASP K  76    CG   OD1  OD2
REMARK 470     LYS K  78    CG   CD   CE   NZ
REMARK 470     SER K  79    OG
REMARK 470     GLN G  91    CG   CD   OE1  NE2
REMARK 470     ASP P  76    CG   OD1  OD2
REMARK 470     LYS P  78    CG   CD   CE   NZ
REMARK 470     SER P  79    OG
REMARK 470     GLN H  91    CG   CD   OE1  NE2
REMARK 470     ASP L  76    CG   OD1  OD2
REMARK 470     LYS L  78    CG   CD   CE   NZ
REMARK 470     SER L  79    OG
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475   M RES C SSEQI
REMARK 475     SER A    9
REMARK 475     ALA A   10
REMARK 475     ALA A   11
REMARK 475     ASP M   76
REMARK 475     CYS M   77
REMARK 475     LYS M   78
REMARK 475     GLY M  121
REMARK 475     ARG M  122
REMARK 475     SER B    9
REMARK 475     ALA B   10
REMARK 475     ALA B   11
REMARK 475     ASP I   76
REMARK 475     CYS I   77
REMARK 475     LYS I   78
REMARK 475     GLY I  121
REMARK 475     ARG I  122
REMARK 475     SER C    9
REMARK 475     ALA C   10
REMARK 475     ALA C   11
REMARK 475     ASP N   76
REMARK 475     CYS N   77
REMARK 475     LYS N   78
REMARK 475     GLY N  121
REMARK 475     ARG N  122
REMARK 475     SER D    9
REMARK 475     ALA D   10
REMARK 475     ALA D   11
REMARK 475     ASP J   76
REMARK 475     CYS J   77
REMARK 475     LYS J   78
REMARK 475     GLY J  121
REMARK 475     ARG J  122
REMARK 475     SER E    9
REMARK 475     ALA E   10
REMARK 475     ALA E   11
REMARK 475     ASP O   76
REMARK 475     CYS O   77
REMARK 475     LYS O   78
REMARK 475     GLY O  121
REMARK 475     ARG O  122
REMARK 475     SER F    9
REMARK 475     ALA F   10
REMARK 475     ALA F   11
REMARK 475     ASP K   76
REMARK 475     CYS K   77
REMARK 475     LYS K   78
REMARK 475     GLY K  121
REMARK 475     ARG K  122
REMARK 475     SER G    9
REMARK 475     ALA G   10
REMARK 475     ALA G   11
REMARK 475     ASP P   76
REMARK 475     CYS P   77
REMARK 475     LYS P   78
REMARK 475     GLY P  121
REMARK 475     ARG P  122
REMARK 475     SER H    9
REMARK 475     ALA H   10
REMARK 475     ALA H   11
REMARK 475     ASP L   76
REMARK 475     CYS L   77
REMARK 475     LYS L   78
REMARK 475     GLY L  121
REMARK 475     ARG L  122
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     GLU A   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU A   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN A  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG A  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR A  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR A  438   OH
REMARK 480     ARG A  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP A  460   CB   CG   OD1  OD2
REMARK 480     GLU A  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS A  466   CB   CG   CD   CE   NZ
REMARK 480     LYS A  474   CB   CG   CD   CE   NZ
REMARK 480     LYS M    4   CB   CG   CD   CE   NZ
REMARK 480     ARG M   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU M   35   CG   CD   OE1  OE2
REMARK 480     GLU M   64   CG   CD   OE1  OE2
REMARK 480     ARG M   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU B   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU B   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN B  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG B  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR B  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR B  438   OH
REMARK 480     ARG B  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP B  460   CB   CG   OD1  OD2
REMARK 480     GLU B  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS B  466   CB   CG   CD   CE   NZ
REMARK 480     LYS B  474   CB   CG   CD   CE   NZ
REMARK 480     LYS I    4   CB   CG   CD   CE   NZ
REMARK 480     ARG I   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU I   35   CG   CD   OE1  OE2
REMARK 480     GLU I   64   CG   CD   OE1  OE2
REMARK 480     ARG I   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU C   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU C   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN C  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG C  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR C  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR C  438   OH
REMARK 480     ARG C  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP C  460   CB   CG   OD1  OD2
REMARK 480     GLU C  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS C  466   CB   CG   CD   CE   NZ
REMARK 480     LYS C  474   CB   CG   CD   CE   NZ
REMARK 480     LYS N    4   CB   CG   CD   CE   NZ
REMARK 480     ARG N   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU N   35   CG   CD   OE1  OE2
REMARK 480     GLU N   64   CG   CD   OE1  OE2
REMARK 480     ARG N   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU D   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU D   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN D  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG D  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR D  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR D  438   OH
REMARK 480     ARG D  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP D  460   CB   CG   OD1  OD2
REMARK 480     GLU D  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS D  466   CB   CG   CD   CE   NZ
REMARK 480     LYS D  474   CB   CG   CD   CE   NZ
REMARK 480     LYS J    4   CB   CG   CD   CE   NZ
REMARK 480     ARG J   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU J   35   CG   CD   OE1  OE2
REMARK 480     GLU J   64   CG   CD   OE1  OE2
REMARK 480     ARG J   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU E   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU E   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN E  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG E  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR E  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR E  438   OH
REMARK 480     ARG E  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP E  460   CB   CG   OD1  OD2
REMARK 480     GLU E  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS E  466   CB   CG   CD   CE   NZ
REMARK 480     LYS E  474   CB   CG   CD   CE   NZ
REMARK 480     LYS O    4   CB   CG   CD   CE   NZ
REMARK 480     ARG O   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU O   35   CG   CD   OE1  OE2
REMARK 480     GLU O   64   CG   CD   OE1  OE2
REMARK 480     ARG O   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU F   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU F   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN F  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG F  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR F  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR F  438   OH
REMARK 480     ARG F  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP F  460   CB   CG   OD1  OD2
REMARK 480     GLU F  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS F  466   CB   CG   CD   CE   NZ
REMARK 480     LYS F  474   CB   CG   CD   CE   NZ
REMARK 480     LYS K    4   CB   CG   CD   CE   NZ
