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PDBsum entry 4hhh

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Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
4hhh
Jmol
Contents
Protein chains
458 a.a.
123 a.a.
Ligands
RUB ×4
Waters ×789
HEADER    LYASE                                   09-OCT-12   4HHH
TITLE     STRUCTURE OF PISUM SATIVUM RUBISCO
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT;
COMPND   5 EC: 4.1.1.39;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN;
COMPND   8 CHAIN: S, T, U, V
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;
SOURCE   3 ORGANISM_COMMON: GARDEN PEA,PEAS;
SOURCE   4 ORGANISM_TAXID: 3888;
SOURCE   5 TISSUE: LEAF;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: PISUM SATIVUM;
SOURCE   8 ORGANISM_COMMON: GARDEN PEA,PEAS;
SOURCE   9 ORGANISM_TAXID: 3888;
SOURCE  10 TISSUE: LEAF
KEYWDS    RUBISCO, RIBULOSE-1,5-BISPHOSPHATE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.C.LOEWEN,A.L.DIDYCHUK,J.SWITALA,M.C.LOEWEN
REVDAT   3   23-JAN-13 4HHH    1       JRNL
REVDAT   2   09-JAN-13 4HHH    1       JRNL
REVDAT   1   31-OCT-12 4HHH    0
JRNL        AUTH   P.C.LOEWEN,A.L.DIDYCHUK,J.SWITALA,R.PEREZ-LUQUE,I.FITA,
JRNL        AUTH 2 M.C.LOEWEN
JRNL        TITL   STRUCTURE OF PISUM SATIVUM RUBISCO WITH BOUND RIBULOSE
JRNL        TITL 2 1,5-BISPHOSPHATE.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  69    10 2013
JRNL        REFN                   ESSN 1744-3091
JRNL        PMID   23295478
JRNL        DOI    10.1107/S1744309112047549
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.6.0117
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 109.95
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0
REMARK   3   NUMBER OF REFLECTIONS             : 116023
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201
REMARK   3   R VALUE            (WORKING SET) : 0.197
REMARK   3   FREE R VALUE                     : 0.279
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 5993
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7714
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.06
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950
REMARK   3   BIN FREE R VALUE SET COUNT          : 414
REMARK   3   BIN FREE R VALUE                    : 0.2920
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 18528
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 72
REMARK   3   SOLVENT ATOMS            : 789
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.65
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -6.73000
REMARK   3    B22 (A**2) : 0.84000
REMARK   3    B33 (A**2) : 5.89000
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.076
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.057
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.102
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.854
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.734
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19441 ; 0.020 ; 0.020
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 26445 ; 2.446 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2424 ; 9.035 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   906 ;35.757 ;22.925
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3245 ;21.867 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   154 ;22.363 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2812 ; 0.160 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14996 ; 0.013 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 12
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     12       A     469      0
REMARK   3           2     B     12       B     469      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : A C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     12       A     469      0
REMARK   3           2     C     12       C     469      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : A D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     12       A     469      0
REMARK   3           2     D     12       D     469      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 4
REMARK   3     CHAIN NAMES                    : B C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B     12       B     469      0
REMARK   3           2     C     12       C     469      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 5
REMARK   3     CHAIN NAMES                    : B D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B     12       B     469      0
REMARK   3           2     D     12       D     469      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 6
REMARK   3     CHAIN NAMES                    : C D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C     12       C     469      0
REMARK   3           2     D     12       D     469      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 7
REMARK   3     CHAIN NAMES                    : S T
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     S      1       S     123      0
REMARK   3           2     T      1       T     123      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 8
REMARK   3     CHAIN NAMES                    : S U
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     S      1       S     123      0
REMARK   3           2     U      1       U     123      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 9
REMARK   3     CHAIN NAMES                    : S V
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     S      1       S     123      0
REMARK   3           2     V      1       V     123      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 10
REMARK   3     CHAIN NAMES                    : T U
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     T      1       T     123      0
REMARK   3           2     U      1       U     123      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 11
REMARK   3     CHAIN NAMES                    : T V
