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PDBsum entry 2pfm

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Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
2pfm
Jmol
Contents
Protein chains
434 a.a.
Ligands
MLI ×3
Waters ×508
HEADER    LYASE                                   05-APR-07   2PFM
TITLE     CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE (PURB) FROM BACILLUS
TITLE    2 ANTHRACIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ADENYLOSUCCINATE LYASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.3.2.2;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE   3 ORGANISM_TAXID: 1392;
SOURCE   4 GENE: PURB;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-YSBLIC
KEYWDS    ADENYLOSUCCINATE LYASE, PURB, PURINE BIOSYNTHESIS, BA0290, BACILLUS
KEYWDS   2 ANTHRACIS, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.M.LEVDIKOV,E.V.BLAGOVA,M.BAUMGART,O.V.MOROZ,A.J.WILKINSON,
AUTHOR   2 K.S.WILSON
REVDAT   3   13-JUL-11 2PFM    1       VERSN
REVDAT   2   24-FEB-09 2PFM    1       VERSN
REVDAT   1   17-APR-07 2PFM    0
JRNL        AUTH   V.M.LEVDIKOV,E.V.BLAGOVA,A.J.WILKINSON,K.S.WILSON
JRNL        TITL   CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE (PURB) FROM
JRNL        TITL 2 BACILLUS ANTHRACIS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.19
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 73838
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) : 0.165
REMARK   3   R VALUE            (WORKING SET) : 0.163
REMARK   3   FREE R VALUE                     : 0.208
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3909
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2641
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360
REMARK   3   BIN FREE R VALUE SET COUNT          : 167
REMARK   3   BIN FREE R VALUE                    : 0.2920
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7004
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 21
REMARK   3   SOLVENT ATOMS            : 508
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.96
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.46000
REMARK   3    B22 (A**2) : 0.46000
REMARK   3    B33 (A**2) : -0.69000
REMARK   3    B12 (A**2) : 0.23000
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): 0.376
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.026
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7172 ; 0.016 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  4900 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9688 ; 1.560 ; 1.950
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11925 ; 1.080 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   870 ; 6.551 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   349 ;37.868 ;24.040
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1320 ;17.957 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;16.883 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1071 ; 0.210 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7929 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  1443 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1811 ; 0.227 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5304 ; 0.206 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3539 ; 0.182 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3612 ; 0.092 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   428 ; 0.154 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.074 ; 0.200
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):    67 ; 0.334 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):   176 ; 0.281 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    41 ; 0.273 ; 0.200
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):  5644 ; 1.217 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1757 ; 0.293 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7000 ; 1.440 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3297 ; 2.533 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2687 ; 3.676 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 14920 ; 1.391 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   515 ; 6.644 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 11937 ; 1.777 ; 3.000
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 2PFM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-07.
