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PDBsum entry 1rbl

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1rbl
Jmol
Contents
Protein chains
(+ 2 more) 467 a.a. *
(+ 2 more) 109 a.a. *
Ligands
CAP ×8
FMT ×8
Metals
_MG ×8
Waters ×292
* Residue conservation analysis
HEADER    LYASE                                   12-MAY-93   1RBL
TITLE     STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE
TITLE    2 CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301
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 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE   7 ORGANISM_TAXID: 269084;
SOURCE   8 STRAIN: PCC 6301
KEYWDS    LYASE(CARBON-CARBON), LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.NEWMAN,S.GUTTERIDGE,C.-I.BRANDEN,T.A.JONES
REVDAT   4   13-JUL-11 1RBL    1       VERSN
REVDAT   3   24-FEB-09 1RBL    1       VERSN
REVDAT   2   08-MAR-95 1RBL    1       AUTHOR JRNL
REVDAT   1   22-JUN-94 1RBL    0
JRNL        AUTH   J.NEWMAN,C.I.BRANDEN,T.A.JONES
JRNL        TITL   STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE
JRNL        TITL 2 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM SYNECHOCOCCUS
JRNL        TITL 3 PCC6301.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   548 1993
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15299492
JRNL        DOI    10.1107/S090744499300530X
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 ACTIVATED QUATERNARY COMPLEX AT
REMARK   1  TITL 3 2.2 ANGSTROMS RESOLUTION
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    2.20 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) : 2.20
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) : 0.200
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          : 200
REMARK   3   SOLVENT ATOMS            : 292
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.26
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.26
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:
REMARK   3  THERE ARE SEVEN NON-CRYSTALLOGRAPHIC SYMMETRY OPERATORS,
REMARK   3  AND THESE MUST BE USED TO GENERATE THE ENTIRE L8S8
REMARK   3  MOLECULE.  THE FORMAT OF THE FOLLOWING TRANSFORMATIONS IS
REMARK   3  FROM X-PLOR, THUS THE SYMMETRY RELATED CHAINS ARE GENERATED
REMARK   3  BY R'=R*R + T, R=ROTATION MATRIX, T=TRANSLATION.
REMARK   4
REMARK   4 1RBL 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   (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
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      111.95000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.85000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.95000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.85000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      111.95000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.95000
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: THESE ARE THE ROTATION/TRANSLATION COMPONENTS TO MAP AN
REMARK 300 LS MONOMER (AM) ONTO THE REST OF THE MOLECULE.  THESE
REMARK 300 MATRICES WERE OBTAINED FROM X-PLOR AFTER REFINEMENT OF THE
REMARK 300 WHOLE L8S8 920710.
REMARK 300
REMARK 300 MTRIX 1 TAKES AM TO BI.
REMARK 300
REMARK 300 MTRIX 2 TAKES AM TO CN.
REMARK 300
REMARK 300 MTRIX 3 TAKES AM TO DJ.
REMARK 300
REMARK 300 MTRIX 4 TAKES AM TO EO.
REMARK 300
REMARK 300 MTRIX 5 TAKES AM TO FK.
REMARK 300
REMARK 300 MTRIX 6 TAKES AM TO GP.
REMARK 300
REMARK 300 MTRIX 7 TAKES AM TO HL.
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 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     ARG M  122
REMARK 475     SER B    9
REMARK 475     ALA B   10
REMARK 475     ALA B   11
REMARK 475     ARG I  122
REMARK 475     SER C    9
REMARK 475     ALA C   10
REMARK 475     ALA C   11
REMARK 475     ARG N  122
REMARK 475     SER D    9
REMARK 475     ALA D   10
REMARK 475     ALA D   11
REMARK 475     ARG J  122
REMARK 475     SER E    9
REMARK 475     ALA E   10
REMARK 475     ALA E   11
REMARK 475     ARG O  122
REMARK 475     SER F    9
REMARK 475     ALA F   10
REMARK 475     ALA F   11
REMARK 475     ARG K  122
REMARK 475     SER G    9
REMARK 475     ALA G   10
REMARK 475     ALA G   11
REMARK 475     ARG P  122
REMARK 475     SER H    9
REMARK 475     ALA H   10
REMARK 475     ALA H   11
REMARK 475     ARG L  122
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT A 478   O1
REMARK 620 2 FMT A 478   O2   43.5
REMARK 620 3 CAP A 476   O2   81.4 100.6
REMARK 620 4 GLU A 204   OE1 106.7 101.5 154.6
REMARK 620 5 CAP A 476   O3   49.3  92.5  70.9  95.7
REMARK 620 6 CAP A 476   O7  137.4 166.5  68.6  90.9  91.5
REMARK 620 7 ASP A 203   OD1 131.0  89.1 100.5  92.3 171.4  85.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B 476   O3
REMARK 620 2 CAP B 476   O7   91.5
REMARK 620 3 FMT B 478   O1   49.3 137.4
REMARK 620 4 FMT B 478   O2   92.5 166.5  43.5
REMARK 620 5 CAP B 476   O2   70.9  68.6  81.4 100.6
REMARK 620 6 GLU B 204   OE1  95.7  90.9 106.7 101.6 154.6
REMARK 620 7 ASP B 203   OD1 171.4  85.1 131.0  89.1 100.5  92.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 203   OD1
REMARK 620 2 GLU C 204   OE1  92.2
REMARK 620 3 CAP C 476   O7   85.1  90.9
REMARK 620 4 FMT C 478   O2   89.1 101.6 166.5
REMARK 620 5 CAP C 476   O3  171.4  95.7  91.5  92.5
REMARK 620 6 CAP C 476   O2  100.5 154.6  68.6 100.6  70.9
REMARK 620 7 FMT C 478   O1  131.0 106.7 137.4  43.5  49.3  81.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP D 476   O3
REMARK 620 2 FMT D 478   O1   49.3
REMARK 620 3 CAP D 476   O2   71.0  81.4
REMARK 620 4 FMT D 478   O2   92.5  43.5 100.6
REMARK 620 5 GLU D 204   OE1  95.7 106.7 154.6 101.5
REMARK 620 6 CAP D 476   O7   91.5 137.5  68.6 166.5  90.9
REMARK 620 7 ASP D 203   OD1 171.4 131.0 100.5  89.1  92.2  85.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT E 478   O2
REMARK 620 2 GLU E 204   OE1 101.5
REMARK 620 3 ASP E 203   OD1  89.1  92.2
REMARK 620 4 FMT E 478   O1   43.5 106.7 131.0
REMARK 620 5 CAP E 476   O2  100.6 154.6 100.5  81.4
REMARK 620 6 CAP E 476   O7  166.5  90.9  85.1 137.5  68.6
REMARK 620 7 CAP E 476   O3   92.5  95.7 171.4  49.3  71.0  91.5
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG F 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT F 478   O2
REMARK 620 2 FMT F 478   O1   43.5
REMARK 620 3 CAP F 476   O3   92.5  49.3
REMARK 620 4 ASP F 203   OD1  89.1 130.9 171.4
REMARK 620 5 CAP F 476   O2  100.6  81.4  70.9 100.4
REMARK 620 6 CAP F 476   O7  166.5 137.5  91.5  85.1  68.6
REMARK 620 7 GLU F 204   OE1 101.5 106.7  95.7  92.3 154.6  90.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG G 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 204   OE1
REMARK 620 2 FMT G 478   O2  101.5
REMARK 620 3 FMT G 478   O1  106.7  43.5
REMARK 620 4 CAP G 476   O3   95.7  92.5  49.3
REMARK 620 5 CAP G 476   O2  154.6 100.6  81.4  70.9
REMARK 620 6 ASP G 203   OD1  92.3  89.1 131.0 171.4 100.5
REMARK 620 7 CAP G 476   O7   90.9 166.5 137.5  91.5  68.6  85.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H 477  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP H 476   O7
REMARK 620 2 ASP H 203   OD1  85.1
REMARK 620 3 CAP H 476   O2   68.6 100.5
REMARK 620 4 FMT H 478   O2  166.5  89.1 100.6
REMARK 620 5 FMT H 478   O1  137.5 130.9  81.4  43.5
REMARK 620 6 CAP H 476   O3   91.5 171.4  70.9  92.5  49.3
REMARK 620 7 GLU H 204   OE1  90.9  92.2 154.6 101.5 106.7  95.7
REMARK 620 N                    1     2     3     4     5     6
REMARK 650
REMARK 650 HELIX
REMARK 650 HELICES A, B, BB, C, AND D PRESENTED ON THE HELIX RECORD
REMARK 650 BELOW ARE THE HELICES OF THE N-TERMINAL DOMAIN.