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     T      1       T     123      0
REMARK   3           2     V      1       V     123      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 12
REMARK   3     CHAIN NAMES                    : U V
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     U      1       U     123      0
REMARK   3           2     V      1       V     123      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  TWIN DETAILS
REMARK   3   NUMBER OF TWIN DOMAINS  : 2
REMARK   3      TWIN DOMAIN   : 1
REMARK   3      TWIN OPERATOR : H, K, L
REMARK   3      TWIN FRACTION : 0.580
REMARK   3      TWIN DOMAIN   : 2
REMARK   3      TWIN OPERATOR : K, H, -L
REMARK   3      TWIN FRACTION : 0.420
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK   3  THE INPUT
REMARK   4
REMARK   4 4HHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB075471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CLSI
REMARK 200  BEAMLINE                       : 08ID-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI (111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 116075
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 109.950
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1
REMARK 200  DATA REDUNDANCY                : 2.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.22200
REMARK 200   FOR THE DATA SET  : 3.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.38700
REMARK 200  R SYM FOR SHELL            (I) : 0.38700
REMARK 200   FOR SHELL         : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX MR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG6000, 0.1 M HEPES, PH 7.0,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,-Y,-Z+1/2
REMARK 290       4555   -X+1/2,-Y,Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       54.89500
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.72000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       54.89500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      100.72000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 111960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 118930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -448.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, T, S, C, D, V, U
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     1
REMARK 465     SER A     2
REMARK 465     PRO A     3
REMARK 465     GLN A     4
REMARK 465     THR A     5
REMARK 465     GLU A     6
REMARK 465     THR A     7
REMARK 465     LYS A     8
REMARK 465     ALA A     9
REMARK 465     LYS A    10
REMARK 465     VAL A    11
REMARK 465     PRO A   470
REMARK 465     ALA A   471
REMARK 465     MET A   472
REMARK 465     ASP A   473
REMARK 465     THR A   474
REMARK 465     LEU A   475
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
REMARK 465     GLN B     4
REMARK 465     THR B     5
REMARK 465     GLU B     6
REMARK 465     THR B     7
REMARK 465     LYS B     8
REMARK 465     ALA B     9
REMARK 465     LYS B    10
REMARK 465     VAL B    11
REMARK 465     PRO B   470
REMARK 465     ALA B   471
REMARK 465     MET B   472
REMARK 465     ASP B   473
REMARK 465     THR B   474
REMARK 465     LEU B   475
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     PRO C     3
REMARK 465     GLN C     4
REMARK 465     THR C     5
REMARK 465     GLU C     6
REMARK 465     THR C     7
REMARK 465     LYS C     8
REMARK 465     ALA C     9
REMARK 465     LYS C    10
REMARK 465     VAL C    11
REMARK 465     PRO C   470
REMARK 465     ALA C   471
REMARK 465     MET C   472
REMARK 465     ASP C   473
REMARK 465     THR C   474
REMARK 465     LEU C   475
REMARK 465     MET D     1
REMARK 465     SER D     2
REMARK 465     PRO D     3
REMARK 465     GLN D     4
REMARK 465     THR D     5
REMARK 465     GLU D     6
REMARK 465     THR D     7
REMARK 465     LYS D     8
REMARK 465     ALA D     9
REMARK 465     LYS D    10
REMARK 465     VAL D    11
REMARK 465     PRO D   470
REMARK 465     ALA D   471
REMARK 465     MET D   472
REMARK 465     ASP D   473
REMARK 465     THR D   474
REMARK 465     LEU D   475
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   NZ   LYS C   201     NE2  HIS C   294              1.70
REMARK 500   OH   TYR T    94     O    HOH T   228              1.79
REMARK 500   OE1  GLU D   234     O    HOH D   667              1.84
REMARK 500   OD2  ASP C   367     O    HOH C   732              1.87
REMARK 500   NZ   LYS A   252     OD1  ASP D   286              1.88
REMARK 500   O    HOH A   635     O    HOH A   759              1.88
REMARK 500   O    HOH C   650     O    HOH C   737              1.92
REMARK 500   OD1  ASN B   123     O    HOH B   716              1.96
REMARK 500   OD1  ASP D   347     O    HOH D   646              1.97
REMARK 500   NZ   LYS D   201     NE2  HIS D   294              1.98
REMARK 500   O    HOH C   696     O    HOH T   222              1.98
REMARK 500   O    HOH A   652     O    HOH A   730              1.98
REMARK 500   O    HOH T   209     O    HOH T   235              1.99
REMARK 500   O    HOH C   701     O    HOH D   611              1.99
REMARK 500   OE1  GLU D   340     O    HOH D   712              2.00
REMARK 500   O    TYR B   353     O    HOH B   707              2.02
REMARK 500   O    HOH A   610     O    HOH D   669              2.03
REMARK 500   O    HOH B   685     O    HOH B   720              2.03
REMARK 500   OH   TYR S    62     O    HOH S   209              2.05
REMARK 500   OH   TYR D   190     OE1  GLU D   231              2.05
REMARK 500   OD2  ASP A   351     O    HOH A   731              2.05
REMARK 500   N    LYS A   305     O    HOH A   753              2.06
REMARK 500   NE2  GLN A    96     OD1  ASN A   306              2.06
REMARK 500   OE2  GLU V    13     O    HOH V   212              2.07
REMARK 500   O    HOH A   728     O    HOH A   729              2.07