REMARK 100 THE RCSB ID CODE IS RCSB042322.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.9
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00040
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : TOROIDAL MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78074
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
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                : 12.100
REMARK 200  R MERGE                    (I) : 0.12500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03
REMARK 200  COMPLETENESS FOR SHELL     (%) : 42.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.75300
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: 1C3C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, PH 6.9, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
REMARK 290       7555   Y,X,-Z+1/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+2/3
REMARK 290      10555   -Y,-X,-Z+5/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+1/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.32967
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      116.65933
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       87.49450
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      145.82417
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.16483
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.32967
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      116.65933
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      145.82417
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       87.49450
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       29.16483
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 35160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 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  0.500000 -0.866025  0.000000      -77.19050
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000     -133.69787
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -29.16483
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 B 452  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 918  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     GLY A    -8
REMARK 465     SER A    -7
REMARK 465     SER A    -6
REMARK 465     HIS A    -5
REMARK 465     HIS A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     GLY B    -8
REMARK 465     SER B    -7
REMARK 465     SER B    -6
REMARK 465     HIS B    -5
REMARK 465     HIS B    -4
REMARK 465     HIS B    -3
REMARK 465     HIS B    -2
REMARK 465     HIS B    -1
REMARK 465     HIS B     0
REMARK 465     MET B     1
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    ALA A  82      -18.53    117.47
REMARK 500    ALA A 147      -84.62   -113.10
REMARK 500    THR A 213     -141.03   -101.82
REMARK 500    ARG A 251       58.32     39.11
REMARK 500    HIS A 301     -123.43     54.83
REMARK 500    ARG A 303      152.78    148.99
REMARK 500    SER B   3      -28.80   -150.40
REMARK 500    ALA B 147      -91.01   -113.34
REMARK 500    THR B 213     -127.42   -103.87
REMARK 500    HIS B 301     -127.34     50.36
REMARK 500    ARG B 303      151.91    149.06
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 ILE B    2     SER B    3                  -70.44
REMARK 500 SER B    3     ARG B    4                  147.63
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 A1036        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH A1112        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH B 570        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH B 658        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH B 664        DISTANCE =  5.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 903