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEET LN1 IS -2X, +1, +2X.
REMARK 700 THE DSSP RUN DID NOT INDICATE THAT STRAND 2 WAS INDEED A
REMARK 700 STRAND.  HOWEVER, THE A/B BARREL IS CLEARLY THAT, SO STRAND
REMARK 700 2 IS INCLUDED AS A "REAL" STRAND.
REMARK 700 SHEET SS1 IS +1,-2X,-1.
REMARK 700 THE SHEET PRESENTED AS *LC1* ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY AN EIGHT-STRANDED BETA-BARREL.  THIS IS
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST
REMARK 700 AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: MG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE MAGNESIUM BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE BINDING SITE OF THE FIRST PHOSPHATE GROUP OF
REMARK 800  THE CAP
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE BINDING SITE OF THE 2ND PHOSPHATE OF CAP
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: OTHER RESIDUES INVOLVED IN BINDING THE CAP
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG2
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: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG3
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: CA3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG4
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: CA4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG5
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: 2P5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG6
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: CA6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG7
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: CA7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG8
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: 2P8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA8
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 CAP A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT H 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT G 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 477
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE ADVISORY NOTICE
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999      SWISS-PROT ENTRY NAME: RBL_SYNP6
REMARK 999
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES
REMARK 999
REMARK 999        NAME   NUMBER         NAME   CHAIN  SEQ/INSERT CODE
REMARK 999        PRO       38          ARG     A       41
REMARK 999        VAL       39          PHE     A       42
REMARK 999        GLN       88          ALA     A       91
REMARK 999        ARG      353          ALA     A      356
REMARK 999        ASP       64          ALA     M       76
REMARK 999        LYS       66          ALA     M       78
REMARK 999        SER       67          ALA     M       79
REMARK 999        GLN       97          GLU     M      109
REMARK 999        VAL      101          SER     M      113
DBREF  1RBL A    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL M    2   122  UNP    P04716   RBS_SYNP6        1    109
DBREF  1RBL B    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL I    2   122  UNP    P04716   RBS_SYNP6        1    109
DBREF  1RBL C    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL N    2   122  UNP    P04716   RBS_SYNP6        1    109
DBREF  1RBL D    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL J    2   122  UNP    P04716   RBS_SYNP6        1    109
DBREF  1RBL E    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL O    2   122  UNP    P04716   RBS_SYNP6        1    109
DBREF  1RBL F    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL K    2   122  UNP    P04716   RBS_SYNP6        1    109
DBREF  1RBL G    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL P    2   122  UNP    P04716   RBS_SYNP6        1    109
DBREF  1RBL H    9   475  UNP    P00880   RBL_SYNP6        6    472
DBREF  1RBL L    2   122  UNP    P04716   RBS_SYNP6        1    109
SEQADV 1RBL ARG A   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE A   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA A   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA A  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA M   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA M   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA M   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU M  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER M  113  UNP  P04716    VAL   100 CONFLICT
SEQADV 1RBL ARG B   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE B   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA B   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA B  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA I   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA I   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA I   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU I  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER I  113  UNP  P04716    VAL   100 CONFLICT
SEQADV 1RBL ARG C   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE C   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA C   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA C  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA N   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA N   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA N   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU N  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER N  113  UNP  P04716    VAL   100 CONFLICT
SEQADV 1RBL ARG D   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE D   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA D   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA D  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA J   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA J   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA J   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU J  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER J  113  UNP  P04716    VAL   100 CONFLICT
SEQADV 1RBL ARG E   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE E   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA E   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA E  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA O   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA O   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA O   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU O  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER O  113  UNP  P04716    VAL   100 CONFLICT
SEQADV 1RBL ARG F   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE F   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA F   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA F  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA K   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA K   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA K   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU K  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER K  113  UNP  P04716    VAL   100 CONFLICT
SEQADV 1RBL ARG G   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE G   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA G   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA G  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA P   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA P   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA P   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU P  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER P  113  UNP  P04716    VAL   100 CONFLICT
SEQADV 1RBL ARG H   41  UNP  P00880    PRO    38 CONFLICT
SEQADV 1RBL PHE H   42  UNP  P00880    VAL    39 CONFLICT
SEQADV 1RBL ALA H   91  UNP  P00880    GLN    88 CONFLICT
SEQADV 1RBL ALA H  356  UNP  P00880    ARG   353 CONFLICT
SEQADV 1RBL ALA L   76  UNP  P04716    ASP    63 CONFLICT
SEQADV 1RBL ALA L   78  UNP  P04716    LYS    65 CONFLICT
SEQADV 1RBL ALA L   79  UNP  P04716    SER    66 CONFLICT
SEQADV 1RBL GLU L  109  UNP  P04716    GLN    96 CONFLICT
SEQADV 1RBL SER L  113  UNP  P04716    VAL   100 CONFLICT