REMARK 500   O    ALA D   328     O    HOH D   734              2.07
REMARK 500   O    HOH A   708     O    HOH D   648              2.07
REMARK 500   O    SER D   379     O    HOH D   730              2.08
REMARK 500   OD1  ASN A   205     O    HOH A   749              2.08
REMARK 500   NH1  ARG D   285     O    HOH D   669              2.09
REMARK 500   OH   TYR D   100     O    HOH D   685              2.09
REMARK 500   OE1  GLN U    25     O    HOH U   221              2.10
REMARK 500   O    HOH D   665     O    HOH U   207              2.10
REMARK 500   NZ   LYS V    11     O    HOH V   238              2.10
REMARK 500   OE1  GLN B   304     O    HOH B   708              2.10
REMARK 500   O    GLY A   179     NE2  GLN V   109              2.11
REMARK 500   O4P  RUB C   501     O    HOH C   703              2.12
REMARK 500   O    HOH C   609     O    HOH C   708              2.12
REMARK 500   OH   TYR B   185     O    HOH B   703              2.12
REMARK 500   O    GLU B   338     OG1  THR B   342              2.12
REMARK 500   O    HOH C   640     O    HOH C   700              2.12
REMARK 500   OD1  ASP B   160     O    HOH B   647              2.13
REMARK 500   O    HOH D   742     O    HOH D   743              2.13
REMARK 500   OH   TYR T    32     O    HOH T   243              2.14
REMARK 500   O    MET V    69     O    HOH V   209              2.14
REMARK 500   OD1  ASP C   286     NZ   LYS D   252              2.15
REMARK 500   OD1  ASP D   160     OH   TYR D   165              2.15
REMARK 500   O    HOH D   691     O    HOH D   727              2.15
REMARK 500   ND2  ASN D   306     O    HOH D   728              2.15
REMARK 500   O    GLY C   233     O    HOH C   725              2.15
REMARK 500
REMARK 500 THIS ENTRY HAS      64 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    ASN S   105     O    HOH A   727     2555     1.92
REMARK 500   ND2  ASN D   207     O    HOH C   615     2555     1.94
REMARK 500   OG1  THR D    75     NE2  GLN T   109     2555     2.00
REMARK 500   OD2  ASP A   106     OG   SER A   370     2555     2.05
REMARK 500   CG2  THR A    65     O    HOH B   728     2555     2.07
REMARK 500   OD2  ASP B   106     OG   SER D   370     2555     2.13
REMARK 500   OG1  THR C    75     NE2  GLN U   109     2555     2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    TRP A 214   NE1   TRP A 214   CE2    -0.088
REMARK 500    HIS A 282   CG    HIS A 282   CD2     0.063
REMARK 500    GLY A 373   N     GLY A 373   CA      0.100
REMARK 500    HIS B 307   CG    HIS B 307   CD2     0.066
REMARK 500    HIS B 409   CG    HIS B 409   CD2     0.057
REMARK 500    GLU C 204   CD    GLU C 204   OE2     0.071
REMARK 500    HIS C 292   CG    HIS C 292   CD2     0.084
REMARK 500    HIS C 327   CG    HIS C 327   CD2     0.061
REMARK 500    TRP D  70   CE2   TRP D  70   CD2     0.073
REMARK 500    GLU D 248   CD    GLU D 248   OE2     0.066
REMARK 500    HIS D 292   CG    HIS D 292   CD2     0.065
REMARK 500    HIS D 383   CG    HIS D 383   CD2     0.060
REMARK 500    TRP D 411   CE2   TRP D 411   CD2     0.073
REMARK 500    HIS S  55   CG    HIS S  55   CD2     0.056
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A 131   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    LEU A 135   CB  -  CG  -  CD1 ANGL. DEV. =  12.6 DEGREES
REMARK 500    ASP A 160   CB  -  CG  -  OD2 ANGL. DEV. =   8.1 DEGREES
REMARK 500    CYS A 172   CA  -  CB  -  SG  ANGL. DEV. =   9.9 DEGREES
REMARK 500    ASP A 202   CB  -  CG  -  OD1 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ASP A 202   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ASP A 203   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES
REMARK 500    VAL A 206   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES
REMARK 500    ARG A 213   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 213   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    CYS A 221   CA  -  CB  -  SG  ANGL. DEV. = -11.5 DEGREES
REMARK 500    LEU A 240   CB  -  CG  -  CD1 ANGL. DEV. =  12.3 DEGREES
REMARK 500    ARG A 253   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG A 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A 258   CG  -  CD  -  NE  ANGL. DEV. = -15.9 DEGREES
REMARK 500    ASP A 268   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ASP A 352   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ARG A 358   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP A 367   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP A 367   CB  -  CG  -  OD2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    LEU B 130   CA  -  CB  -  CG  ANGL. DEV. =  20.6 DEGREES
REMARK 500    ASP B 137   CB  -  CG  -  OD1 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    PRO B 141   C   -  N   -  CA  ANGL. DEV. = -11.0 DEGREES
REMARK 500    PRO B 152   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES
REMARK 500    ASP B 216   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    CYS B 221   CA  -  CB  -  SG  ANGL. DEV. =   9.1 DEGREES
REMARK 500    ARG B 253   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG B 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ASP B 286   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES
REMARK 500    ASP B 286   CB  -  CG  -  OD2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    LEU B 290   CB  -  CG  -  CD1 ANGL. DEV. = -12.0 DEGREES
REMARK 500    LEU B 335   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES
REMARK 500    ASP B 396   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    PRO B 415   C   -  N   -  CD  ANGL. DEV. = -15.3 DEGREES
REMARK 500    LEU C 138   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES
REMARK 500    ARG C 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    PRO C 263   C   -  N   -  CA  ANGL. DEV. =  14.7 DEGREES
REMARK 500    LEU C 289   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES
REMARK 500    LEU C 314   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES
REMARK 500    ARG C 319   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ASP C 324   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    PRO C 376   C   -  N   -  CA  ANGL. DEV. = -10.8 DEGREES
REMARK 500    ASP D  35   CB  -  CG  -  OD1 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ASP D 268   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES
REMARK 500    ASP D 268   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    TYR D 269   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    TYR D 269   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG D 295   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      59 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PRO A  27       -3.29    -57.81
REMARK 500    THR A  31      152.25    -49.19
REMARK 500    VAL A  48      107.73    -45.31
REMARK 500    SER A  62      -78.63   -159.13
REMARK 500    PRO A  91      127.86    -38.11
REMARK 500    ASP A  94      -79.34     67.17
REMARK 500    LEU A 107       -9.41    -59.66
REMARK 500    SER A 119      -63.20   -105.34
REMARK 500    ASN A 123      -43.60   -145.75
REMARK 500    LEU A 133      123.00   -170.25
REMARK 500    LYS A 146       -4.91    -57.95
REMARK 500    HIS A 153      -60.63   -144.51
REMARK 500    ASN A 163       26.09     83.57
REMARK 500    ASN A 207      -93.41   -135.74
REMARK 500    MET A 212      106.87   -169.01
REMARK 500    TYR A 239      101.49    -24.43
REMARK 500    ILE A 264      146.33   -170.34
REMARK 500    MET A 297       -0.12     88.21
REMARK 500    HIS A 307      114.24   -163.00
REMARK 500    PHE A 311      -23.95    -38.99
REMARK 500    VAL A 331      -74.25     57.44
REMARK 500    LYS A 356      120.84    -34.60
REMARK 500    VAL A 369       66.47     32.79
REMARK 500    SER A 379      110.97    162.41
REMARK 500    ASP A 396      -18.69    -49.76
REMARK 500    ASP B  33       -5.60    -45.86
REMARK 500    PRO B  50      -70.90    -19.09
REMARK 500    SER B  62      -93.02   -148.03
REMARK 500    THR B  75     -167.83   -120.68
REMARK 500    GLU B  93      124.19    -33.18
REMARK 500    VAL B 124       -7.91    -51.54
REMARK 500    PHE B 127      112.69    -19.52
REMARK 500    TYR B 142       -3.74    -57.71
REMARK 500    HIS B 153      -54.33   -139.87
REMARK 500    GLN B 156      -79.53    -54.07
REMARK 500    THR B 200     -164.18   -103.90
REMARK 500    LYS B 201      148.71   -172.85
REMARK 500    ASN B 207     -107.13   -143.30
REMARK 500    MET B 212       96.90    170.42
REMARK 500    ASP B 216      -77.45    -27.77
REMARK 500    ALA B 296      110.29    -13.85
REMARK 500    MET B 297      -25.44     88.66
REMARK 500    VAL B 331      -42.99     52.70
REMARK 500    ASP B 357       98.31   -171.26
REMARK 500    SER B 370       -7.85     80.83
REMARK 500    LEU B 371      127.20    -38.02
REMARK 500    SER B 379      114.41    175.10
REMARK 500    THR B 406      -47.40   -135.44
REMARK 500    LEU B 424      -71.91    -63.33
REMARK 500    GLU B 425      -35.37    -29.93
REMARK 500
REMARK 500 THIS ENTRY HAS     160 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PHE A  199     THR A  200                  143.11
REMARK 500 GLU C   93     ASP C   94                 -147.36
REMARK 500 GLY C  195     GLY C  196                  147.23
REMARK 500 PHE C  199     THR C  200                  147.83
REMARK 500 LYS S   47     LYS S   48                 -141.63
REMARK 500 GLU V  121     SER V  122                  149.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASP A  94        20.8      L          L   OUTSIDE RANGE
REMARK 500    LYS A 183        25.0      L          L   OUTSIDE RANGE
REMARK 500    LYS A 201        24.0      L          L   OUTSIDE RANGE
REMARK 500    GLU A 259        24.9      L          L   OUTSIDE RANGE
REMARK 500    ASP A 302        22.2      L          L   OUTSIDE RANGE
REMARK 500    ASN A 306        24.1      L          L   OUTSIDE RANGE
REMARK 500    TYR B  24        23.1      L          L   OUTSIDE RANGE
REMARK 500    GLN B 156        24.6      L          L   OUTSIDE RANGE
REMARK 500    TYR B 239        23.5      L          L   OUTSIDE RANGE
REMARK 500    ILE B 293        24.7      L          L   OUTSIDE RANGE
REMARK 500    ALA B 296        24.0      L          L   OUTSIDE RANGE
REMARK 500    ARG B 303        23.0      L          L   OUTSIDE RANGE
REMARK 500    PHE B 345        24.8      L          L   OUTSIDE RANGE
REMARK 500    TYR B 363        24.0      L          L   OUTSIDE RANGE
REMARK 500    ILE B 382        24.8      L          L   OUTSIDE RANGE
REMARK 500    VAL B 384        25.0      L          L   OUTSIDE RANGE
REMARK 500    LEU C  37        24.1      L          L   OUTSIDE RANGE
REMARK 500    TYR C 226        23.8      L          L   OUTSIDE RANGE
REMARK 500    THR D 147        23.8      L          L   OUTSIDE RANGE
REMARK 500    HIS D 153        24.6      L          L   OUTSIDE RANGE
REMARK 500    TYR D 269        19.0      L          L   OUTSIDE RANGE
REMARK 500    THR D 279        22.8      L          L   OUTSIDE RANGE
REMARK 500    SER D 281        25.0      L          L   OUTSIDE RANGE
REMARK 500    THR D 330        23.7      L          L   OUTSIDE RANGE
REMARK 500    PHE D 345        21.9      L          L   OUTSIDE RANGE
REMARK 500    SER D 370        23.0      L          L   OUTSIDE RANGE
REMARK 500    HIS D 383        24.9      L          L   OUTSIDE RANGE
REMARK 500    TYR S 123        21.0      L          L   OUTSIDE RANGE
REMARK 500    HIS T  55        24.1      L          L   OUTSIDE RANGE
REMARK 500    ASN U 106        24.7      L          L   OUTSIDE RANGE
REMARK 500    HIS V  55        24.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB D 501
DBREF  4HHH A    1   475  UNP    P04717   RBL_PEA          1    475
DBREF  4HHH B    1   475  UNP    P04717   RBL_PEA          1    475
DBREF  4HHH C    1   475  UNP    P04717   RBL_PEA          1    475