REMARK 480     ARG K   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU K   35   CG   CD   OE1  OE2
REMARK 480     GLU K   64   CG   CD   OE1  OE2
REMARK 480     ARG K   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU G   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU G   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN G  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG G  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR G  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR G  438   OH
REMARK 480     ARG G  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP G  460   CB   CG   OD1  OD2
REMARK 480     GLU G  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS G  466   CB   CG   CD   CE   NZ
REMARK 480     LYS G  474   CB   CG   CD   CE   NZ
REMARK 480     LYS P    4   CB   CG   CD   CE   NZ
REMARK 480     ARG P   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU P   35   CG   CD   OE1  OE2
REMARK 480     GLU P   64   CG   CD   OE1  OE2
REMARK 480     ARG P   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU H   93   CB   CG   CD   OE1  OE2
REMARK 480     GLU H   94   CB   CG   CD   OE1  OE2
REMARK 480     GLN H  429   CB   CG   CD   OE1  NE2
REMARK 480     ARG H  431   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     TYR H  438   CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 480     TYR H  438   OH
REMARK 480     ARG H  439   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     ASP H  460   CB   CG   OD1  OD2
REMARK 480     GLU H  464   CB   CG   CD   OE1  OE2
REMARK 480     LYS H  466   CB   CG   CD   CE   NZ
REMARK 480     LYS H  474   CB   CG   CD   CE   NZ
REMARK 480     LYS L    4   CB   CG   CD   CE   NZ
REMARK 480     ARG L   24   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU L   35   CG   CD   OE1  OE2
REMARK 480     GLU L   64   CG   CD   OE1  OE2
REMARK 480     ARG L   88   CB   CG   CD   NE   CZ   NH1  NH2
REMARK 700
REMARK 700 SHEET
REMARK 700 S1 IN *SHEET RECORDS BELOW IS THE L-SUBUNIT N-TERMINAL
REMARK 700 SHEET.  S2 IN *SHEET* RECORDS BELOW IS THE L-SUBUNIT C-TERM
REMARK 700 DOMAIN SHEET.  S3 IN *SHEET* RECORDS BELOW IS THE S-SUBUNIT
REMARK 700 SHEET.  THIS SHEET IS +1, -2X, -1.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: XBP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 3P5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 3P8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP H 476
DBREF  1RSC A    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC M    2   123  UNP    P04716   RBS_SYNP6        1    110
DBREF  1RSC B    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC I    2   123  UNP    P04716   RBS_SYNP6        1    110
DBREF  1RSC C    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC N    2   123  UNP    P04716   RBS_SYNP6        1    110
DBREF  1RSC D    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC J    2   123  UNP    P04716   RBS_SYNP6        1    110
DBREF  1RSC E    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC O    2   123  UNP    P04716   RBS_SYNP6        1    110
DBREF  1RSC F    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC K    2   123  UNP    P04716   RBS_SYNP6        1    110
DBREF  1RSC G    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC P    2   123  UNP    P04716   RBS_SYNP6        1    110
DBREF  1RSC H    4   475  UNP    P00880   RBL_SYNP6        1    472
DBREF  1RSC L    2   123  UNP    P04716   RBS_SYNP6        1    110
SEQADV 1RSC GLU M  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RSC GLU I  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RSC GLU N  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RSC GLU J  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RSC GLU O  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RSC GLU K  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RSC GLU P  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RSC GLU L  109  UNP  P04716    GLN    96 CONFLICT
SEQRES   1 A  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 A  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 A  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 A  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 A  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 A  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 A  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 A  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 A  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 A  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 A  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 A  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 A  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 A  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 A  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 A  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 A  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 A  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 A  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 A  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 A  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 A  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 A  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 A  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 A  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 A  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 A  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 A  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 A  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 A  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 A  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 A  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 A  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 A  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 A  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 A  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 A  472  MET ASP LYS LEU
SEQRES   1 M  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 M  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 M  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 M  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 M  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 M  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 M  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 M  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 M  111  VAL HIS ARG PRO GLY ARG TYR