SEQRES   1 A  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 A  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 A  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 A  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 A  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 A  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 A  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 A  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 A  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 A  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 A  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 A  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 A  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 A  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 A  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 A  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 A  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 A  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 A  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 A  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 A  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 A  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 A  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 A  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 A  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 A  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 A  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 A  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 A  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 A  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 A  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 A  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 A  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 A  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 A  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 A  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 M  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 M  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 M  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 M  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 M  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 M  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 M  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 M  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 M  109  HIS ARG PRO GLY ARG
SEQRES   1 B  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 B  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 B  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 B  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 B  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 B  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 B  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 B  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 B  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 B  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 B  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 B  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 B  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 B  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 B  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 B  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 B  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 B  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 B  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 B  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 B  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 B  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 B  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 B  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 B  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 B  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 B  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 B  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 B  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 B  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 B  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 B  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 B  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 B  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 B  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 B  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 I  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 I  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 I  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 I  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 I  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 I  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 I  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 I  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 I  109  HIS ARG PRO GLY ARG
SEQRES   1 C  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 C  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 C  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 C  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 C  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 C  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 C  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 C  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 C  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 C  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 C  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 C  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 C  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 C  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 C  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 C  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 C  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 C  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 C  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 C  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 C  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 C  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 C  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 C  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 C  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 C  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 C  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 C  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 C  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 C  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 C  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 C  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 C  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 C  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 C  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 C  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 N  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 N  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 N  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 N  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 N  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 N  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 N  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 N  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 N  109  HIS ARG PRO GLY ARG