DBREF  4HHH D    1   475  UNP    P04717   RBL_PEA          1    475
DBREF  4HHH S    1   123  PDB    4HHH     4HHH             1    123
DBREF  4HHH T    1   123  PDB    4HHH     4HHH             1    123
DBREF  4HHH U    1   123  PDB    4HHH     4HHH             1    123
DBREF  4HHH V    1   123  PDB    4HHH     4HHH             1    123
SEQRES   1 A  475  MET SER PRO GLN THR GLU THR LYS ALA LYS VAL GLY PHE
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 A  475  PRO ASP TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 A  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR GLU ILE GLU PRO VAL PRO
SEQRES   8 A  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 A  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO TYR ALA
SEQRES  12 A  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 A  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU
SEQRES  19 A  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 A  475  GLU GLU MET LEU LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 A  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 A  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 A  475  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  475  ARG GLU ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 A  475  ASP TYR ILE LYS LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 A  475  THR GLN ASP TRP VAL SER LEU PRO GLY VAL ILE PRO VAL
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 A  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 A  475  ALA ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 A  475  PHE PRO ALA MET ASP THR LEU
SEQRES   1 B  475  MET SER PRO GLN THR GLU THR LYS ALA LYS VAL GLY PHE
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 B  475  PRO ASP TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 B  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 B  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR GLU ILE GLU PRO VAL PRO
SEQRES   8 B  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 B  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO TYR ALA
SEQRES  12 B  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 B  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU
SEQRES  19 B  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 B  475  GLU GLU MET LEU LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 B  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 B  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 B  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 B  475  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  475  ARG GLU ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 B  475  ASP TYR ILE LYS LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 B  475  THR GLN ASP TRP VAL SER LEU PRO GLY VAL ILE PRO VAL
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 B  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 B  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 B  475  ALA ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 B  475  PHE PRO ALA MET ASP THR LEU
SEQRES   1 C  475  MET SER PRO GLN THR GLU THR LYS ALA LYS VAL GLY PHE
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 C  475  PRO ASP TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 C  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 C  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR GLU ILE GLU PRO VAL PRO
SEQRES   8 C  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 C  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO TYR ALA
SEQRES  12 C  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 C  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU
SEQRES  19 C  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 C  475  GLU GLU MET LEU LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 C  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 C  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 C  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 C  475  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 C  475  ARG GLU ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 C  475  ASP TYR ILE LYS LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 C  475  THR GLN ASP TRP VAL SER LEU PRO GLY VAL ILE PRO VAL
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 C  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 C  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 C  475  ALA ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 C  475  PHE PRO ALA MET ASP THR LEU
SEQRES   1 D  475  MET SER PRO GLN THR GLU THR LYS ALA LYS VAL GLY PHE
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR LYS LEU THR TYR TYR THR
SEQRES   3 D  475  PRO ASP TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 D  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 D  475  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR GLU ILE GLU PRO VAL PRO
SEQRES   8 D  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 D  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO TYR ALA
SEQRES  12 D  475  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 D  475  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 D  475  ALA GLU ALA ILE TYR LYS SER GLN ALA GLU THR GLY GLU
SEQRES  19 D  475  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 D  475  GLU GLU MET LEU LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 D  475  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 D  475  PHE THR ALA ASN THR THR LEU SER HIS TYR CYS ARG ASP
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 D  475  VAL ILE ASP ARG GLN LYS ASN HIS GLY MET HIS PHE ARG
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG LEU SER GLY GLY ASP HIS
SEQRES  26 D  475  ILE HIS ALA GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 D  475  ARG GLU ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 D  475  ASP TYR ILE LYS LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 D  475  THR GLN ASP TRP VAL SER LEU PRO GLY VAL ILE PRO VAL