SEQRES   1 B  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 B  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 B  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 B  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 B  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 B  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 B  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 B  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 B  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 B  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 B  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 B  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 B  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 B  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 B  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 B  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 B  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 B  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 B  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 B  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 B  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 B  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 B  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 B  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 B  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 B  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 B  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 B  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 B  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 B  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 B  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 B  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 B  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 B  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 B  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 B  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 B  472  MET ASP LYS LEU
SEQRES   1 I  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 I  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 I  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 I  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 I  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 I  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 I  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 I  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 I  111  VAL HIS ARG PRO GLY ARG TYR
SEQRES   1 C  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 C  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 C  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 C  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 C  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 C  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 C  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 C  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 C  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 C  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 C  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 C  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 C  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 C  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 C  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 C  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 C  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 C  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 C  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 C  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 C  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 C  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 C  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 C  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 C  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 C  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 C  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 C  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 C  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 C  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 C  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 C  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 C  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 C  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 C  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 C  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 C  472  MET ASP LYS LEU
SEQRES   1 N  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 N  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 N  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 N  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 N  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 N  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 N  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 N  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 N  111  VAL HIS ARG PRO GLY ARG TYR
SEQRES   1 D  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 D  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 D  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 D  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 D  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 D  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 D  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 D  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 D  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 D  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 D  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 D  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 D  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 D  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 D  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 D  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 D  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 D  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 D  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 D  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 D  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 D  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 D  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 D  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 D  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 D  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 D  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 D  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 D  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 D  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 D  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 D  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 D  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 D  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 D  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 D  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 D  472  MET ASP LYS LEU
SEQRES   1 J  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 J  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 J  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 J  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 J  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 J  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 J  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 J  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 J  111  VAL HIS ARG PRO GLY ARG TYR