SEQRES   1 D  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 D  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 D  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 D  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 D  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 D  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 D  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 D  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 D  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 D  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 D  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 D  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 D  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 D  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 D  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 D  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 D  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 D  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 D  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 D  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 D  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 D  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 D  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 D  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 D  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 D  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 D  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 D  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 D  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 D  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 D  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 D  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 D  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 D  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 D  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 D  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 J  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 J  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 J  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 J  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 J  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 J  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 J  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 J  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 J  109  HIS ARG PRO GLY ARG
SEQRES   1 E  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 E  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 E  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 E  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 E  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 E  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 E  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 E  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 E  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 E  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 E  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 E  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 E  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 E  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 E  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 E  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 E  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 E  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 E  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 E  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 E  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 E  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 E  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 E  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 E  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 E  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 E  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 E  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 E  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 E  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 E  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 E  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 E  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 E  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 E  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 E  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 O  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 O  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 O  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 O  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 O  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 O  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 O  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 O  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 O  109  HIS ARG PRO GLY ARG
SEQRES   1 F  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 F  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 F  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 F  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 F  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 F  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 F  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 F  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 F  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 F  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 F  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 F  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 F  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 F  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 F  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 F  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 F  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 F  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 F  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 F  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 F  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 F  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 F  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 F  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 F  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 F  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 F  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 F  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 F  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 F  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 F  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 F  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 F  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 F  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 F  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 F  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 K  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 K  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 K  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 K  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 K  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 K  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 K  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 K  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 K  109  HIS ARG PRO GLY ARG
SEQRES   1 G  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 G  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 G  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 G  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 G  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 G  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 G  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 G  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 G  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 G  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 G  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 G  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 G  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 G  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 G  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 G  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 G  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 G  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 G  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 G  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 G  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 G  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 G  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 G  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 G  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 G  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 G  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 G  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 G  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 G  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 G  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 G  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 G  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 G  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 G  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 G  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 P  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 P  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 P  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 P  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 P  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 P  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 P  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 P  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 P  109  HIS ARG PRO GLY ARG