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 D  475  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 D  475  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY ASN
SEQRES  35 D  475  ALA ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES  37 D  475  PHE PRO ALA MET ASP THR LEU
SEQRES   1 S  123  MET GLN VAL TRP PRO PRO ILE GLY LYS LYS LYS PHE GLU
SEQRES   2 S  123  THR LEU SER TYR LEU PRO PRO LEU THR ARG ASP GLN LEU
SEQRES   3 S  123  LEU LYS GLU VAL GLU TYR LEU LEU ARG LYS GLY TRP VAL
SEQRES   4 S  123  PRO CYS LEU GLU PHE GLU LEU LYS LYS GLY PHE VAL TYR
SEQRES   5 S  123  ARG GLU HIS ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 S  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY THR THR
SEQRES   7 S  123  ASP PRO ALA GLN VAL LEU LYS GLU LEU ASP GLU VAL LYS
SEQRES   8 S  123  LYS GLU TYR PRO ARG ALA PHE VAL ARG VAL ILE GLY PHE
SEQRES   9 S  123  ASN ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 S  123  HIS THR PRO GLU SER TYR
SEQRES   1 T  123  MET GLN VAL TRP PRO PRO ILE GLY LYS LYS LYS PHE GLU
SEQRES   2 T  123  THR LEU SER TYR LEU PRO PRO LEU THR ARG ASP GLN LEU
SEQRES   3 T  123  LEU LYS GLU VAL GLU TYR LEU LEU ARG LYS GLY TRP VAL
SEQRES   4 T  123  PRO CYS LEU GLU PHE GLU LEU LYS LYS GLY PHE VAL TYR
SEQRES   5 T  123  ARG GLU HIS ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 T  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY THR THR
SEQRES   7 T  123  ASP PRO ALA GLN VAL LEU LYS GLU LEU ASP GLU VAL LYS
SEQRES   8 T  123  LYS GLU TYR PRO ARG ALA PHE VAL ARG VAL ILE GLY PHE
SEQRES   9 T  123  ASN ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 T  123  HIS THR PRO GLU SER TYR
SEQRES   1 U  123  MET GLN VAL TRP PRO PRO ILE GLY LYS LYS LYS PHE GLU
SEQRES   2 U  123  THR LEU SER TYR LEU PRO PRO LEU THR ARG ASP GLN LEU
SEQRES   3 U  123  LEU LYS GLU VAL GLU TYR LEU LEU ARG LYS GLY TRP VAL
SEQRES   4 U  123  PRO CYS LEU GLU PHE GLU LEU LYS LYS GLY PHE VAL TYR
SEQRES   5 U  123  ARG GLU HIS ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 U  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY THR THR
SEQRES   7 U  123  ASP PRO ALA GLN VAL LEU LYS GLU LEU ASP GLU VAL LYS
SEQRES   8 U  123  LYS GLU TYR PRO ARG ALA PHE VAL ARG VAL ILE GLY PHE
SEQRES   9 U  123  ASN ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 U  123  HIS THR PRO GLU SER TYR
SEQRES   1 V  123  MET GLN VAL TRP PRO PRO ILE GLY LYS LYS LYS PHE GLU
SEQRES   2 V  123  THR LEU SER TYR LEU PRO PRO LEU THR ARG ASP GLN LEU
SEQRES   3 V  123  LEU LYS GLU VAL GLU TYR LEU LEU ARG LYS GLY TRP VAL
SEQRES   4 V  123  PRO CYS LEU GLU PHE GLU LEU LYS LYS GLY PHE VAL TYR
SEQRES   5 V  123  ARG GLU HIS ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 V  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY THR THR
SEQRES   7 V  123  ASP PRO ALA GLN VAL LEU LYS GLU LEU ASP GLU VAL LYS
SEQRES   8 V  123  LYS GLU TYR PRO ARG ALA PHE VAL ARG VAL ILE GLY PHE
SEQRES   9 V  123  ASN ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 V  123  HIS THR PRO GLU SER TYR
HET    RUB  A 501      18
HET    RUB  B 501      18
HET    RUB  C 501      18
HET    RUB  D 501      18
HETNAM     RUB RIBULOSE-1,5-DIPHOSPHATE
FORMUL   9  RUB    4(C5 H12 O11 P2)
FORMUL  13  HOH   *789(H2 O)
HELIX    1   1 TYR A   20  TYR A   25  1                                   6
HELIX    2   2 PRO A   49  SER A   61  1                                  13
HELIX    3   3 VAL A   69  GLY A   73  5                                   5
HELIX    4   4 SER A   76  LYS A   81  1                                   6
HELIX    5   5 PRO A  104  PHE A  108  5                                   5
HELIX    6   6 SER A  112  VAL A  121  1                                  10
HELIX    7   7 ASN A  123  PHE A  127  5                                   5
HELIX    8   8 PRO A  141  LYS A  146  1                                   6
HELIX    9   9 GLY A  154  ASN A  163  1                                  10
HELIX   10  10 SER A  181  ARG A  194  1                                  14
HELIX   11  11 ARG A  213  GLY A  233  1                                  21
HELIX   12  12 THR A  246  GLY A  261  1                                  16
HELIX   13  13 TYR A  269  GLY A  273  1                                   5
HELIX   14  14 GLY A  273  GLY A  288  1                                  16
HELIX   15  15 MET A  297  ARG A  303  1                                   7
HELIX   16  16 HIS A  310  GLY A  322  1                                  13
HELIX   17  17 GLU A  338  ASP A  351  1                                  14
HELIX   18  18 HIS A  383  TRP A  385  5                                   3
HELIX   19  19 HIS A  386  PHE A  394  1                                   9
HELIX   20  20 GLY A  403  GLY A  408  1                                   6
HELIX   21  21 GLY A  412  GLU A  433  1                                  22
HELIX   22  22 GLU A  440  LYS A  450  1                                  11
HELIX   23  23 SER A  452  TRP A  462  1                                  11
HELIX   24  24 TYR B   20  TYR B   25  1                                   6
HELIX   25  25 PRO B   49  SER B   61  1                                  13
HELIX   26  26 VAL B   69  GLY B   73  5                                   5
HELIX   27  27 SER B   76  LYS B   81  1                                   6
HELIX   28  28 PRO B  104  PHE B  108  5                                   5
HELIX   29  29 SER B  112  GLY B  122  1                                  11
HELIX   30  30 TYR B  144  PHE B  148  5                                   5
HELIX   31  31 HIS B  153  ASN B  163  1                                  11
HELIX   32  32 SER B  181  GLY B  195  1                                  15
HELIX   33  33 ARG B  213  GLY B  233  1                                  21