SEQRES   1 E  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 E  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 E  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 E  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 E  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 E  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 E  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 E  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 E  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 E  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 E  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 E  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 E  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 E  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 E  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 E  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 E  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 E  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 E  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 E  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 E  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 E  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 E  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 E  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 E  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 E  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 E  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 E  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 E  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 E  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 E  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 E  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 E  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 E  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 E  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 E  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 E  472  MET ASP LYS LEU
SEQRES   1 O  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 O  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 O  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 O  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 O  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 O  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 O  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 O  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 O  111  VAL HIS ARG PRO GLY ARG TYR
SEQRES   1 F  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 F  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 F  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 F  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 F  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 F  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 F  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 F  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 F  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 F  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 F  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 F  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 F  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 F  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 F  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 F  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 F  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 F  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 F  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 F  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 F  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 F  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 F  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 F  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 F  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 F  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 F  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 F  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 F  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 F  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 F  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 F  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 F  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 F  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 F  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 F  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 F  472  MET ASP LYS LEU
SEQRES   1 K  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 K  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 K  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 K  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 K  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 K  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 K  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 K  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 K  111  VAL HIS ARG PRO GLY ARG TYR
SEQRES   1 G  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 G  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 G  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 G  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 G  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 G  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 G  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 G  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 G  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 G  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 G  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 G  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 G  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 G  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 G  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 G  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 G  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 G  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 G  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 G  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 G  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 G  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 G  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 G  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 G  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 G  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 G  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 G  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 G  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 G  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 G  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 G  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 G  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 G  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 G  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 G  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 G  472  MET ASP LYS LEU