SEQRES   1 H  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES   2 H  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES   3 H  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES   4 H  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES   5 H  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES   6 H  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES   7 H  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES   8 H  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   9 H  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES  10 H  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES  11 H  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES  12 H  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES  13 H  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  14 H  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  15 H  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  16 H  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES  17 H  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES  18 H  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES  19 H  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES  20 H  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES  21 H  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES  22 H  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES  23 H  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES  24 H  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES  25 H  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES  26 H  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES  27 H  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES  28 H  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES  29 H  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  30 H  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES  31 H  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  32 H  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES  33 H  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  34 H  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES  35 H  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES  36 H  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES   1 L  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES   2 L  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES   3 L  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES   4 L  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES   5 L  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES   6 L  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES   7 L  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES   8 L  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES   9 L  109  HIS ARG PRO GLY ARG
HET     MG  A 477       1
HET     MG  B 477       1
HET     MG  C 477       1
HET     MG  D 477       1
HET     MG  E 477       1
HET     MG  F 477       1
HET     MG  G 477       1
HET     MG  H 477       1
HET    CAP  A 476      21
HET    CAP  B 476      21
HET    CAP  C 476      21
HET    CAP  D 476      21
HET    CAP  E 476      21
HET    CAP  F 476      21
HET    CAP  G 476      21
HET    CAP  H 476      21
HET    FMT  A 478       3
HET    FMT  B 478       3
HET    FMT  C 478       3
HET    FMT  D 478       3
HET    FMT  E 478       3
HET    FMT  F 478       3
HET    FMT  G 478       3
HET    FMT  H 478       3
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM     FMT FORMIC ACID
FORMUL  17   MG    8(MG 2+)
FORMUL  25  CAP    8(C6 H14 O13 P2)
FORMUL  33  FMT    8(C H2 O2)
FORMUL  41  HOH   *292(H2 O)
HELIX    1   A LYS A   21  TYR A   24  1SEE REMARK 8.                      4
HELIX    2   B ALA A   50  GLU A   60  1SEE REMARK 8.                     11
HELIX    3  BB MET A   77  TYR A   80  1SEE REMARK 8.                      4
HELIX    4   C VAL A  113  VAL A  121  1SEE REMARK 8.                      9
HELIX    5   D VAL A  142  VAL A  145  1SEE REMARK 8.                      4
HELIX    6   E ILE A  155  LEU A  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX    7   1 ALA A  182  ARG A  194  1FIRST HELIX OF A/B BARREL         13
HELIX    8   2 TRP A  214  THR A  232  12ND HELIX OF A/B BARREL           19
HELIX    9   3 CYS A  247  GLU A  259  13RD HELIX OF A/B BARREL           13
HELIX   10   4 PHE A  269  ASN A  287  14TH HELIX OF A/B BARREL           19
HELIX   11   F HIS A  298  ASP A  302  1                                   5
HELIX   12   5 PHE A  311  SER A  321  15TH HELIX OF A/B BARREL           11
HELIX   13   6 LYS A  339  ARG A  350  16TH HELIX OF A/B BARREL           12
HELIX   14   7 MET A  387  PHE A  394  17TH HELIX OF A/B BARREL            8
HELIX   15   P GLY A  404  LEU A  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX   16   8 ASN A  413  GLU A  433  18TH HELIX OF A/B BARREL           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  B' TYR A   80  GLU A   93  12ND HELIX - SMALL SUBUNIT         14
HELIX   20   A LYS B   21  TYR B   24  1SEE REMARK 8.                      4
HELIX   21   B ALA B   50  GLU B   60  1SEE REMARK 8.                     11
HELIX   22  BB MET B   77  TYR B   80  1SEE REMARK 8.                      4
HELIX   23   C VAL B  113  VAL B  121  1SEE REMARK 8.                      9
HELIX   24   D VAL B  142  VAL B  145  1SEE REMARK 8.                      4
HELIX   25   E ILE B  155  LEU B  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX   26   1 ALA B  182  ARG B  194  1FIRST HELIX OF A/B BARREL         13
HELIX   27   2 TRP B  214  THR B  232  12ND HELIX OF A/B BARREL           19
HELIX   28   3 CYS B  247  GLU B  259  13RD HELIX OF A/B BARREL           13
HELIX   29   4 PHE B  269  ASN B  287  14TH HELIX OF A/B BARREL           19
HELIX   30   F HIS B  298  ASP B  302  1                                   5
HELIX   31   5 PHE B  311  SER B  321  15TH HELIX OF A/B BARREL           11
HELIX   32   6 LYS B  339  ARG B  350  16TH HELIX OF A/B BARREL           12
HELIX   33   7 MET B  387  PHE B  394  17TH HELIX OF A/B BARREL            8
HELIX   34   P GLY B  404  LEU B  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX   35   8 ASN B  413  GLU B  433  18TH HELIX OF A/B BARREL           21
HELIX   36   G LEU B  437  TRP B  451  1                                  15
HELIX   37   H PRO B  453  TRP B  462  1                                  10
HELIX   38  B' TYR B   80  GLU B   93  12ND HELIX - SMALL SUBUNIT         14
HELIX   39   A LYS C   21  TYR C   24  1SEE REMARK 8.                      4
HELIX   40   B ALA C   50  GLU C   60  1SEE REMARK 8.                     11
HELIX   41  BB MET C   77  TYR C   80  1SEE REMARK 8.                      4
HELIX   42   C VAL C  113  VAL C  121  1SEE REMARK 8.                      9
HELIX   43   D VAL C  142  VAL C  145  1SEE REMARK 8.                      4
HELIX   44   E ILE C  155  LEU C  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX   45   1 ALA C  182  ARG C  194  1FIRST HELIX OF A/B BARREL         13
HELIX   46   2 TRP C  214  THR C  232  12ND HELIX OF A/B BARREL           19
HELIX   47   3 CYS C  247  GLU C  259  13RD HELIX OF A/B BARREL           13
HELIX   48   4 PHE C  269  ASN C  287  14TH HELIX OF A/B BARREL           19
HELIX   49   F HIS C  298  ASP C  302  1                                   5
HELIX   50   5 PHE C  311  SER C  321  15TH HELIX OF A/B BARREL           11
HELIX   51   6 LYS C  339  ARG C  350  16TH HELIX OF A/B BARREL           12
HELIX   52   7 MET C  387  PHE C  394  17TH HELIX OF A/B BARREL            8
HELIX   53   P GLY C  404  LEU C  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX   54   8 ASN C  413  GLU C  433  18TH HELIX OF A/B BARREL           21
HELIX   55   G LEU C  437  TRP C  451  1                                  15