HELIX   34  34 THR B  246  GLY B  261  1                                  16
HELIX   35  35 TYR B  269  GLY B  273  1                                   5
HELIX   36  36 GLY B  273  ASN B  287  1                                  15
HELIX   37  37 MET B  297  ARG B  303  1                                   7
HELIX   38  38 HIS B  310  GLY B  322  1                                  13
HELIX   39  39 GLU B  338  ASP B  351  1                                  14
HELIX   40  40 HIS B  383  TRP B  385  5                                   3
HELIX   41  41 HIS B  386  GLY B  395  1                                  10
HELIX   42  42 GLY B  403  GLY B  408  1                                   6
HELIX   43  43 GLY B  412  GLY B  434  1                                  23
HELIX   44  44 GLU B  440  LYS B  450  1                                  11
HELIX   45  45 SER B  452  TRP B  462  1                                  11
HELIX   46  46 PRO C   49  SER C   61  1                                  13
HELIX   47  47 VAL C   69  LEU C   74  5                                   6
HELIX   48  48 SER C   76  LYS C   81  1                                   6
HELIX   49  49 PRO C  104  PHE C  108  5                                   5
HELIX   50  50 SER C  112  GLY C  122  1                                  11
HELIX   51  51 ASN C  123  PHE C  127  5                                   5
HELIX   52  52 PRO C  141  LYS C  146  1                                   6
HELIX   53  53 HIS C  153  ASN C  163  1                                  11
HELIX   54  54 SER C  181  GLY C  195  1                                  15
HELIX   55  55 ARG C  213  GLY C  233  1                                  21
HELIX   56  56 THR C  246  GLY C  261  1                                  16
HELIX   57  57 TYR C  269  GLY C  273  1                                   5
HELIX   58  58 GLY C  273  ASN C  287  1                                  15
HELIX   59  59 MET C  297  ARG C  303  1                                   7
HELIX   60  60 HIS C  310  GLY C  322  1                                  13
HELIX   61  61 GLU C  338  ASP C  351  1                                  14
HELIX   62  62 HIS C  383  TRP C  385  5                                   3
HELIX   63  63 HIS C  386  GLY C  395  1                                  10
HELIX   64  64 GLY C  403  GLY C  408  1                                   6
HELIX   65  65 GLY C  412  GLU C  433  1                                  22
HELIX   66  66 ASP C  436  SER C  452  1                                  17
HELIX   67  67 SER C  452  TRP C  462  1                                  11
HELIX   68  68 TYR D   20  TYR D   25  1                                   6
HELIX   69  69 PRO D   49  GLU D   60  1                                  12
HELIX   70  70 VAL D   69  THR D   75  5                                   7
HELIX   71  71 SER D   76  LYS D   81  1                                   6
HELIX   72  72 PRO D  104  PHE D  108  5                                   5
HELIX   73  73 SER D  112  GLY D  122  1                                  11
HELIX   74  74 PRO D  141  LYS D  146  1                                   6
HELIX   75  75 GLY D  154  ASN D  163  1                                  10
HELIX   76  76 SER D  181  ARG D  194  1                                  14
HELIX   77  77 ARG D  213  GLY D  233  1                                  21
HELIX   78  78 THR D  246  LEU D  260  1                                  15
HELIX   79  79 TYR D  269  GLY D  273  1                                   5
HELIX   80  80 GLY D  273  GLY D  288  1                                  16
HELIX   81  81 MET D  297  ARG D  303  1                                   7
HELIX   82  82 HIS D  310  GLY D  322  1                                  13
HELIX   83  83 GLU D  338  ASP D  351  1                                  14
HELIX   84  84 HIS D  383  TRP D  385  5                                   3
HELIX   85  85 HIS D  386  PHE D  394  1                                   9
HELIX   86  86 GLY D  403  GLY D  408  1                                   6
HELIX   87  87 GLY D  412  GLU D  433  1                                  22
HELIX   88  88 GLU D  440  SER D  452  1                                  13
HELIX   89  89 SER D  452  TRP D  462  1                                  11
HELIX   90  90 THR S   22  LYS S   36  1                                  15
HELIX   91  91 PRO S   80  TYR S   94  1                                  15
HELIX   92  92 THR T   22  GLY T   37  1                                  16
HELIX   93  93 PRO T   80  TYR T   94  1                                  15
HELIX   94  94 ASP U   24  LEU U   34  1                                  11
HELIX   95  95 ASP U   79  TYR U   94  1                                  16
HELIX   96  96 THR V   22  LYS V   36  1                                  15
HELIX   97  97 PRO V   80  TYR V   94  1                                  15
SHEET    1   A 5 ARG A  83  VAL A  90  0
SHEET    2   A 5 GLN A  96  TYR A 103 -1  O  TYR A 100   N  GLU A  86
SHEET    3   A 5 ILE A  36  PRO A  44 -1  N  ILE A  36   O  TYR A 103
SHEET    4   A 5 LEU A 130  ARG A 139 -1  O  ARG A 134   N  ARG A  41
SHEET    5   A 5 GLY A 308  MET A 309  1  O  GLY A 308   N  LEU A 135
SHEET    1   B 8 LEU A 169  GLY A 171  0
SHEET    2   B 8 VAL A 399  GLN A 401  1  O  LEU A 400   N  LEU A 169
SHEET    3   B 8 ILE A 375  ALA A 378  1  N  ALA A 378   O  VAL A 399
SHEET    4   B 8 HIS A 325  HIS A 327  1  N  ILE A 326   O  VAL A 377
SHEET    5   B 8 LEU A 290  HIS A 294  1  N  ILE A 293   O  HIS A 325
SHEET    6   B 8 ILE A 264  ASP A 268  1  N  VAL A 265   O  HIS A 292
SHEET    7   B 8 GLY A 237  ASN A 241  1  N  LEU A 240   O  MET A 266
SHEET    8   B 8 PHE A 199  LYS A 201  1  N  THR A 200   O  TYR A 239
SHEET    1   C 2 TYR A 353  ILE A 354  0
SHEET    2   C 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  ILE A 354
SHEET    1   D 5 ARG B  83  PRO B  89  0
