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PDBsum entry 4f0h

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Lyase PDB id
4f0h
Jmol
Contents
Protein chains
448 a.a.
138 a.a.
Ligands
OXY
PO4 ×2
Waters ×336
HEADER    LYASE                                   04-MAY-12   4F0H
TITLE     UNACTIVATED RUBISCO WITH OXYGEN BOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A;
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: B;
COMPND   9 SYNONYM: RUBISCO SMALL SUBUNIT;
COMPND  10 EC: 4.1.1.39
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GALDIERIA SULPHURARIA;
SOURCE   3 ORGANISM_COMMON: RED ALGA;
SOURCE   4 ORGANISM_TAXID: 130081;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: GALDIERIA SULPHURARIA;
SOURCE   7 ORGANISM_COMMON: RED ALGA;
SOURCE   8 ORGANISM_TAXID: 130081
KEYWDS    ALPHA BETA DOMAIN, CATALYTIC DOMAIN TIM BARREL,
KEYWDS   2 CARBOXYLASE/OXYGENASE, NITROSYLATION, CHLOROPLAST, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.STEC
REVDAT   2   12-DEC-12 4F0H    1       JRNL
REVDAT   1   14-NOV-12 4F0H    0
JRNL        AUTH   B.STEC
JRNL        TITL   STRUCTURAL MECHANISM OF RUBISCO ACTIVATION BY CARBAMYLATION
JRNL        TITL 2 OF THE ACTIVE SITE LYSINE.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 18785 2012
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   23112176
JRNL        DOI    10.1073/PNAS.1210754109
REMARK   2
REMARK   2 RESOLUTION.    1.96 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.96
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2
REMARK   3   NUMBER OF REFLECTIONS             : 37497
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) : 0.166
REMARK   3   R VALUE            (WORKING SET) : 0.163
REMARK   3   FREE R VALUE                     : 0.223
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1979
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) : 1.96
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.01
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1496
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.16
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800
REMARK   3   BIN FREE R VALUE SET COUNT          : 77
REMARK   3   BIN FREE R VALUE                    : 0.3370
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4658
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 12
REMARK   3   SOLVENT ATOMS            : 336
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.94
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.02000
REMARK   3    B22 (A**2) : -0.02000
REMARK   3    B33 (A**2) : 0.04000
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): 0.178
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.166
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.237
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4800 ; 0.021 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6496 ; 1.906 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   590 ; 6.568 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   220 ;35.865 ;23.682
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   830 ;16.505 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;16.158 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   704 ; 0.133 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3635 ; 0.010 ; 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):  2927 ; 2.514 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4711 ; 3.528 ; 4.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1873 ; 3.082 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1785 ; 4.146 ; 4.000
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 : NULL
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 ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 4F0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-NOV-03
REMARK 200  TEMPERATURE           (KELVIN) : 298.0
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : CONFOCAL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37497
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.960
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.04500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.33000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3RUB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M POTASSIUM PHOSPHATE, 26%
REMARK 280  AMMONIUM SULFATE, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      16555   -Y+1/2,-X+1/2,-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  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       68.22000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       60.83500
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       68.22000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       60.83500
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       68.22000
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       60.83500
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       68.22000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       60.83500
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       68.22000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       60.83500
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       68.22000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       60.83500
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       68.22000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       60.83500
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       68.22000
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       68.22000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       60.83500
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: 100840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 126570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -485.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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      136.44000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      136.44000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      136.44000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      136.44000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000      136.44000
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000      136.44000
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000      136.44000
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000      136.44000
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A1131  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 784  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1034  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 717  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1110  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1103  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 830  LIES ON A SPECIAL POSITION.