HELIX   56   H PRO C  453  TRP C  462  1                                  10
HELIX   57  B' TYR C   80  GLU C   93  12ND HELIX - SMALL SUBUNIT         14
HELIX   58   A LYS D   21  TYR D   24  1SEE REMARK 8.                      4
HELIX   59   B ALA D   50  GLU D   60  1SEE REMARK 8.                     11
HELIX   60  BB MET D   77  TYR D   80  1SEE REMARK 8.                      4
HELIX   61   C VAL D  113  VAL D  121  1SEE REMARK 8.                      9
HELIX   62   D VAL D  142  VAL D  145  1SEE REMARK 8.                      4
HELIX   63   E ILE D  155  LEU D  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX   64   1 ALA D  182  ARG D  194  1FIRST HELIX OF A/B BARREL         13
HELIX   65   2 TRP D  214  THR D  232  12ND HELIX OF A/B BARREL           19
HELIX   66   3 CYS D  247  GLU D  259  13RD HELIX OF A/B BARREL           13
HELIX   67   4 PHE D  269  ASN D  287  14TH HELIX OF A/B BARREL           19
HELIX   68   F HIS D  298  ASP D  302  1                                   5
HELIX   69   5 PHE D  311  SER D  321  15TH HELIX OF A/B BARREL           11
HELIX   70   6 LYS D  339  ARG D  350  16TH HELIX OF A/B BARREL           12
HELIX   71   7 MET D  387  PHE D  394  17TH HELIX OF A/B BARREL            8
HELIX   72   P GLY D  404  LEU D  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX   73   8 ASN D  413  GLU D  433  18TH HELIX OF A/B BARREL           21
HELIX   74   G LEU D  437  TRP D  451  1                                  15
HELIX   75   H PRO D  453  TRP D  462  1                                  10
HELIX   76  B' TYR D   80  GLU D   93  12ND HELIX - SMALL SUBUNIT         14
HELIX   77   A LYS E   21  TYR E   24  1SEE REMARK 8.                      4
HELIX   78   B ALA E   50  GLU E   60  1SEE REMARK 8.                     11
HELIX   79  BB MET E   77  TYR E   80  1SEE REMARK 8.                      4
HELIX   80   C VAL E  113  VAL E  121  1SEE REMARK 8.                      9
HELIX   81   D VAL E  142  VAL E  145  1SEE REMARK 8.                      4
HELIX   82   E ILE E  155  LEU E  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX   83   1 ALA E  182  ARG E  194  1FIRST HELIX OF A/B BARREL         13
HELIX   84   2 TRP E  214  THR E  232  12ND HELIX OF A/B BARREL           19
HELIX   85   3 CYS E  247  GLU E  259  13RD HELIX OF A/B BARREL           13
HELIX   86   4 PHE E  269  ASN E  287  14TH HELIX OF A/B BARREL           19
HELIX   87   F HIS E  298  ASP E  302  1                                   5
HELIX   88   5 PHE E  311  SER E  321  15TH HELIX OF A/B BARREL           11
HELIX   89   6 LYS E  339  ARG E  350  16TH HELIX OF A/B BARREL           12
HELIX   90   7 MET E  387  PHE E  394  17TH HELIX OF A/B BARREL            8
HELIX   91   P GLY E  404  LEU E  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX   92   8 ASN E  413  GLU E  433  18TH HELIX OF A/B BARREL           21
HELIX   93   G LEU E  437  TRP E  451  1                                  15
HELIX   94   H PRO E  453  TRP E  462  1                                  10
HELIX   95  B' TYR E   80  GLU E   93  12ND HELIX - SMALL SUBUNIT         14
HELIX   96   A LYS F   21  TYR F   24  1SEE REMARK 8.                      4
HELIX   97   B ALA F   50  GLU F   60  1SEE REMARK 8.                     11
HELIX   98  BB MET F   77  TYR F   80  1SEE REMARK 8.                      4
HELIX   99   C VAL F  113  VAL F  121  1SEE REMARK 8.                      9
HELIX  100   D VAL F  142  VAL F  145  1SEE REMARK 8.                      4
HELIX  101   E ILE F  155  LEU F  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX  102   1 ALA F  182  ARG F  194  1FIRST HELIX OF A/B BARREL         13
HELIX  103   2 TRP F  214  THR F  232  12ND HELIX OF A/B BARREL           19
HELIX  104   3 CYS F  247  GLU F  259  13RD HELIX OF A/B BARREL           13
HELIX  105   4 PHE F  269  ASN F  287  14TH HELIX OF A/B BARREL           19
HELIX  106   F HIS F  298  ASP F  302  1                                   5
HELIX  107   5 PHE F  311  SER F  321  15TH HELIX OF A/B BARREL           11
HELIX  108   6 LYS F  339  ARG F  350  16TH HELIX OF A/B BARREL           12
HELIX  109   7 MET F  387  PHE F  394  17TH HELIX OF A/B BARREL            8
HELIX  110   P GLY F  404  LEU F  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX  111   8 ASN F  413  GLU F  433  18TH HELIX OF A/B BARREL           21
HELIX  112   G LEU F  437  TRP F  451  1                                  15
HELIX  113   H PRO F  453  TRP F  462  1                                  10
HELIX  114  B' TYR F   80  GLU F   93  12ND HELIX - SMALL SUBUNIT         14
HELIX  115   A LYS G   21  TYR G   24  1SEE REMARK 8.                      4
HELIX  116   B ALA G   50  GLU G   60  1SEE REMARK 8.                     11
HELIX  117  BB MET G   77  TYR G   80  1SEE REMARK 8.                      4
HELIX  118   C VAL G  113  VAL G  121  1SEE REMARK 8.                      9
HELIX  119   D VAL G  142  VAL G  145  1SEE REMARK 8.                      4
HELIX  120   E ILE G  155  LEU G  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX  121   1 ALA G  182  ARG G  194  1FIRST HELIX OF A/B BARREL         13
HELIX  122   2 TRP G  214  THR G  232  12ND HELIX OF A/B BARREL           19
HELIX  123   3 CYS G  247  GLU G  259  13RD HELIX OF A/B BARREL           13
HELIX  124   4 PHE G  269  ASN G  287  14TH HELIX OF A/B BARREL           19
HELIX  125   F HIS G  298  ASP G  302  1                                   5
HELIX  126   5 PHE G  311  SER G  321  15TH HELIX OF A/B BARREL           11
HELIX  127   6 LYS G  339  ARG G  350  16TH HELIX OF A/B BARREL           12
HELIX  128   7 MET G  387  PHE G  394  17TH HELIX OF A/B BARREL            8
HELIX  129   P GLY G  404  LEU G  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX  130   8 ASN G  413  GLU G  433  18TH HELIX OF A/B BARREL           21
HELIX  131   G LEU G  437  TRP G  451  1                                  15
HELIX  132   H PRO G  453  TRP G  462  1                                  10
HELIX  133  B' TYR G   80  GLU G   93  12ND HELIX - SMALL SUBUNIT         14
HELIX  134   A LYS H   21  TYR H   24  1SEE REMARK 8.                      4
HELIX  135   B ALA H   50  GLU H   60  1SEE REMARK 8.                     11
HELIX  136  BB MET H   77  TYR H   80  1SEE REMARK 8.                      4
HELIX  137   C VAL H  113  VAL H  121  1SEE REMARK 8.                      9
HELIX  138   D VAL H  142  VAL H  145  1SEE REMARK 8.                      4
HELIX  139   E ILE H  155  LEU H  162  1LINKS N-TERM & C-TERM DOMAINS      8
HELIX  140   1 ALA H  182  ARG H  194  1FIRST HELIX OF A/B BARREL         13
HELIX  141   2 TRP H  214  THR H  232  12ND HELIX OF A/B BARREL           19
HELIX  142   3 CYS H  247  GLU H  259  13RD HELIX OF A/B BARREL           13
HELIX  143   4 PHE H  269  ASN H  287  14TH HELIX OF A/B BARREL           19
HELIX  144   F HIS H  298  ASP H  302  1                                   5
HELIX  145   5 PHE H  311  SER H  321  15TH HELIX OF A/B BARREL           11
HELIX  146   6 LYS H  339  ARG H  350  16TH HELIX OF A/B BARREL           12
HELIX  147   7 MET H  387  PHE H  394  17TH HELIX OF A/B BARREL            8
HELIX  148   P GLY H  404  LEU H  407  1P FOR PHOSPHATE BINDING HELIX      4
HELIX  149   8 ASN H  413  GLU H  433  18TH HELIX OF A/B BARREL           21
HELIX  150   G LEU H  437  TRP H  451  1                                  15
HELIX  151   H PRO H  453  TRP H  462  1                                  10
HELIX  152  B' TYR H   80  GLU H   93  12ND HELIX - SMALL SUBUNIT         14
SHEET    1 LN1 4 LYS A  83  PRO A  89  0
SHEET    2 LN1 4 SER A  96  TYR A 103 -1
SHEET    3 LN1 4 LEU A  36  PRO A  44 -1
SHEET    4 LN1 4 ILE A 130  ARG A 139 -1
SHEET    1 LC1 9 MET A 169  GLY A 171  0
SHEET    2 LC1 9 THR A 200  ASP A 202  1
SHEET    3 LC1 9 LEU A 240  ASN A 241  1
SHEET    4 LC1 9 ILE A 264  ASP A 268  1
SHEET    5 LC1 9 LEU A 290  HIS A 294  1
SHEET    6 LC1 9 HIS A 325  HIS A 327  1
SHEET    7 LC1 9 LEU A 375  SER A 379  1
SHEET    8 LC1 9 VAL A 399  GLN A 401  1
SHEET    9 LC1 9 MET A 169  GLY A 171  1
SHEET    1 SS1 4 THR M  68  MET M  69  0
SHEET    2 SS1 4 HIS M  39  ASN M  45 -1
SHEET    3 SS1 4 TYR M  98  ASP M 105 -1
SHEET    4 SS1 4 CYS M 110  HIS M 118 -1
SHEET    1 LN2 4 LYS B  83  PRO B  89  0
SHEET    2 LN2 4 SER B  96  TYR B 103 -1
SHEET    3 LN2 4 LEU B  36  PRO B  44 -1
SHEET    4 LN2 4 ILE B 130  ARG B 139 -1
SHEET    1 LC2 9 MET B 169  GLY B 171  0
SHEET    2 LC2 9 THR B 200  ASP B 202  1