SHEET    2   D 5 PHE B  97  TYR B 103 -1  O  ALA B 102   N  ARG B  83
SHEET    3   D 5 ILE B  36  PRO B  44 -1  N  ILE B  36   O  TYR B 103
SHEET    4   D 5 LEU B 130  ARG B 139 -1  O  ARG B 134   N  ARG B  41
SHEET    5   D 5 GLY B 308  MET B 309  1  O  GLY B 308   N  LEU B 135
SHEET    1   E 8 LEU B 169  GLY B 171  0
SHEET    2   E 8 VAL B 399  GLN B 401  1  O  LEU B 400   N  LEU B 169
SHEET    3   E 8 ILE B 375  SER B 379  1  N  PRO B 376   O  VAL B 399
SHEET    4   E 8 HIS B 325  HIS B 327  1  N  ILE B 326   O  VAL B 377
SHEET    5   E 8 LEU B 290  HIS B 294  1  N  ILE B 293   O  HIS B 325
SHEET    6   E 8 ILE B 264  ASP B 268  1  N  VAL B 265   O  HIS B 292
SHEET    7   E 8 GLY B 237  ASN B 241  1  N  LEU B 240   O  MET B 266
SHEET    8   E 8 PHE B 199  LYS B 201  1  N  THR B 200   O  TYR B 239
SHEET    1   F 2 TYR B 353  ILE B 354  0
SHEET    2   F 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  ILE B 354
SHEET    1   G 4 ARG C  83  PRO C  89  0
SHEET    2   G 4 PHE C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88
SHEET    3   G 4 ILE C  36  PRO C  44 -1  N  ILE C  36   O  TYR C 103
SHEET    4   G 4 LEU C 130  ARG C 139 -1  O  ARG C 134   N  ARG C  41
SHEET    1   H 8 LEU C 169  GLY C 171  0
SHEET    2   H 8 VAL C 399  GLN C 401  1  O  LEU C 400   N  LEU C 169
SHEET    3   H 8 ILE C 375  SER C 379  1  N  ALA C 378   O  VAL C 399
SHEET    4   H 8 HIS C 325  HIS C 327  1  N  ILE C 326   O  VAL C 377
SHEET    5   H 8 LEU C 290  HIS C 294  1  N  LEU C 291   O  HIS C 325
SHEET    6   H 8 ILE C 264  ASP C 268  1  N  VAL C 265   O  HIS C 292
SHEET    7   H 8 GLY C 237  ASN C 241  1  N  LEU C 240   O  MET C 266
SHEET    8   H 8 PHE C 199  LYS C 201  1  N  THR C 200   O  TYR C 239
SHEET    1   I 2 TYR C 353  ILE C 354  0
SHEET    2   I 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  ILE C 354
SHEET    1   J 4 ARG D  83  PRO D  89  0
SHEET    2   J 4 PHE D  97  TYR D 103 -1  O  ILE D  98   N  GLU D  88
SHEET    3   J 4 ILE D  36  PRO D  44 -1  N  PHE D  40   O  ALA D  99
SHEET    4   J 4 LEU D 130  ARG D 139 -1  O  ARG D 134   N  ARG D  41
SHEET    1   K 8 LEU D 169  GLY D 171  0
SHEET    2   K 8 VAL D 399  GLN D 401  1  O  LEU D 400   N  LEU D 169
SHEET    3   K 8 ILE D 375  ALA D 378  1  N  ALA D 378   O  GLN D 401
SHEET    4   K 8 HIS D 325  HIS D 327  1  N  ILE D 326   O  ILE D 375
SHEET    5   K 8 LEU D 290  HIS D 294  1  N  ILE D 293   O  HIS D 327
SHEET    6   K 8 ILE D 264  ASP D 268  1  N  HIS D 267   O  HIS D 292
SHEET    7   K 8 GLY D 237  ASN D 241  1  N  LEU D 240   O  MET D 266
SHEET    8   K 8 PHE D 199  LYS D 201  1  N  THR D 200   O  TYR D 239
SHEET    1   L 2 TYR D 353  ILE D 354  0
SHEET    2   L 2 GLN D 366  ASP D 367 -1  O  GLN D 366   N  ILE D 354
SHEET    1   M 4 THR S  68  TRP S  70  0
SHEET    2   M 4 VAL S  39  GLU S  45 -1  N  PHE S  44   O  THR S  68
SHEET    3   M 4 PHE S  98  PHE S 104 -1  O  PHE S 104   N  VAL S  39
SHEET    4   M 4 GLN S 111  HIS S 118 -1  O  ALA S 117   N  VAL S  99
SHEET    1   N 4 THR T  68  MET T  69  0
SHEET    2   N 4 VAL T  39  GLU T  45 -1  N  PHE T  44   O  THR T  68
SHEET    3   N 4 PHE T  98  ASN T 105 -1  O  ILE T 102   N  CYS T  41
SHEET    4   N 4 VAL T 110  HIS T 118 -1  O  ALA T 117   N  VAL T  99
SHEET    1   O 4 THR U  68  TRP U  70  0
SHEET    2   O 4 VAL U  39  GLU U  45 -1  N  PHE U  44   O  THR U  68
SHEET    3   O 4 PHE U  98  PHE U 104 -1  O  ARG U 100   N  GLU U  43
SHEET    4   O 4 SER U 114  HIS U 118 -1  O  ALA U 117   N  VAL U  99
SHEET    1   P 4 THR V  68  TRP V  70  0
SHEET    2   P 4 VAL V  39  GLU V  45 -1  N  LEU V  42   O  TRP V  70
SHEET    3   P 4 PHE V  98  PHE V 104 -1  O  ILE V 102   N  CYS V  41
SHEET    4   P 4 GLN V 111  HIS V 118 -1  O  ALA V 117   N  VAL V  99
SSBOND   1 CYS C  247    CYS D  247                          1555   2555  2.37
CISPEP   1 GLU A   93    ASP A   94          0         4.74
CISPEP   2 LYS A  175    PRO A  176          0        -0.29
CISPEP   3 ASP B   94    ASN B   95          0         5.79
CISPEP   4 LYS B  175    PRO B  176          0        -1.26
CISPEP   5 LYS C  175    PRO C  176          0         5.39
CISPEP   6 LYS D  175    PRO D  176          0       -12.83
CISPEP   7 GLU U  121    SER U  122          0         4.16
SITE     1 AC1 23 THR A 173  LYS A 177  ASP A 203  GLU A 204
SITE     2 AC1 23 HIS A 294  ARG A 295  HIS A 327  LYS A 334
SITE     3 AC1 23 LEU A 335  SER A 379  GLY A 380  GLY A 381
SITE     4 AC1 23 GLY A 403  GLY A 404  HOH A 622  HOH A 634
SITE     5 AC1 23 HOH A 661  HOH A 662  HOH A 682  THR B  65
SITE     6 AC1 23 TRP B  66  ASN B 123  HOH B 716
SITE     1 AC2 22 THR A  65  TRP A  66  ASN A 123  LYS B 175
SITE     2 AC2 22 ASP B 203  GLU B 204  HIS B 294  ARG B 295
SITE     3 AC2 22 HIS B 327  LYS B 334  LEU B 335  SER B 379
SITE     4 AC2 22 GLY B 380  GLY B 381  GLY B 403  GLY B 404
SITE     5 AC2 22 HOH B 611  HOH B 638  HOH B 682  HOH B 684
SITE     6 AC2 22 HOH B 691  HOH B 728
SITE     1 AC3 22 THR C 173  LYS C 175  ASP C 203  GLU C 204
SITE     2 AC3 22 HIS C 294  ARG C 295  HIS C 327  LEU C 335
SITE     3 AC3 22 SER C 379  GLY C 380  GLY C 381  GLY C 403
SITE     4 AC3 22 GLY C 404  HOH C 614  HOH C 651  HOH C 652
SITE     5 AC3 22 HOH C 675  HOH C 703  HOH C 737  THR D  65
SITE     6 AC3 22 TRP D  66  ASN D 123
SITE     1 AC4 20 THR C  65  TRP C  66  ASN C 123  LYS D 175
SITE     2 AC4 20 LYS D 177  ASP D 203  GLU D 204  ARG D 295
SITE     3 AC4 20 HIS D 327  LYS D 334  LEU D 335  SER D 379
SITE     4 AC4 20 GLY D 381  GLY D 403  GLY D 404  HOH D 709
SITE     5 AC4 20 HOH D 717  HOH D 719  HOH D 720  HOH D 745
CRYST1  109.790  109.950  201.440  90.00  90.00  90.00 P 21 2 21    16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.009108  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009095  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004964        0.00000
      
PROCHECK
Go to PROCHECK summary
 References