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     GLN A     3
REMARK 465     SER A     4
REMARK 465     LEU A     5
REMARK 465     GLU A     6
REMARK 465     GLU A     7
REMARK 465     LYS A     8
REMARK 465     SER A     9
REMARK 465     VAL A    10
REMARK 465     GLN A    11
REMARK 465     GLU A    12
REMARK 465     ARG A    13
REMARK 465     THR A    14
REMARK 465     ARG A    15
REMARK 465     ILE A    16
REMARK 465     LYS A    17
REMARK 465     ASN A    18
REMARK 465     SER A    19
REMARK 465     ARG A    20
REMARK 465     TYR A    21
REMARK 465     GLU A    22
REMARK 465     SER A    23
REMARK 465     GLY A    24
REMARK 465     VAL A    25
REMARK 465     ILE A    26
REMARK 465     PHE A   475
REMARK 465     ASN A   476
REMARK 465     TYR A   477
REMARK 465     THR A   478
REMARK 465     SER A   479
REMARK 465     THR A   480
REMARK 465     ASP A   481
REMARK 465     THR A   482
REMARK 465     SER A   483
REMARK 465     ASP A   484
REMARK 465     PHE A   485
REMARK 465     VAL A   486
REMARK 465     GLU A   487
REMARK 465     THR A   488
REMARK 465     PRO A   489
REMARK 465     THR A   490
REMARK 465     ALA A   491
REMARK 465     ASN A   492
REMARK 465     ILE A   493
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   O    HOH A  1023     O    HOH A  1086              1.63
REMARK 500   OH   TYR A    28     OE1  GLU A    69              2.09
REMARK 500   OH   TYR A   153     O    HOH A  1167              2.14
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    HOH A  1045     O    HOH B   808     4565     2.12
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    PRO A 100   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG A 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
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    TYR A  38      133.88    -38.21
REMARK 500    SER A  71      -99.75   -127.54
REMARK 500    ALA A  73       59.16   -104.16
REMARK 500    PRO A 100      -71.58    -14.90
REMARK 500    ASN A 216      -80.79   -123.54
REMARK 500    MET A 221      114.55   -169.91
REMARK 500    ALA A 304      125.32    -37.47
REMARK 500    LYS A 342       16.22    -66.62
REMARK 500    LEU A 343       49.21   -157.64
REMARK 500    GLU A 344       27.18    -58.81
REMARK 500    ILE A 473      108.58    -58.30
REMARK 500    ILE B 591      -74.41   -113.57
REMARK 500    ASP B 616     -139.14   -118.92
REMARK 500    SER B 618     -121.20     44.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1150        DISTANCE =  6.66 ANGSTROMS
REMARK 525    HOH B 784        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH B 808        DISTANCE =  5.47 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F0K   RELATED DB: PDB
REMARK 900 RELATED ID: 4F0M   RELATED DB: PDB
DBREF  4F0H A    1   493  UNP    P23755   RBL_GALSU        1    493
DBREF  4F0H B  501   638  UNP    P23756   RBS_GALSU        1    138
SEQRES   1 A  493  MET SER GLN SER LEU GLU GLU LYS SER VAL GLN GLU ARG
SEQRES   2 A  493  THR ARG ILE LYS ASN SER ARG TYR GLU SER GLY VAL ILE
SEQRES   3 A  493  PRO TYR ALA LYS MET GLY TYR TRP ASN PRO ASP TYR GLN
SEQRES   4 A  493  VAL LYS ASP THR ASP VAL LEU ALA LEU PHE ARG VAL THR
SEQRES   5 A  493  PRO GLN PRO GLY VAL ASP PRO ILE GLU ALA ALA ALA ALA
SEQRES   6 A  493  VAL ALA GLY GLU SER SER THR ALA THR TRP THR VAL VAL
SEQRES   7 A  493  TRP THR ASP LEU LEU THR ALA ALA ASP LEU TYR ARG ALA
SEQRES   8 A  493  LYS ALA TYR LYS VAL ASP GLN VAL PRO ASN ASN PRO GLU
SEQRES   9 A  493  GLN TYR PHE ALA TYR ILE ALA TYR GLU LEU ASP LEU PHE
SEQRES  10 A  493  GLU GLU GLY SER ILE ALA ASN LEU THR ALA SER ILE ILE
SEQRES  11 A  493  GLY ASN VAL PHE GLY PHE LYS ALA VAL LYS ALA LEU ARG