SEQRES   1 P  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 P  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 P  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 P  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 P  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 P  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 P  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 P  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 P  111  VAL HIS ARG PRO GLY ARG TYR
SEQRES   1 H  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 H  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 H  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 H  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 H  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 H  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 H  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 H  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 H  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 H  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 H  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 H  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 H  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 H  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 H  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 H  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 H  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 H  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 H  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 H  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 H  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 H  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 H  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 H  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 H  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 H  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 H  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 H  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 H  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 H  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 H  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 H  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 H  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 H  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 H  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 H  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 H  472  MET ASP LYS LEU
SEQRES   1 L  111  MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES   2 L  111  THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES   3 L  111  ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES   4 L  111  PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES   5 L  111  PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES   6 L  111  LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES   7 L  111  ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES   8 L  111  PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES   9 L  111  VAL HIS ARG PRO GLY ARG TYR
MODRES 1RSC THR E   65  THR  GLYCOSYLATION SITE
MODRES 1RSC THR H   65  THR  GLYCOSYLATION SITE
HET    XBP  A 476      18
HET    XBP  B 476      18
HET    XBP  C 476      18
HET    XBP  D 476      18
HET    XBP  E 476      18
HET    XBP  F 476      18
HET    XBP  G 476      18
HET    XBP  H 476      18
HETNAM     XBP XYLULOSE-1,5-BISPHOSPHATE
FORMUL  17  XBP    8(C5 H12 O11 P2)
FORMUL  25  HOH   *206(H2 O)
HELIX    1   A LYS A   21  TYR A   24  1                                   4
HELIX    2   B ALA A   50  GLU A   60  1N-TERMINAL DOMAIN HELICES         11
HELIX    3  BB MET A   77  TYR A   80  1N-TERMINAL DOMAIN HELICES          4
HELIX    4   C VAL A  113  VAL A  121  1N-TERMINAL DOMAIN HELICES          9
HELIX    5   D VAL A  142  VAL A  145  1                                   4
HELIX    6   E ILE A  155  LEU A  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX    7   1 ALA A  182  ARG A  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX    8   2 TRP A  214  THR A  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX    9   3 CYS A  247  GLU A  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX   10   4 PHE A  269  ASN A  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX   11   F HIS A  298  ASP A  302  1                                   5
HELIX   12   5 PHE A  311  SER A  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX   13   6 LYS A  339  ARG A  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX   14   7 MET A  387  PHE A  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX   15   P GLY A  404  LEU A  407  1P - PHOSPHATE BINDING HELIX        4
HELIX   16   8 ASN A  413  GLU A  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX   17   G LEU A  437  TRP A  451  1                                  15
HELIX   18   H PRO A  453  TRP A  462  1                                  10
HELIX   19  MA ASP M   23  GLN M   36  11ST HELIX OF S-SUBUNIT            14
HELIX   20  MB PRO M   80  GLU M   93  12ND HELIX OF S-SUBUNIT            14
HELIX   21   A LYS B   21  TYR B   24  1                                   4
HELIX   22   B ALA B   50  GLU B   60  1N-TERMINAL DOMAIN HELICES         11
HELIX   23  BB MET B   77  TYR B   80  1N-TERMINAL DOMAIN HELICES          4
HELIX   24   C VAL B  113  VAL B  121  1N-TERMINAL DOMAIN HELICES          9
HELIX   25   D VAL B  142  VAL B  145  1                                   4
HELIX   26   E ILE B  155  LEU B  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX   27   1 ALA B  182  ARG B  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX   28   2 TRP B  214  THR B  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX   29   3 CYS B  247  GLU B  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX   30   4 PHE B  269  ASN B  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX   31   F HIS B  298  ASP B  302  1                                   5
HELIX   32   5 PHE B  311  SER B  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX   33   6 LYS B  339  ARG B  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX   34   7 MET B  387  PHE B  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX   35   P GLY B  404  LEU B  407  1P - PHOSPHATE BINDING HELIX        4
HELIX   36   8 ASN B  413  GLU B  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX   37   G LEU B  437  TRP B  451  1                                  15
HELIX   38   H PRO B  453  TRP B  462  1                                  10
HELIX   39  MA ASP I   23  GLN I   36  11ST HELIX OF S-SUBUNIT            14
HELIX   40  MB PRO I   80  GLU I   93  12ND HELIX OF S-SUBUNIT            14