DBREF  2PFM A    1   435  UNP    Q81ZH6   Q81ZH6_BACAN     1    435
DBREF  2PFM B    1   435  UNP    Q81ZH6   Q81ZH6_BACAN     1    435
SEQADV 2PFM GLY A   -8  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM SER A   -7  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM SER A   -6  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS A   -5  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS A   -4  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS A   -3  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS A   -2  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS A   -1  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS A    0  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM GLY B   -8  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM SER B   -7  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM SER B   -6  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS B   -5  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS B   -4  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS B   -3  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS B   -2  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS B   -1  UNP  Q81ZH6              CLONING ARTIFACT
SEQADV 2PFM HIS B    0  UNP  Q81ZH6              CLONING ARTIFACT
SEQRES   1 A  444  GLY SER SER HIS HIS HIS HIS HIS HIS MET ILE SER ARG
SEQRES   2 A  444  TYR THR ARG PRO GLU MET GLY ALA ILE TRP THR GLU GLU
SEQRES   3 A  444  ASN LYS PHE LYS ALA TRP LEU GLU VAL GLU ILE LEU ALA
SEQRES   4 A  444  CYS GLU ALA TRP ALA GLU LEU GLY ASP ILE PRO LYS GLU
SEQRES   5 A  444  ASP VAL LYS LYS ILE ARG GLU HIS ALA SER PHE ASP ILE
SEQRES   6 A  444  ASP ARG ILE TYR GLU ILE GLU LYS GLU THR ARG HIS ASP
SEQRES   7 A  444  VAL VAL ALA PHE THR ARG ALA VAL SER GLU THR PRO ALA
SEQRES   8 A  444  LEU GLY GLU GLU ARG LYS TRP VAL HIS TYR GLY LEU THR
SEQRES   9 A  444  SER THR ASP VAL VAL ASP THR ALA LEU SER TYR ILE LEU
SEQRES  10 A  444  LYS GLN ALA ASN GLU ILE ILE LEU LYS ASP LEU GLU ASN
SEQRES  11 A  444  PHE VAL SER ILE LEU ALA ASN LYS ALA LYS GLU HIS LYS
SEQRES  12 A  444  TYR THR ILE MET MET GLY ARG THR HIS GLY VAL HIS ALA
SEQRES  13 A  444  GLU PRO THR THR PHE GLY LEU LYS LEU GLY LEU TRP TYR
SEQRES  14 A  444  GLU GLU MET LYS ARG ASN VAL GLU ARG PHE LYS GLN ALA
SEQRES  15 A  444  ALA ASN THR VAL ARG VAL GLY LYS LEU SER GLY ALA VAL
SEQRES  16 A  444  GLY THR TYR ALA ASN ILE ASP PRO PHE VAL GLU LYS TYR
SEQRES  17 A  444  VAL CYS GLU ASN LEU GLY LEU GLU ALA ALA PRO ILE SER
SEQRES  18 A  444  THR GLN THR LEU GLN ARG ASP ARG HIS ALA HIS TYR MET
SEQRES  19 A  444  SER THR LEU ALA LEU ILE ALA THR SER ILE GLU LYS MET
SEQRES  20 A  444  ALA VAL GLU ILE ARG GLY LEU GLN LYS SER GLU THR ARG
SEQRES  21 A  444  GLU VAL GLU GLU ALA PHE ALA LYS GLY GLN LYS GLY SER
SEQRES  22 A  444  SER ALA MET PRO HIS LYS ARG ASN PRO ILE GLY SER GLU
SEQRES  23 A  444  ASN MET THR GLY LEU ALA ARG VAL ILE ARG GLY TYR MET
SEQRES  24 A  444  MET THR ALA TYR GLU ASN VAL PRO LEU TRP HIS GLU ARG
SEQRES  25 A  444  ASP ILE SER HIS SER SER ALA GLU ARG VAL ILE LEU PRO
SEQRES  26 A  444  ASP ALA THR ILE ALA LEU ASN TYR MET LEU ASN ARG PHE
SEQRES  27 A  444  GLY ASN ILE VAL LYS ASN LEU THR VAL TYR PRO GLU ASN
SEQRES  28 A  444  MET LYS ARG ASN MET THR ARG THR TYR GLY LEU ILE TYR
SEQRES  29 A  444  SER GLN ARG VAL MET LEU THR LEU ILE ASP LYS GLY MET
SEQRES  30 A  444  VAL ARG GLU GLU ALA TYR ASP ILE VAL GLN PRO LYS ALA
SEQRES  31 A  444  MET GLU ALA TRP GLU THR GLN VAL GLN PHE LYS GLU LEU
SEQRES  32 A  444  VAL GLU ALA ASP GLU ARG ILE THR SER LYS LEU THR GLN
SEQRES  33 A  444  GLU GLU ILE ASN GLU CYS PHE ASN TYR GLU HIS HIS MET