SEQRES  12 A  493  LEU GLU ASP MET ARG LEU PRO PHE ALA TYR ILE LYS THR
SEQRES  13 A  493  PHE GLN GLY PRO ALA THR GLY VAL ILE LEU GLU ARG GLU
SEQRES  14 A  493  ARG LEU ASP LYS PHE GLY ARG PRO LEU LEU GLY SNC THR
SEQRES  15 A  493  THR LYS PRO LYS LEU GLY LEU SER GLY LYS ASN TYR GLY
SEQRES  16 A  493  ARG VAL VAL TYR GLU ALA LEU LYS GLY GLY LEU ASP PHE
SEQRES  17 A  493  VAL LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE MET
SEQRES  18 A  493  ARG TRP ARG GLU ARG TYR LEU PHE VAL MET GLU ALA VAL
SEQRES  19 A  493  ASN LYS ALA ALA ALA ALA THR GLY GLU VAL LYS GLY HIS
SEQRES  20 A  493  TYR LEU ASN VAL THR ALA ALA THR MET GLU GLU MET TYR
SEQRES  21 A  493  ALA ARG ALA GLN LEU ALA LYS GLU LEU GLY SER VAL ILE
SEQRES  22 A  493  ILE MET ILE ASP LEU VAL ILE GLY TYR THR ALA ILE GLN
SEQRES  23 A  493  THR MET ALA LYS TRP ALA ARG ASP ASN ASP MET ILE LEU
SEQRES  24 A  493  HIS LEU HIS ARG ALA GLY ASN SER THR TYR SER ARG GLN
SEQRES  25 A  493  LYS ASN HIS GLY MET ASN PHE ARG VAL ILE CYS LYS TRP
SEQRES  26 A  493  MET ARG MET ALA GLY VAL ASP HIS ILE HIS ALA GLY THR
SEQRES  27 A  493  VAL VAL GLY LYS LEU GLU GLY ASP PRO ILE ILE THR ARG
SEQRES  28 A  493  GLY PHE TYR LYS THR LEU LEU LEU PRO LYS LEU GLU ARG
SEQRES  29 A  493  ASN LEU GLN GLU GLY LEU PHE PHE ASP MET ASP TRP ALA
SEQRES  30 A  493  SER LEU ARG LYS VAL MET PRO VAL ALA SER GLY GLY ILE
SEQRES  31 A  493  HIS ALA GLY GLN MET HIS GLN LEU ILE HIS TYR LEU GLY
SEQRES  32 A  493  GLU ASP VAL VAL LEU GLN PHE GLY GLY GLY THR ILE GLY
SEQRES  33 A  493  HIS PRO ASP GLY ILE GLN SER GLY ALA THR ALA ASN ARG
SEQRES  34 A  493  VAL ALA LEU GLU ALA MET ILE LEU ALA ARG ASN GLU ASN
SEQRES  35 A  493  ARG ASP PHE LEU THR GLU GLY PRO GLU ILE LEU ARG GLU
SEQRES  36 A  493  ALA ALA LYS ASN SNC GLY ALA LEU ARG THR ALA LEU ASP
SEQRES  37 A  493  LEU TRP LYS ASP ILE THR PHE ASN TYR THR SER THR ASP
SEQRES  38 A  493  THR SER ASP PHE VAL GLU THR PRO THR ALA ASN ILE
SEQRES   1 B  138  MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO ASP
SEQRES   2 B  138  LEU THR ASP GLU GLN ILE LYS LYS GLN ILE ASP TYR MET
SEQRES   3 B  138  ILE SER LYS LYS LEU ALA ILE GLY ILE GLU TYR THR ASN
SEQRES   4 B  138  ASP ILE HIS PRO ARG ASN SER PHE TRP GLU MET TRP GLY
SEQRES   5 B  138  LEU PRO LEU PHE GLU VAL THR ASP PRO ALA PRO VAL LEU
SEQRES   6 B  138  PHE GLU ILE ASN ALA CYS ARG LYS ALA LYS SER ASN PHE
SEQRES   7 B  138  TYR ILE LYS VAL VAL GLY PHE SER SER GLU ARG GLY ILE
SEQRES   8 B  138  GLU SER THR ILE ILE SER PHE ILE VAL ASN ARG PRO LYS
SEQRES   9 B  138  HIS GLU PRO GLY PHE ASN LEU ILE ARG GLN GLU ASP LYS
SEQRES  10 B  138  SER ARG SER ILE LYS TYR SER ILE GLN ALA TYR GLU THR
SEQRES  11 B  138  TYR LYS PRO GLU ASP GLN ARG TYR
MODRES 4F0H SNC A  181  CYS  S-NITROSO-CYSTEINE
MODRES 4F0H SNC A  460  CYS  S-NITROSO-CYSTEINE
HET    SNC  A 181       8
HET    SNC  A 460       8
HET    OXY  A 501       2
HET    PO4  A 502       5
HET    PO4  A 503       5
HETNAM     SNC S-NITROSO-CYSTEINE
HETNAM     OXY OXYGEN MOLECULE
HETNAM     PO4 PHOSPHATE ION
FORMUL   1  SNC    2(C3 H6 N2 O3 S)
FORMUL   3  OXY    O2
FORMUL   4  PO4    2(O4 P 3-)
FORMUL   6  HOH   *336(H2 O)
HELIX    1   1 ASP A   58  SER A   70  1                                  13
HELIX    2   2 VAL A   78  THR A   84  5                                   7
HELIX    3   3 ALA A   85  ARG A   90  5                                   6
HELIX    4   4 GLU A  113  PHE A  117  5                                   5
HELIX    5   5 SER A  121  GLY A  131  1                                  11
HELIX    6   6 ASN A  132  PHE A  136  5                                   5
HELIX    7   7 PRO A  150  LYS A  155  1                                   6
HELIX    8   8 THR A  162  ASP A  172  1                                  11