HELIX   41   A LYS C   21  TYR C   24  1                                   4
HELIX   42   B ALA C   50  GLU C   60  1N-TERMINAL DOMAIN HELICES         11
HELIX   43  BB MET C   77  TYR C   80  1N-TERMINAL DOMAIN HELICES          4
HELIX   44   C VAL C  113  VAL C  121  1N-TERMINAL DOMAIN HELICES          9
HELIX   45   D VAL C  142  VAL C  145  1                                   4
HELIX   46   E ILE C  155  LEU C  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX   47   1 ALA C  182  ARG C  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX   48   2 TRP C  214  THR C  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX   49   3 CYS C  247  GLU C  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX   50   4 PHE C  269  ASN C  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX   51   F HIS C  298  ASP C  302  1                                   5
HELIX   52   5 PHE C  311  SER C  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX   53   6 LYS C  339  ARG C  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX   54   7 MET C  387  PHE C  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX   55   P GLY C  404  LEU C  407  1P - PHOSPHATE BINDING HELIX        4
HELIX   56   8 ASN C  413  GLU C  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX   57   G LEU C  437  TRP C  451  1                                  15
HELIX   58   H PRO C  453  TRP C  462  1                                  10
HELIX   59  MA ASP N   23  GLN N   36  11ST HELIX OF S-SUBUNIT            14
HELIX   60  MB PRO N   80  GLU N   93  12ND HELIX OF S-SUBUNIT            14
HELIX   61   A LYS D   21  TYR D   24  1                                   4
HELIX   62   B ALA D   50  GLU D   60  1N-TERMINAL DOMAIN HELICES         11
HELIX   63  BB MET D   77  TYR D   80  1N-TERMINAL DOMAIN HELICES          4
HELIX   64   C VAL D  113  VAL D  121  1N-TERMINAL DOMAIN HELICES          9
HELIX   65   D VAL D  142  VAL D  145  1                                   4
HELIX   66   E ILE D  155  LEU D  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX   67   1 ALA D  182  ARG D  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX   68   2 TRP D  214  THR D  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX   69   3 CYS D  247  GLU D  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX   70   4 PHE D  269  ASN D  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX   71   F HIS D  298  ASP D  302  1                                   5
HELIX   72   5 PHE D  311  SER D  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX   73   6 LYS D  339  ARG D  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX   74   7 MET D  387  PHE D  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX   75   P GLY D  404  LEU D  407  1P - PHOSPHATE BINDING HELIX        4
HELIX   76   8 ASN D  413  GLU D  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX   77   G LEU D  437  TRP D  451  1                                  15
HELIX   78   H PRO D  453  TRP D  462  1                                  10
HELIX   79  MA ASP J   23  GLN J   36  11ST HELIX OF S-SUBUNIT            14
HELIX   80  MB PRO J   80  GLU J   93  12ND HELIX OF S-SUBUNIT            14
HELIX   81   A LYS E   21  TYR E   24  1                                   4
HELIX   82   B ALA E   50  GLU E   60  1N-TERMINAL DOMAIN HELICES         11
HELIX   83  BB MET E   77  TYR E   80  1N-TERMINAL DOMAIN HELICES          4
HELIX   84   C VAL E  113  VAL E  121  1N-TERMINAL DOMAIN HELICES          9
HELIX   85   D VAL E  142  VAL E  145  1                                   4
HELIX   86   E ILE E  155  LEU E  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX   87   1 ALA E  182  ARG E  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX   88   2 TRP E  214  THR E  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX   89   3 CYS E  247  GLU E  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX   90   4 PHE E  269  ASN E  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX   91   F HIS E  298  ASP E  302  1                                   5
HELIX   92   5 PHE E  311  SER E  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX   93   6 LYS E  339  ARG E  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX   94   7 MET E  387  PHE E  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX   95   P GLY E  404  LEU E  407  1P - PHOSPHATE BINDING HELIX        4
HELIX   96   8 ASN E  413  GLU E  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX   97   G LEU E  437  TRP E  451  1                                  15
HELIX   98   H PRO E  453  TRP E  462  1                                  10
HELIX   99  MA ASP O   23  GLN O   36  11ST HELIX OF S-SUBUNIT            14
HELIX  100  MB PRO O   80  GLU O   93  12ND HELIX OF S-SUBUNIT            14
HELIX  101   A LYS F   21  TYR F   24  1                                   4
HELIX  102   B ALA F   50  GLU F   60  1N-TERMINAL DOMAIN HELICES         11
HELIX  103  BB MET F   77  TYR F   80  1N-TERMINAL DOMAIN HELICES          4
HELIX  104   C VAL F  113  VAL F  121  1N-TERMINAL DOMAIN HELICES          9
HELIX  105   D VAL F  142  VAL F  145  1                                   4
HELIX  106   E ILE F  155  LEU F  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX  107   1 ALA F  182  ARG F  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX  108   2 TRP F  214  THR F  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX  109   3 CYS F  247  GLU F  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX  110   4 PHE F  269  ASN F  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX  111   F HIS F  298  ASP F  302  1                                   5
HELIX  112   5 PHE F  311  SER F  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX  113   6 LYS F  339  ARG F  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX  114   7 MET F  387  PHE F  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX  115   P GLY F  404  LEU F  407  1P - PHOSPHATE BINDING HELIX        4
HELIX  116   8 ASN F  413  GLU F  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX  117   G LEU F  437  TRP F  451  1                                  15
HELIX  118   H PRO F  453  TRP F  462  1                                  10
HELIX  119  MA ASP K   23  GLN K   36  11ST HELIX OF S-SUBUNIT            14
HELIX  120  MB PRO K   80  GLU K   93  12ND HELIX OF S-SUBUNIT            14
HELIX  121   A LYS G   21  TYR G   24  1                                   4
HELIX  122   B ALA G   50  GLU G   60  1N-TERMINAL DOMAIN HELICES         11
HELIX  123  BB MET G   77  TYR G   80  1N-TERMINAL DOMAIN HELICES          4
HELIX  124   C VAL G  113  VAL G  121  1N-TERMINAL DOMAIN HELICES          9
HELIX  125   D VAL G  142  VAL G  145  1                                   4
HELIX  126   E ILE G  155  LEU G  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX  127   1 ALA G  182  ARG G  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX  128   2 TRP G  214  THR G  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX  129   3 CYS G  247  GLU G  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX  130   4 PHE G  269  ASN G  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX  131   F HIS G  298  ASP G  302  1                                   5