SEQRES  34 A  444  GLN HIS VAL ASP THR ILE PHE GLU ARG LEU GLY LEU ASN
SEQRES  35 A  444  GLU ALA
SEQRES   1 B  444  GLY SER SER HIS HIS HIS HIS HIS HIS MET ILE SER ARG
SEQRES   2 B  444  TYR THR ARG PRO GLU MET GLY ALA ILE TRP THR GLU GLU
SEQRES   3 B  444  ASN LYS PHE LYS ALA TRP LEU GLU VAL GLU ILE LEU ALA
SEQRES   4 B  444  CYS GLU ALA TRP ALA GLU LEU GLY ASP ILE PRO LYS GLU
SEQRES   5 B  444  ASP VAL LYS LYS ILE ARG GLU HIS ALA SER PHE ASP ILE
SEQRES   6 B  444  ASP ARG ILE TYR GLU ILE GLU LYS GLU THR ARG HIS ASP
SEQRES   7 B  444  VAL VAL ALA PHE THR ARG ALA VAL SER GLU THR PRO ALA
SEQRES   8 B  444  LEU GLY GLU GLU ARG LYS TRP VAL HIS TYR GLY LEU THR
SEQRES   9 B  444  SER THR ASP VAL VAL ASP THR ALA LEU SER TYR ILE LEU
SEQRES  10 B  444  LYS GLN ALA ASN GLU ILE ILE LEU LYS ASP LEU GLU ASN
SEQRES  11 B  444  PHE VAL SER ILE LEU ALA ASN LYS ALA LYS GLU HIS LYS
SEQRES  12 B  444  TYR THR ILE MET MET GLY ARG THR HIS GLY VAL HIS ALA
SEQRES  13 B  444  GLU PRO THR THR PHE GLY LEU LYS LEU GLY LEU TRP TYR
SEQRES  14 B  444  GLU GLU MET LYS ARG ASN VAL GLU ARG PHE LYS GLN ALA
SEQRES  15 B  444  ALA ASN THR VAL ARG VAL GLY LYS LEU SER GLY ALA VAL
SEQRES  16 B  444  GLY THR TYR ALA ASN ILE ASP PRO PHE VAL GLU LYS TYR
SEQRES  17 B  444  VAL CYS GLU ASN LEU GLY LEU GLU ALA ALA PRO ILE SER
SEQRES  18 B  444  THR GLN THR LEU GLN ARG ASP ARG HIS ALA HIS TYR MET
SEQRES  19 B  444  SER THR LEU ALA LEU ILE ALA THR SER ILE GLU LYS MET
SEQRES  20 B  444  ALA VAL GLU ILE ARG GLY LEU GLN LYS SER GLU THR ARG
SEQRES  21 B  444  GLU VAL GLU GLU ALA PHE ALA LYS GLY GLN LYS GLY SER
SEQRES  22 B  444  SER ALA MET PRO HIS LYS ARG ASN PRO ILE GLY SER GLU
SEQRES  23 B  444  ASN MET THR GLY LEU ALA ARG VAL ILE ARG GLY TYR MET
SEQRES  24 B  444  MET THR ALA TYR GLU ASN VAL PRO LEU TRP HIS GLU ARG
SEQRES  25 B  444  ASP ILE SER HIS SER SER ALA GLU ARG VAL ILE LEU PRO
SEQRES  26 B  444  ASP ALA THR ILE ALA LEU ASN TYR MET LEU ASN ARG PHE
SEQRES  27 B  444  GLY ASN ILE VAL LYS ASN LEU THR VAL TYR PRO GLU ASN
SEQRES  28 B  444  MET LYS ARG ASN MET THR ARG THR TYR GLY LEU ILE TYR
SEQRES  29 B  444  SER GLN ARG VAL MET LEU THR LEU ILE ASP LYS GLY MET
SEQRES  30 B  444  VAL ARG GLU GLU ALA TYR ASP ILE VAL GLN PRO LYS ALA
SEQRES  31 B  444  MET GLU ALA TRP GLU THR GLN VAL GLN PHE LYS GLU LEU
SEQRES  32 B  444  VAL GLU ALA ASP GLU ARG ILE THR SER LYS LEU THR GLN
SEQRES  33 B  444  GLU GLU ILE ASN GLU CYS PHE ASN TYR GLU HIS HIS MET
SEQRES  34 B  444  GLN HIS VAL ASP THR ILE PHE GLU ARG LEU GLY LEU ASN
SEQRES  35 B  444  GLU ALA
HET    MLI  A 901       7
HET    MLI  A 902       7
HET    MLI  A 903       7
HETNAM     MLI MALONATE ION
FORMUL   3  MLI    3(C3 H2 O4 2-)
FORMUL   6  HOH   *508(H2 O)
HELIX    1   1 ARG A    7  TRP A   14  1                                   8
HELIX    2   2 THR A   15  LEU A   37  1                                  23
HELIX    3   3 PRO A   41  ALA A   52  1                                  12
HELIX    4   4 ASP A   55  ARG A   67  1                                  13
HELIX    5   5 HIS A   68  GLU A   79  1                                  12
HELIX    6   6 GLY A   84  VAL A   90  5                                   7
HELIX    7   7 THR A   95  HIS A  133  1                                  39
HELIX    8   8 PHE A  152  VAL A  177  1                                  26
HELIX    9   9 ASP A  193  LEU A  204  1                                  12
HELIX   10  10 ARG A  218  GLN A  246  1                                  29
HELIX   11  11 PRO A  273  ASN A  296  1                                  24
HELIX   12  12 ILE A  305  ASN A  335  1                                  31
HELIX   13  13 TYR A  339  THR A  348  1                                  10