HELIX    9   9 SER A  190  GLY A  205  1                                  16
HELIX   10  10 ARG A  222  GLY A  242  1                                  21
HELIX   11  11 THR A  255  GLY A  270  1                                  16
HELIX   12  12 GLY A  281  ASN A  295  1                                  15
HELIX   13  13 ASN A  306  ARG A  311  1                                   6
HELIX   14  14 ASN A  318  GLY A  330  1                                  13
HELIX   15  15 ASP A  346  LEU A  359  1                                  14
HELIX   16  16 HIS A  391  GLY A  393  5                                   3
HELIX   17  17 GLN A  394  GLY A  403  1                                  10
HELIX   18  18 GLY A  411  GLY A  416  1                                   6
HELIX   19  19 GLY A  420  GLU A  441  1                                  22
HELIX   20  20 ASP A  444  ASN A  459  1                                  16
HELIX   21  21 SNC A  460  TRP A  470  1                                  11
HELIX   22  22 THR B  515  LYS B  529  1                                  15
HELIX   23  23 ASP B  560  LYS B  575  1                                  16
HELIX   24  24 GLU B  629  LYS B  632  5                                   4
HELIX   25  25 PRO B  633  ARG B  637  5                                   5
SHEET    1   A 5 LYS A  92  VAL A  99  0
SHEET    2   A 5 ASN A 102  TYR A 112 -1  O  PHE A 107   N  ASP A  97
SHEET    3   A 5 VAL A  45  PRO A  53 -1  N  VAL A  51   O  TYR A 106
SHEET    4   A 5 VAL A 139  ARG A 148 -1  O  ARG A 143   N  ARG A  50
SHEET    5   A 5 GLY A 316  MET A 317  1  O  GLY A 316   N  LEU A 144
SHEET    1   B 8 LEU A 178  SNC A 181  0
SHEET    2   B 8 VAL A 407  PHE A 410  1  O  PHE A 410   N  GLY A 180
SHEET    3   B 8 MET A 383  ALA A 386  1  N  ALA A 386   O  GLN A 409
SHEET    4   B 8 HIS A 333  HIS A 335  1  N  ILE A 334   O  MET A 383
SHEET    5   B 8 ILE A 298  HIS A 302  1  N  LEU A 301   O  HIS A 333
SHEET    6   B 8 ILE A 273  ASP A 277  1  N  ILE A 276   O  HIS A 302
SHEET    7   B 8 GLY A 246  ASN A 250  1  N  LEU A 249   O  MET A 275
SHEET    8   B 8 PHE A 208  LYS A 210  1  N  VAL A 209   O  TYR A 248
SHEET    1   C 2 LYS A 361  LEU A 362  0
SHEET    2   C 2 MET A 374  ASP A 375 -1  O  MET A 374   N  LEU A 362
SHEET    1   D 4 GLU B 549  MET B 550  0
SHEET    2   D 4 ALA B 532  THR B 538 -1  N  TYR B 537   O  GLU B 549
SHEET    3   D 4 TYR B 579  SER B 586 -1  O  LYS B 581   N  GLU B 536
SHEET    4   D 4 SER B 593  ASN B 601 -1  O  VAL B 600   N  ILE B 580
SHEET    1   E 2 PHE B 609  GLU B 615  0
SHEET    2   E 2 ILE B 621  ALA B 627 -1  O  SER B 624   N  ILE B 612
LINK         C   GLY A 180                 N   SNC A 181     1555   1555  1.33
LINK         C   SNC A 181                 N   THR A 182     1555   1555  1.33
LINK         C   ASN A 459                 N   SNC A 460     1555   1555  1.34
LINK         C   SNC A 460                 N   GLY A 461     1555   1555  1.33
CISPEP   1 LYS A  184    PRO A  185          0       -11.54
SITE     1 AC1  6 THR A 182  HIS A 302  HIS A 335  SER A 387
SITE     2 AC1  6 GLN A 409  HOH A1036
SITE     1 AC2  8 GLY A 131  ASN A 132  ARG A 303  ALA A 304
SITE     2 AC2  8 GLY A 305  ASN A 306  SER A 307  HOH A1100
SITE     1 AC3  8 TRP A  75  LYS A 184  GLY A 389  PHE A 410
SITE     2 AC3  8 GLY A 411  GLY A 412  HOH A1104  HOH A1161
CRYST1  136.440  136.440  121.670  90.00  90.00  90.00 I 4 2 2      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      0.007329  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007329  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008219        0.00000
      
PROCHECK
Go to PROCHECK summary
 References