SHEET    3 LC2 9 LEU B 240  ASN B 241  1
SHEET    4 LC2 9 ILE B 264  ASP B 268  1
SHEET    5 LC2 9 LEU B 290  HIS B 294  1
SHEET    6 LC2 9 HIS B 325  HIS B 327  1
SHEET    7 LC2 9 LEU B 375  SER B 379  1
SHEET    8 LC2 9 VAL B 399  GLN B 401  1
SHEET    9 LC2 9 MET B 169  GLY B 171  1
SHEET    1 SS2 4 THR I  68  MET I  69  0
SHEET    2 SS2 4 HIS I  39  ASN I  45 -1
SHEET    3 SS2 4 TYR I  98  ASP I 105 -1
SHEET    4 SS2 4 CYS I 110  HIS I 118 -1
SHEET    1 LN3 4 LYS C  83  PRO C  89  0
SHEET    2 LN3 4 SER C  96  TYR C 103 -1
SHEET    3 LN3 4 LEU C  36  PRO C  44 -1
SHEET    4 LN3 4 ILE C 130  ARG C 139 -1
SHEET    1 LC3 9 MET C 169  GLY C 171  0
SHEET    2 LC3 9 THR C 200  ASP C 202  1
SHEET    3 LC3 9 LEU C 240  ASN C 241  1
SHEET    4 LC3 9 ILE C 264  ASP C 268  1
SHEET    5 LC3 9 LEU C 290  HIS C 294  1
SHEET    6 LC3 9 HIS C 325  HIS C 327  1
SHEET    7 LC3 9 LEU C 375  SER C 379  1
SHEET    8 LC3 9 VAL C 399  GLN C 401  1
SHEET    9 LC3 9 MET C 169  GLY C 171  1
SHEET    1 SS3 4 THR N  68  MET N  69  0
SHEET    2 SS3 4 HIS N  39  ASN N  45 -1
SHEET    3 SS3 4 TYR N  98  ASP N 105 -1
SHEET    4 SS3 4 CYS N 110  HIS N 118 -1
SHEET    1 LN4 4 LYS D  83  PRO D  89  0
SHEET    2 LN4 4 SER D  96  TYR D 103 -1
SHEET    3 LN4 4 LEU D  36  PRO D  44 -1
SHEET    4 LN4 4 ILE D 130  ARG D 139 -1
SHEET    1 LC4 9 MET D 169  GLY D 171  0
SHEET    2 LC4 9 THR D 200  ASP D 202  1
SHEET    3 LC4 9 LEU D 240  ASN D 241  1
SHEET    4 LC4 9 ILE D 264  ASP D 268  1
SHEET    5 LC4 9 LEU D 290  HIS D 294  1
SHEET    6 LC4 9 HIS D 325  HIS D 327  1
SHEET    7 LC4 9 LEU D 375  SER D 379  1
SHEET    8 LC4 9 VAL D 399  GLN D 401  1
SHEET    9 LC4 9 MET D 169  GLY D 171  1
SHEET    1 SS4 4 THR J  68  MET J  69  0
SHEET    2 SS4 4 HIS J  39  ASN J  45 -1
SHEET    3 SS4 4 TYR J  98  ASP J 105 -1
SHEET    4 SS4 4 CYS J 110  HIS J 118 -1
SHEET    1 LN5 4 LYS E  83  PRO E  89  0
SHEET    2 LN5 4 SER E  96  TYR E 103 -1
SHEET    3 LN5 4 LEU E  36  PRO E  44 -1
SHEET    4 LN5 4 ILE E 130  ARG E 139 -1
SHEET    1 LC5 9 MET E 169  GLY E 171  0
SHEET    2 LC5 9 THR E 200  ASP E 202  1
SHEET    3 LC5 9 LEU E 240  ASN E 241  1
SHEET    4 LC5 9 ILE E 264  ASP E 268  1
SHEET    5 LC5 9 LEU E 290  HIS E 294  1
SHEET    6 LC5 9 HIS E 325  HIS E 327  1
SHEET    7 LC5 9 LEU E 375  SER E 379  1
SHEET    8 LC5 9 VAL E 399  GLN E 401  1
SHEET    9 LC5 9 MET E 169  GLY E 171  1
SHEET    1 SS5 4 THR O  68  MET O  69  0
SHEET    2 SS5 4 HIS O  39  ASN O  45 -1
SHEET    3 SS5 4 TYR O  98  ASP O 105 -1
SHEET    4 SS5 4 CYS O 110  HIS O 118 -1
SHEET    1 LN6 4 LYS F  83  PRO F  89  0
SHEET    2 LN6 4 SER F  96  TYR F 103 -1
SHEET    3 LN6 4 LEU F  36  PRO F  44 -1
SHEET    4 LN6 4 ILE F 130  ARG F 139 -1
SHEET    1 LC6 9 MET F 169  GLY F 171  0
SHEET    2 LC6 9 THR F 200  ASP F 202  1
SHEET    3 LC6 9 LEU F 240  ASN F 241  1
SHEET    4 LC6 9 ILE F 264  ASP F 268  1
SHEET    5 LC6 9 LEU F 290  HIS F 294  1
SHEET    6 LC6 9 HIS F 325  HIS F 327  1
SHEET    7 LC6 9 LEU F 375  SER F 379  1
SHEET    8 LC6 9 VAL F 399  GLN F 401  1
SHEET    9 LC6 9 MET F 169  GLY F 171  1
SHEET    1 SS6 4 THR K  68  MET K  69  0
SHEET    2 SS6 4 HIS K  39  ASN K  45 -1
SHEET    3 SS6 4 TYR K  98  ASP K 105 -1
SHEET    4 SS6 4 CYS K 110  HIS K 118 -1
SHEET    1 LN7 4 LYS G  83  PRO G  89  0
SHEET    2 LN7 4 SER G  96  TYR G 103 -1
SHEET    3 LN7 4 LEU G  36  PRO G  44 -1
SHEET    4 LN7 4 ILE G 130  ARG G 139 -1
SHEET    1 LC7 9 MET G 169  GLY G 171  0
SHEET    2 LC7 9 THR G 200  ASP G 202  1
SHEET    3 LC7 9 LEU G 240  ASN G 241  1
SHEET    4 LC7 9 ILE G 264  ASP G 268  1
SHEET    5 LC7 9 LEU G 290  HIS G 294  1
SHEET    6 LC7 9 HIS G 325  HIS G 327  1
SHEET    7 LC7 9 LEU G 375  SER G 379  1
SHEET    8 LC7 9 VAL G 399  GLN G 401  1
SHEET    9 LC7 9 MET G 169  GLY G 171  1
SHEET    1 SS7 4 THR P  68  MET P  69  0
SHEET    2 SS7 4 HIS P  39  ASN P  45 -1
SHEET    3 SS7 4 TYR P  98  ASP P 105 -1
SHEET    4 SS7 4 CYS P 110  HIS P 118 -1
SHEET    1 LN8 4 LYS H  83  PRO H  89  0
SHEET    2 LN8 4 SER H  96  TYR H 103 -1
SHEET    3 LN8 4 LEU H  36  PRO H  44 -1
SHEET    4 LN8 4 ILE H 130  ARG H 139 -1
SHEET    1 LC8 9 MET H 169  GLY H 171  0
SHEET    2 LC8 9 THR H 200  ASP H 202  1
SHEET    3 LC8 9 LEU H 240  ASN H 241  1
SHEET    4 LC8 9 ILE H 264  ASP H 268  1
SHEET    5 LC8 9 LEU H 290  HIS H 294  1
SHEET    6 LC8 9 HIS H 325  HIS H 327  1
SHEET    7 LC8 9 LEU H 375  SER H 379  1
SHEET    8 LC8 9 VAL H 399  GLN H 401  1
SHEET    9 LC8 9 MET H 169  GLY H 171  1
SHEET    1 SS8 4 THR L  68  MET L  69  0
SHEET    2 SS8 4 HIS L  39  ASN L  45 -1
SHEET    3 SS8 4 TYR L  98  ASP L 105 -1
SHEET    4 SS8 4 CYS L 110  HIS L 118 -1
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.19
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.18
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.18
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.23
LINK         NZ  LYS A 201                 C   FMT A 478     1555   1555  1.45
LINK         NZ  LYS B 201                 C   FMT B 478     1555   1555  1.45
LINK         NZ  LYS C 201                 C   FMT C 478     1555   1555  1.45
LINK         NZ  LYS D 201                 C   FMT D 478     1555   1555  1.45
LINK         NZ  LYS E 201                 C   FMT E 478     1555   1555  1.45
LINK         NZ  LYS F 201                 C   FMT F 478     1555   1555  1.45
LINK         NZ  LYS G 201                 C   FMT G 478     1555   1555  1.45
LINK         NZ  LYS H 201                 C   FMT H 478     1555   1555  1.45
LINK        MG    MG A 477                 O1  FMT A 478     1555   1555  3.13
LINK        MG    MG A 477                 O2  FMT A 478     1555   1555  2.37
LINK        MG    MG A 477                 O2  CAP A 476     1555   1555  2.39
LINK        MG    MG A 477                 OE1 GLU A 204     1555   1555  2.34
LINK        MG    MG A 477                 O3  CAP A 476     1555   1555  2.36
LINK        MG    MG A 477                 O7  CAP A 476     1555   1555  2.41
LINK        MG    MG A 477                 OD1 ASP A 203     1555   1555  2.33
LINK        MG    MG B 477                 O3  CAP B 476     1555   1555  2.36
LINK        MG    MG B 477                 O7  CAP B 476     1555   1555  2.42
LINK        MG    MG B 477                 O1  FMT B 478     1555   1555  3.13
LINK        MG    MG B 477                 O2  FMT B 478     1555   1555  2.37
LINK        MG    MG B 477                 O2  CAP B 476     1555   1555  2.39
LINK        MG    MG B 477                 OE1 GLU B 204     1555   1555  2.34
LINK        MG    MG B 477                 OD1 ASP B 203     1555   1555  2.33
LINK        MG    MG C 477                 OD1 ASP C 203     1555   1555  2.33
LINK        MG    MG C 477                 OE1 GLU C 204     1555   1555  2.34
LINK        MG    MG C 477                 O7  CAP C 476     1555   1555  2.42
LINK        MG    MG C 477                 O2  FMT C 478     1555   1555  2.37
LINK        MG    MG C 477                 O3  CAP C 476     1555   1555  2.36
LINK        MG    MG C 477                 O2  CAP C 476     1555   1555  2.39
LINK        MG    MG C 477                 O1  FMT C 478     1555   1555  3.13
LINK        MG    MG D 477                 O3  CAP D 476     1555   1555  2.36
LINK        MG    MG D 477                 O1  FMT D 478     1555   1555  3.13
LINK        MG    MG D 477                 O2  CAP D 476     1555   1555  2.39
LINK        MG    MG D 477                 O2  FMT D 478     1555   1555  2.37
LINK        MG    MG D 477                 OE1 GLU D 204     1555   1555  2.34
LINK        MG    MG D 477                 O7  CAP D 476     1555   1555  2.42
LINK        MG    MG D 477                 OD1 ASP D 203     1555   1555  2.33
LINK        MG    MG E 477                 O2  FMT E 478     1555   1555  2.37
LINK        MG    MG E 477                 OE1 GLU E 204     1555   1555  2.34
LINK        MG    MG E 477                 OD1 ASP E 203     1555   1555  2.33
LINK        MG    MG E 477                 O1  FMT E 478     1555   1555  3.13
LINK        MG    MG E 477                 O2  CAP E 476     1555   1555  2.39
LINK        MG    MG E 477                 O7  CAP E 476     1555   1555  2.41
LINK        MG    MG E 477                 O3  CAP E 476     1555   1555  2.36
LINK        MG    MG F 477                 O2  FMT F 478     1555   1555  2.37
LINK        MG    MG F 477                 O1  FMT F 478     1555   1555  3.13