HELIX   14  14 GLY A  352  ILE A  354  5                                   3
HELIX   15  15 TYR A  355  LYS A  366  1                                  12
HELIX   16  16 VAL A  369  GLN A  388  1                                  20
HELIX   17  17 GLN A  390  ALA A  397  1                                   8
HELIX   18  18 ASP A  398  SER A  403  1                                   6
HELIX   19  19 THR A  406  PHE A  414  1                                   9
HELIX   20  20 ASN A  415  GLN A  421  5                                   7
HELIX   21  21 HIS A  422  GLY A  431  1                                  10
HELIX   22  22 ARG B    7  TRP B   14  1                                   8
HELIX   23  23 THR B   15  GLY B   38  1                                  24
HELIX   24  24 PRO B   41  ALA B   52  1                                  12
HELIX   25  25 ASP B   55  ARG B   67  1                                  13
HELIX   26  26 HIS B   68  GLU B   79  1                                  12
HELIX   27  27 GLY B   84  VAL B   90  5                                   7
HELIX   28  28 THR B   95  HIS B  133  1                                  39
HELIX   29  29 PHE B  152  VAL B  177  1                                  26
HELIX   30  30 ASP B  193  LEU B  204  1                                  12
HELIX   31  31 ARG B  218  GLN B  246  1                                  29
HELIX   32  32 PRO B  273  ASN B  296  1                                  24
HELIX   33  33 ILE B  305  ASN B  335  1                                  31
HELIX   34  34 TYR B  339  THR B  348  1                                  10
HELIX   35  35 GLY B  352  ILE B  354  5                                   3
HELIX   36  36 TYR B  355  LYS B  366  1                                  12
HELIX   37  37 VAL B  369  GLN B  388  1                                  20
HELIX   38  38 GLN B  390  ALA B  397  1                                   8
HELIX   39  39 ASP B  398  SER B  403  1                                   6
HELIX   40  40 THR B  406  PHE B  414  1                                   9
HELIX   41  41 ASN B  415  GLN B  421  5                                   7
HELIX   42  42 HIS B  422  GLY B  431  1                                  10
SHEET    1   A 2 ILE A 137  THR A 142  0
SHEET    2   A 2 VAL A 145  THR A 151 -1  O  THR A 150   N  MET A 138
SHEET    1   B 2 VAL A 179  GLY A 180  0
SHEET    2   B 2 GLU A 207  ALA A 208  1  O  GLU A 207   N  GLY A 180
SHEET    1   C 2 VAL A 253  GLU A 254  0
SHEET    2   C 2 THR A 337  VAL A 338 -1  O  THR A 337   N  GLU A 254
SHEET    1   D 2 ILE B 137  THR B 142  0
SHEET    2   D 2 VAL B 145  THR B 151 -1  O  THR B 150   N  MET B 138
SHEET    1   E 2 VAL B 179  GLY B 180  0
SHEET    2   E 2 GLU B 207  ALA B 208  1  O  GLU B 207   N  GLY B 180
SHEET    1   F 2 VAL B 253  GLU B 254  0
SHEET    2   F 2 THR B 337  VAL B 338 -1  O  THR B 337   N  GLU B 254
CISPEP   1 ILE A    2    SER A    3          0        19.95
SITE     1 AC1 11 THR A 142  HIS A 143  HIS B  68  SER B  96
SITE     2 AC1 11 GLN B 214  GLY B 263  SER B 264  MET B 267
SITE     3 AC1 11 LYS B 270  ASN B 272  HOH B 649
SITE     1 AC2 10 HIS A  68  SER A  96  GLN A 214  GLY A 263
SITE     2 AC2 10 SER A 264  MET A 267  LYS A 270  ASN A 272
SITE     3 AC2 10 THR B 142  HIS B 143
SITE     1 AC3  6 GLN A 110  HOH A 951  HOH A 991  HOH A1090
SITE     2 AC3  6 HOH B 616  HOH B 634
CRYST1  154.381  154.381  174.989  90.00  90.00 120.00 P 61 2 2     24
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      0.006477  0.003740  0.000000        0.00000
SCALE2      0.000000  0.007480  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005715        0.00000
      
PROCHECK
Go to PROCHECK summary
 References