HELIX  132   5 PHE G  311  SER G  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX  133   6 LYS G  339  ARG G  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX  134   7 MET G  387  PHE G  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX  135   P GLY G  404  LEU G  407  1P - PHOSPHATE BINDING HELIX        4
HELIX  136   8 ASN G  413  GLU G  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX  137   G LEU G  437  TRP G  451  1                                  15
HELIX  138   H PRO G  453  TRP G  462  1                                  10
HELIX  139  MA ASP P   23  GLN P   36  11ST HELIX OF S-SUBUNIT            14
HELIX  140  MB PRO P   80  GLU P   93  12ND HELIX OF S-SUBUNIT            14
HELIX  141   A LYS H   21  TYR H   24  1                                   4
HELIX  142   B ALA H   50  GLU H   60  1N-TERMINAL DOMAIN HELICES         11
HELIX  143  BB MET H   77  TYR H   80  1N-TERMINAL DOMAIN HELICES          4
HELIX  144   C VAL H  113  VAL H  121  1N-TERMINAL DOMAIN HELICES          9
HELIX  145   D VAL H  142  VAL H  145  1                                   4
HELIX  146   E ILE H  155  LEU H  162  1N-TERM & C-TERM DOMAIN LINK        8
HELIX  147   1 ALA H  182  ARG H  194  1FIRST HELIX OF C-TERM DOMAIN      13
HELIX  148   2 TRP H  214  THR H  232  12ND HELIX OF C-TERM DOMAIN        19
HELIX  149   3 CYS H  247  GLU H  259  13RD HELIX OF C-TERM DOMAIN        13
HELIX  150   4 PHE H  269  ASN H  287  14TH HELIX OF C-TERM DOMAIN        19
HELIX  151   F HIS H  298  ASP H  302  1                                   5
HELIX  152   5 PHE H  311  SER H  321  15TH HELIX OF C-TERM DOMAIN        11
HELIX  153   6 LYS H  339  ARG H  350  16TH HELIX OF C-TERM DOMAIN        12
HELIX  154   7 MET H  387  PHE H  394  17TH HELIX OF C-TERM DOMAIN         8
HELIX  155   P GLY H  404  LEU H  407  1P - PHOSPHATE BINDING HELIX        4
HELIX  156   8 ASN H  413  GLU H  433  18TH HELIX OF C-TERM DOMAIN        21
HELIX  157   G LEU H  437  TRP H  451  1                                  15
HELIX  158   H PRO H  453  TRP H  462  1                                  10
HELIX  159  MA ASP L   23  GLN L   36  11ST HELIX OF S-SUBUNIT            14
HELIX  160  MB PRO L   80  GLU L   93  12ND HELIX OF S-SUBUNIT            14
SHEET    1  S1 4 LYS A  83  PRO A  89  0
SHEET    2  S1 4 SER A  96  TYR A 103 -1
SHEET    3  S1 4 LEU A  36  PRO A  44 -1
SHEET    4  S1 4 ILE A 130  ARG A 139 -1
SHEET    1  S2 8 MET A 169  GLY A 171  0
SHEET    2  S2 8 THR A 200  ASP A 202  1
SHEET    3  S2 8 LEU A 240  ASN A 241  1
SHEET    4  S2 8 ILE A 264  ASP A 268  1
SHEET    5  S2 8 LEU A 290  HIS A 294  1
SHEET    6  S2 8 HIS A 325  HIS A 327  1
SHEET    7  S2 8 LEU A 375  SER A 379  1
SHEET    8  S2 8 VAL A 399  GLN A 401  1
SHEET    1  S3 4 THR M  68  MET M  69  0
SHEET    2  S3 4 HIS M  39  ASN M  45 -1
SHEET    3  S3 4 TYR M  98  ASP M 105 -1
SHEET    4  S3 4 CYS M 110  HIS M 118 -1
SHEET    1  S4 4 LYS B  83  PRO B  89  0
SHEET    2  S4 4 SER B  96  TYR B 103 -1
SHEET    3  S4 4 LEU B  36  PRO B  44 -1
SHEET    4  S4 4 ILE B 130  ARG B 139 -1
SHEET    1  S5 8 MET B 169  GLY B 171  0
SHEET    2  S5 8 THR B 200  ASP B 202  1
SHEET    3  S5 8 LEU B 240  ASN B 241  1
SHEET    4  S5 8 ILE B 264  ASP B 268  1
SHEET    5  S5 8 LEU B 290  HIS B 294  1
SHEET    6  S5 8 HIS B 325  HIS B 327  1
SHEET    7  S5 8 LEU B 375  SER B 379  1
SHEET    8  S5 8 VAL B 399  GLN B 401  1
SHEET    1  S6 4 THR I  68  MET I  69  0
SHEET    2  S6 4 HIS I  39  ASN I  45 -1
SHEET    3  S6 4 TYR I  98  ASP I 105 -1
SHEET    4  S6 4 CYS I 110  HIS I 118 -1
SHEET    1  S7 4 LYS C  83  PRO C  89  0
SHEET    2  S7 4 SER C  96  TYR C 103 -1
SHEET    3  S7 4 LEU C  36  PRO C  44 -1
SHEET    4  S7 4 ILE C 130  ARG C 139 -1
SHEET    1  S8 8 MET C 169  GLY C 171  0
SHEET    2  S8 8 THR C 200  ASP C 202  1
SHEET    3  S8 8 LEU C 240  ASN C 241  1
SHEET    4  S8 8 ILE C 264  ASP C 268  1
SHEET    5  S8 8 LEU C 290  HIS C 294  1
SHEET    6  S8 8 HIS C 325  HIS C 327  1
SHEET    7  S8 8 LEU C 375  SER C 379  1
SHEET    8  S8 8 VAL C 399  GLN C 401  1
SHEET    1  S9 4 THR N  68  MET N  69  0
SHEET    2  S9 4 HIS N  39  ASN N  45 -1
SHEET    3  S9 4 TYR N  98  ASP N 105 -1
SHEET    4  S9 4 CYS N 110  HIS N 118 -1
SHEET    1 S10 4 LYS D  83  PRO D  89  0
SHEET    2 S10 4 SER D  96  TYR D 103 -1
SHEET    3 S10 4 LEU D  36  PRO D  44 -1
SHEET    4 S10 4 ILE D 130  ARG D 139 -1
SHEET    1 S11 8 MET D 169  GLY D 171  0
SHEET    2 S11 8 THR D 200  ASP D 202  1
SHEET    3 S11 8 LEU D 240  ASN D 241  1
SHEET    4 S11 8 ILE D 264  ASP D 268  1
SHEET    5 S11 8 LEU D 290  HIS D 294  1
SHEET    6 S11 8 HIS D 325  HIS D 327  1
SHEET    7 S11 8 LEU D 375  SER D 379  1
SHEET    8 S11 8 VAL D 399  GLN D 401  1
SHEET    1 S12 4 THR J  68  MET J  69  0
SHEET    2 S12 4 HIS J  39  ASN J  45 -1
SHEET    3 S12 4 TYR J  98  ASP J 105 -1
SHEET    4 S12 4 CYS J 110  HIS J 118 -1
SHEET    1 S13 4 LYS E  83  PRO E  89  0
SHEET    2 S13 4 SER E  96  TYR E 103 -1
SHEET    3 S13 4 LEU E  36  PRO E  44 -1
SHEET    4 S13 4 ILE E 130  ARG E 139 -1
SHEET    1 S14 8 MET E 169  GLY E 171  0
SHEET    2 S14 8 THR E 200  ASP E 202  1
SHEET    3 S14 8 LEU E 240  ASN E 241  1
SHEET    4 S14 8 ILE E 264  ASP E 268  1
SHEET    5 S14 8 LEU E 290  HIS E 294  1
SHEET    6 S14 8 HIS E 325  HIS E 327  1
SHEET    7 S14 8 LEU E 375  SER E 379  1
SHEET    8 S14 8 VAL E 399  GLN E 401  1
SHEET    1 S15 4 THR O  68  MET O  69  0
SHEET    2 S15 4 HIS O  39  ASN O  45 -1
SHEET    3 S15 4 TYR O  98  ASP O 105 -1
SHEET    4 S15 4 CYS O 110  HIS O 118 -1
SHEET    1 S16 4 LYS F  83  PRO F  89  0
SHEET    2 S16 4 SER F  96  TYR F 103 -1
SHEET    3 S16 4 LEU F  36  PRO F  44 -1
SHEET    4 S16 4 ILE F 130  ARG F 139 -1
SHEET    1 S17 8 MET F 169  GLY F 171  0
SHEET    2 S17 8 THR F 200  ASP F 202  1
SHEET    3 S17 8 LEU F 240  ASN F 241  1
SHEET    4 S17 8 ILE F 264  ASP F 268  1
SHEET    5 S17 8 LEU F 290  HIS F 294  1
SHEET    6 S17 8 HIS F 325  HIS F 327  1
SHEET    7 S17 8 LEU F 375  SER F 379  1
SHEET    8 S17 8 VAL F 399  GLN F 401  1
SHEET    1 S18 4 THR K  68  MET K  69  0
SHEET    2 S18 4 HIS K  39  ASN K  45 -1
SHEET    3 S18 4 TYR K  98  ASP K 105 -1
SHEET    4 S18 4 CYS K 110  HIS K 118 -1
SHEET    1 S19 4 LYS G  83  PRO G  89  0
SHEET    2 S19 4 SER G  96  TYR G 103 -1
SHEET    3 S19 4 LEU G  36  PRO G  44 -1
SHEET    4 S19 4 ILE G 130  ARG G 139 -1
SHEET    1 S20 8 MET G 169  GLY G 171  0
SHEET    2 S20 8 THR G 200  ASP G 202  1
SHEET    3 S20 8 LEU G 240  ASN G 241  1
SHEET    4 S20 8 ILE G 264  ASP G 268  1
SHEET    5 S20 8 LEU G 290  HIS G 294  1
SHEET    6 S20 8 HIS G 325  HIS G 327  1
SHEET    7 S20 8 LEU G 375  SER G 379  1
SHEET    8 S20 8 VAL G 399  GLN G 401  1
SHEET    1 S21 4 THR P  68  MET P  69  0
SHEET    2 S21 4 HIS P  39  ASN P  45 -1
SHEET    3 S21 4 TYR P  98  ASP P 105 -1
SHEET    4 S21 4 CYS P 110  HIS P 118 -1
SHEET    1 S22 4 LYS H  83  PRO H  89  0
SHEET    2 S22 4 SER H  96  TYR H 103 -1
SHEET    3 S22 4 LEU H  36  PRO H  44 -1