LINK        MG    MG F 477                 O3  CAP F 476     1555   1555  2.36
LINK        MG    MG F 477                 OD1 ASP F 203     1555   1555  2.33
LINK        MG    MG F 477                 O2  CAP F 476     1555   1555  2.39
LINK        MG    MG F 477                 O7  CAP F 476     1555   1555  2.41
LINK        MG    MG F 477                 OE1 GLU F 204     1555   1555  2.34
LINK        MG    MG G 477                 OE1 GLU G 204     1555   1555  2.34
LINK        MG    MG G 477                 O2  FMT G 478     1555   1555  2.37
LINK        MG    MG G 477                 O1  FMT G 478     1555   1555  3.13
LINK        MG    MG G 477                 O3  CAP G 476     1555   1555  2.36
LINK        MG    MG G 477                 O2  CAP G 476     1555   1555  2.39
LINK        MG    MG G 477                 OD1 ASP G 203     1555   1555  2.33
LINK        MG    MG G 477                 O7  CAP G 476     1555   1555  2.41
LINK        MG    MG H 477                 O7  CAP H 476     1555   1555  2.41
LINK        MG    MG H 477                 OD1 ASP H 203     1555   1555  2.33
LINK        MG    MG H 477                 O2  CAP H 476     1555   1555  2.39
LINK        MG    MG H 477                 O2  FMT H 478     1555   1555  2.37
LINK        MG    MG H 477                 O1  FMT H 478     1555   1555  3.13
LINK        MG    MG H 477                 O3  CAP H 476     1555   1555  2.36
LINK        MG    MG H 477                 OE1 GLU H 204     1555   1555  2.34
CISPEP   1 LYS A  175    PRO A  176          0        -4.06
CISPEP   2 LYS B  175    PRO B  176          0        -4.03
CISPEP   3 LYS C  175    PRO C  176          0        -4.16
CISPEP   4 LYS D  175    PRO D  176          0        -4.07
CISPEP   5 LYS E  175    PRO E  176          0        -4.05
CISPEP   6 LYS F  175    PRO F  176          0        -4.00
CISPEP   7 LYS G  175    PRO G  176          0        -4.05
CISPEP   8 LYS H  175    PRO H  176          0        -4.05
SITE     1  MG  3 LYS A 201  ASP A 203  GLU A 204
SITE     1  1P  4 PHE M  65  GLY A 404  GLY A 381  GLY A 403
SITE     1  2P  2 ARG A 295  HIS A 327
SITE     1 CAB  4  MG A 477  LYS A 201  HIS A 294  SER A 379
SITE     1 MG2  3 LYS B 201  ASP B 203  GLU B 204
SITE     1 1P2  4 PHE I  65  GLY B 404  GLY B 381  GLY B 403
SITE     1 2P2  2 ARG B 295  HIS B 327
SITE     1 CA2  4  MG B 477  LYS B 201  HIS B 294  SER B 379
SITE     1 MG3  3 LYS C 201  ASP C 203  GLU C 204
SITE     1 1P3  4 PHE N  65  GLY C 404  GLY C 381  GLY C 403
SITE     1 2P3  2 ARG C 295  HIS C 327
SITE     1 CA3  4  MG C 477  LYS C 201  HIS C 294  SER C 379
SITE     1 MG4  3 LYS D 201  ASP D 203  GLU D 204
SITE     1 1P4  4 PHE J  65  GLY D 404  GLY D 381  GLY D 403
SITE     1 2P4  2 ARG D 295  HIS D 327
SITE     1 CA4  4  MG D 477  LYS D 201  HIS D 294  SER D 379
SITE     1 MG5  3 LYS E 201  ASP E 203  GLU E 204
SITE     1 1P5  4 PHE O  65  GLY E 404  GLY E 381  GLY E 403
SITE     1 2P5  2 ARG E 295  HIS E 327
SITE     1 CA5  4  MG E 477  LYS E 201  HIS E 294  SER E 379
SITE     1 MG6  3 LYS F 201  ASP F 203  GLU F 204
SITE     1 1P6  4 PHE K  65  GLY F 404  GLY F 381  GLY F 403
SITE     1 2P6  2 ARG F 295  HIS F 327
SITE     1 CA6  4  MG F 477  LYS F 201  HIS F 294  SER F 379
SITE     1 MG7  3 LYS G 201  ASP G 203  GLU G 204
SITE     1 1P7  4 PHE P  65  GLY G 404  GLY G 381  GLY G 403
SITE     1 2P7  2 ARG G 295  HIS G 327
SITE     1 CA7  4  MG G 477  LYS G 201  HIS G 294  SER G 379
SITE     1 MG8  3 LYS H 201  ASP H 203  GLU H 204
SITE     1 1P8  4 PHE L  65  GLY H 404  GLY H 381  GLY H 403
SITE     1 2P8  2 ARG H 295  HIS H 327
SITE     1 CA8  4  MG H 477  LYS H 201  HIS H 294  SER H 379
SITE     1 AC1 23 THR A 173  LYS A 175  LYS A 177  HIS A 294
SITE     2 AC1 23 ARG A 295  HIS A 327  LYS A 334  LEU A 335
SITE     3 AC1 23 SER A 379  GLY A 380  GLY A 381  GLY A 403
SITE     4 AC1 23 GLY A 404  THR B  65  TRP B  66  ASN B 123
SITE     5 AC1 23 HOH A 514  HOH A 515  HOH A 520  HOH A 521
SITE     6 AC1 23 HOH A 569  HOH A 570  HOH A 571
SITE     1 AC2 18 THR A  65  TRP A  66  ASN A 123  THR B 173
SITE     2 AC2 18 LYS B 175  LYS B 177  HIS B 294  ARG B 295
SITE     3 AC2 18 HIS B 327  LYS B 334  LEU B 335  SER B 379
SITE     4 AC2 18 GLY B 380  GLY B 381  GLY B 403  GLY B 404
SITE     5 AC2 18 HOH A 502  HOH A 503
SITE     1 AC3 16 THR C 173  LYS C 175  LYS C 177  HIS C 294
SITE     2 AC3 16 ARG C 295  HIS C 327  LYS C 334  LEU C 335
SITE     3 AC3 16 SER C 379  GLY C 380  GLY C 381  GLY C 403
SITE     4 AC3 16 GLY C 404  THR D  65  TRP D  66  ASN D 123
SITE     1 AC4 16 THR C  65  TRP C  66  ASN C 123  THR D 173
SITE     2 AC4 16 LYS D 175  LYS D 177  HIS D 294  ARG D 295
SITE     3 AC4 16 HIS D 327  LYS D 334  LEU D 335  SER D 379
SITE     4 AC4 16 GLY D 380  GLY D 381  GLY D 403  GLY D 404
SITE     1 AC5 16 THR G  65  TRP G  66  ASN G 123  THR H 173
SITE     2 AC5 16 LYS H 175  LYS H 177  HIS H 294  ARG H 295
SITE     3 AC5 16 HIS H 327  LYS H 334  LEU H 335  SER H 379
SITE     4 AC5 16 GLY H 380  GLY H 381  GLY H 403  GLY H 404
SITE     1 AC6 16 THR G 173  LYS G 175  LYS G 177  HIS G 294
SITE     2 AC6 16 ARG G 295  HIS G 327  LYS G 334  LEU G 335
SITE     3 AC6 16 SER G 379  GLY G 380  GLY G 381  GLY G 403
SITE     4 AC6 16 GLY G 404  THR H  65  TRP H  66  ASN H 123
SITE     1 AC7 16 THR E  65  TRP E  66  ASN E 123  THR F 173
SITE     2 AC7 16 LYS F 175  LYS F 177  HIS F 294  ARG F 295
SITE     3 AC7 16 HIS F 327  LYS F 334  LEU F 335  SER F 379
SITE     4 AC7 16 GLY F 380  GLY F 381  GLY F 403  GLY F 404
SITE     1 AC8 16 THR E 173  LYS E 175  LYS E 177  HIS E 294
SITE     2 AC8 16 ARG E 295  HIS E 327  LYS E 334  LEU E 335
SITE     3 AC8 16 SER E 379  GLY E 380  GLY E 381  GLY E 403
SITE     4 AC8 16 GLY E 404  THR F  65  TRP F  66  ASN F 123
SITE     1 AC9  6 LYS A 201  ASP A 202  ASP A 203  GLU A 204
SITE     2 AC9  6 HIS A 294  HIS A 327
SITE     1 AD1  6 LYS D 201  ASP D 202  ASP D 203  GLU D 204
SITE     2 AD1  6 HIS D 294  HIS D 327
SITE     1 AD2  6 LYS E 201  ASP E 202  ASP E 203  GLU E 204
SITE     2 AD2  6 HIS E 294  HIS E 327
SITE     1 AD3  6 LYS F 201  ASP F 202  ASP F 203  GLU F 204
SITE     2 AD3  6 HIS F 294  HIS F 327
SITE     1 AD4  6 LYS H 201  ASP H 202  ASP H 203  GLU H 204
SITE     2 AD4  6 HIS H 294  HIS H 327
SITE     1 AD5  6 LYS G 201  ASP G 202  ASP G 203  GLU G 204
SITE     2 AD5  6 HIS G 294  HIS G 327
SITE     1 AD6  6 LYS C 201  ASP C 202  ASP C 203  GLU C 204
SITE     2 AD6  6 HIS C 294  HIS C 327
SITE     1 AD7  6 LYS B 201  ASP B 202  ASP B 203  GLU B 204
SITE     2 AD7  6 HIS B 294  HIS B 327
SITE     1 AD8  2 ASP A 203  GLU A 204
SITE     1 AD9  2 ASP B 203  GLU B 204
SITE     1 AE1  2 ASP C 203  GLU C 204
SITE     1 AE2  2 ASP D 203  GLU D 204
SITE     1 AE3  2 ASP E 203  GLU E 204
SITE     1 AE4  2 ASP F 203  GLU F 204
SITE     1 AE5  2 ASP G 203  GLU G 204
SITE     1 AE6  2 ASP H 203  GLU H 204
CRYST1  223.900  111.900  199.700  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      0.004466  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008937  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005008        0.00000
MTRIX1   1  0.055254  0.991591  0.117024       58.51700    1
MTRIX2   1  0.991747 -0.068084  0.108639      -60.77910    1
MTRIX3   1  0.115693  0.110056 -0.987169      -12.31830    1
MTRIX1   2 -0.001556  0.994481  0.104910       63.24410    1
MTRIX2   2 -0.993326  0.010562 -0.114852      104.72470    1
MTRIX3   2 -0.115326 -0.104388  0.987827       11.96200    1
MTRIX1   3  0.998390 -0.056422  0.005795        1.35870    1
MTRIX2   3 -0.056413 -0.998406 -0.001652       47.27970    1
MTRIX3   3  0.005879  0.001323 -0.999982       -0.77360    1
MTRIX1   4 -0.999944  0.000591 -0.010574      168.35741    1
MTRIX2   4  0.001717 -0.976187 -0.216926       41.89850    1
MTRIX3   4 -0.010451 -0.216932  0.976131        5.47850    1
MTRIX1   5 -0.055113 -0.992904 -0.105381      109.87600    1
MTRIX2   5 -0.993265  0.043745  0.107292      104.02560    1
MTRIX3   5 -0.101920  0.110584 -0.988627        5.96800    1
MTRIX1   6 -0.000233 -0.993280 -0.115738      105.29090    1
MTRIX2   6  0.994670  0.011703 -0.102440      -62.72860    1
MTRIX3   6  0.103106 -0.115145  0.987983       -6.23160    1
MTRIX1   7 -0.998513  0.054364  0.004006      167.12070    1
MTRIX2   7  0.053928  0.974438  0.218086       -3.88990    1
MTRIX3   7  0.007953  0.217978 -0.975921       -5.57330    1
      
PROCHECK
Go to PROCHECK summary
 References