SHEET    4 S22 4 ILE H 130  ARG H 139 -1
SHEET    1 S23 8 MET H 169  GLY H 171  0
SHEET    2 S23 8 THR H 200  ASP H 202  1
SHEET    3 S23 8 LEU H 240  ASN H 241  1
SHEET    4 S23 8 ILE H 264  ASP H 268  1
SHEET    5 S23 8 LEU H 290  HIS H 294  1
SHEET    6 S23 8 HIS H 325  HIS H 327  1
SHEET    7 S23 8 LEU H 375  SER H 379  1
SHEET    8 S23 8 VAL H 399  GLN H 401  1
SHEET    1 S24 4 THR L  68  MET L  69  0
SHEET    2 S24 4 HIS L  39  ASN L  45 -1
SHEET    3 S24 4 TYR L  98  ASP L 105 -1
SHEET    4 S24 4 CYS L 110  HIS L 118 -1
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.53
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.57
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.59
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.75
LINK         O2P XBP F 476                 OG1 THR E  65     1555   1555  2.04
LINK         OG1 THR H  65                 O2P XBP G 476     1555   1555  2.00
CISPEP   1 LYS A  175    PRO A  176          0        -5.26
CISPEP   2 LYS B  175    PRO B  176          0        -5.26
CISPEP   3 LYS C  175    PRO C  176          0        -5.29
CISPEP   4 LYS D  175    PRO D  176          0        -5.25
CISPEP   5 LYS E  175    PRO E  176          0        -5.34
CISPEP   6 LYS F  175    PRO F  176          0        -5.27
CISPEP   7 LYS G  175    PRO G  176          0        -5.24
CISPEP   8 LYS H  175    PRO H  176          0        -5.19
SITE     1  1P  4 LYS A 334  GLY A 381  GLY A 403  GLY A 404
SITE     1  2P  3 HIS A 327  ARG A 295  SER A 379
SITE     1 XBP  6 LYS A 175  ASP A 203  GLU A 204  HIS A 294
SITE     2 XBP  6 LYS A 334  SER A 379
SITE     1 1P2  4 LYS B 334  GLY B 381  GLY B 403  GLY B 404
SITE     1 2P2  3 HIS B 327  ARG B 295  SER B 379
SITE     1 BP2  6 LYS B 175  ASP B 203  GLU B 204  HIS B 294
SITE     2 BP2  6 LYS B 334  SER B 379
SITE     1 1P3  4 LYS C 334  GLY C 381  GLY C 403  GLY C 404
SITE     1 2P3  3 HIS C 327  ARG C 295  SER C 379
SITE     1 BP3  6 LYS C 175  ASP C 203  GLU C 204  HIS C 294
SITE     2 BP3  6 LYS C 334  SER C 379
SITE     1 1P4  4 LYS D 334  GLY D 381  GLY D 403  GLY D 404
SITE     1 2P4  3 HIS D 327  ARG D 295  SER D 379
SITE     1 BP4  6 LYS D 175  ASP D 203  GLU D 204  HIS D 294
SITE     2 BP4  6 LYS D 334  SER D 379
SITE     1 1P5  4 LYS E 334  GLY E 381  GLY E 403  GLY E 404
SITE     1 3P5  3 HIS E 327  ARG E 295  SER E 379
SITE     1 BP5  6 LYS E 175  ASP E 203  GLU E 204  HIS E 294
SITE     2 BP5  6 LYS E 334  SER E 379
SITE     1 1P6  4 LYS F 334  GLY F 381  GLY F 403  GLY F 404
SITE     1 2P6  3 HIS F 327  ARG F 295  SER F 379
SITE     1 BP6  6 LYS F 175  ASP F 203  GLU F 204  HIS F 294
SITE     2 BP6  6 LYS F 334  SER F 379
SITE     1 1P7  4 LYS G 334  GLY G 381  GLY G 403  GLY G 404
SITE     1 2P7  3 HIS G 327  ARG G 295  SER G 379
SITE     1 BP7  6 LYS G 175  ASP G 203  GLU G 204  HIS G 294
SITE     2 BP7  6 LYS G 334  SER G 379
SITE     1 1P8  4 LYS H 334  GLY H 381  GLY H 403  GLY H 404
SITE     1 3P8  3 HIS H 327  ARG H 295  SER H 379
SITE     1 BP8  6 LYS H 175  ASP H 203  GLU H 204  HIS H 294
SITE     2 BP8  6 LYS H 334  SER H 379
SITE     1 AC1 25 LYS A 175  LYS A 177  ASP A 203  GLU A 204
SITE     2 AC1 25 HIS A 294  ARG A 295  HIS A 327  LYS A 334
SITE     3 AC1 25 LEU A 335  SER A 379  GLY A 380  GLY A 381
SITE     4 AC1 25 GLY A 403  GLY A 404  HOH A 496  HOH A 588
SITE     5 AC1 25 HOH A 589  HOH A 590  HOH A 598  HOH A 599
SITE     6 AC1 25 GLU B  60  THR B  65  TRP B  66  ASN B 123
SITE     7 AC1 25 HOH B 477
SITE     1 AC2 20 GLU A  60  THR A  65  TRP A  66  ASN A 123
SITE     2 AC2 20 HOH A 615  LYS B 175  LYS B 177  ASP B 203
SITE     3 AC2 20 GLU B 204  HIS B 294  ARG B 295  HIS B 327
SITE     4 AC2 20 LYS B 334  LEU B 335  SER B 379  GLY B 380
SITE     5 AC2 20 GLY B 381  GLY B 403  GLY B 404  HOH B 479
SITE     1 AC3 18 LYS C 175  LYS C 177  ASP C 203  GLU C 204
SITE     2 AC3 18 HIS C 294  ARG C 295  HIS C 327  LYS C 334
SITE     3 AC3 18 LEU C 335  SER C 379  GLY C 380  GLY C 381
SITE     4 AC3 18 GLY C 403  GLY C 404  GLU D  60  THR D  65
SITE     5 AC3 18 TRP D  66  ASN D 123
SITE     1 AC4 18 GLU C  60  THR C  65  TRP C  66  ASN C 123
SITE     2 AC4 18 LYS D 175  LYS D 177  ASP D 203  GLU D 204
SITE     3 AC4 18 HIS D 294  ARG D 295  HIS D 327  LYS D 334
SITE     4 AC4 18 LEU D 335  SER D 379  GLY D 380  GLY D 381
SITE     5 AC4 18 GLY D 403  GLY D 404
SITE     1 AC5 18 LYS E 175  LYS E 177  ASP E 203  GLU E 204
SITE     2 AC5 18 HIS E 294  ARG E 295  HIS E 327  LYS E 334
SITE     3 AC5 18 LEU E 335  SER E 379  GLY E 380  GLY E 381
SITE     4 AC5 18 GLY E 403  GLY E 404  GLU F  60  THR F  65
SITE     5 AC5 18 TRP F  66  ASN F 123
SITE     1 AC6 18 GLU E  60  THR E  65  TRP E  66  ASN E 123
SITE     2 AC6 18 LYS F 175  LYS F 177  ASP F 203  GLU F 204
SITE     3 AC6 18 HIS F 294  ARG F 295  HIS F 327  LYS F 334
SITE     4 AC6 18 LEU F 335  SER F 379  GLY F 380  GLY F 381
SITE     5 AC6 18 GLY F 403  GLY F 404
SITE     1 AC7 18 LYS G 175  LYS G 177  ASP G 203  GLU G 204
SITE     2 AC7 18 HIS G 294  ARG G 295  HIS G 327  LYS G 334
SITE     3 AC7 18 LEU G 335  SER G 379  GLY G 380  GLY G 381
SITE     4 AC7 18 GLY G 403  GLY G 404  GLU H  60  THR H  65
SITE     5 AC7 18 TRP H  66  ASN H 123
SITE     1 AC8 18 GLU G  60  THR G  65  TRP G  66  ASN G 123
SITE     2 AC8 18 LYS H 175  LYS H 177  ASP H 203  GLU H 204
SITE     3 AC8 18 HIS H 294  ARG H 295  HIS H 327  LYS H 334
SITE     4 AC8 18 LEU H 335  SER H 379  GLY H 380  GLY H 381
SITE     5 AC8 18 GLY H 403  GLY H 404
CRYST1  224.400  112.600  200.300  90.00  90.00  90.00 P 21 21 21   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      0.004456  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008881  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004993        0.00000
MTRIX1   1  0.054944  0.991599  0.117102       58.71750    1
MTRIX2   1  0.991904 -0.067652  0.107466      -60.96300    1
MTRIX3   1  0.114485  0.110249 -0.987288      -12.23330    1
MTRIX1   2 -0.003182  0.994466  0.105014       63.56160    1
MTRIX2   2 -0.993371  0.008924 -0.114609      104.72820    1
MTRIX3   2 -0.114912 -0.104682  0.987845       11.92890    1
MTRIX1   3  0.998457 -0.055196  0.006022        1.26820    1
MTRIX2   3 -0.055177 -0.998471 -0.003268       46.89430    1
MTRIX3   3  0.006193  0.002931 -0.999977       -0.86640    1
MTRIX1   4 -0.999944  0.001258 -0.010490      168.47231    1
MTRIX2   4  0.003491 -0.976470 -0.215626       41.55370    1
MTRIX3   4 -0.009972 -0.215651  0.976420        5.38740    1
MTRIX1   5 -0.056378 -0.992918 -0.104574      109.90480    1
MTRIX2   5 -0.993220  0.045110  0.107144      103.99110    1
MTRIX3   5 -0.101667  0.109906 -0.988729        5.96560    1
MTRIX1   6 -0.001047 -0.993269 -0.115824      105.05120    1
MTRIX2   6  0.994820  0.012807 -0.100839      -62.86620    1
MTRIX3   6  0.101644 -0.115118  0.988138       -6.11100    1
MTRIX1   7 -0.998542  0.053826  0.004015      167.20731    1
MTRIX2   7  0.053403  0.974410  0.218344       -3.71750    1
MTRIX3   7  0.007841  0.218240 -0.975864       -5.55990    1
      
PROCHECK
Go to PROCHECK summary
 References