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PDBsum entry 3nav

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Lyase PDB id
3nav
Jmol
Contents
Protein chains
261 a.a.
Ligands
EDO
Waters ×381
HEADER    LYASE                                   02-JUN-10   3NAV
TITLE     CRYSTAL STRUCTURE OF AN ALPHA SUBUNIT OF TRYPTOPHAN SYNTHASE FROM
TITLE    2 VIBRIO CHOLERAE O1 BIOVAR EL TOR STR. N16961
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.2.1.20;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE O1 BIOVAR EL TOR;
SOURCE   3 ORGANISM_TAXID: 243277;
SOURCE   4 STRAIN: N16961;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS    TRYPTOPHAN SYNTHASE, ALPHA SUBUNIT, STRUCTURAL GENOMICS, CSGID,
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.NOCEK,M.MAKOWSKA-GRZYSKA,K.KWON,A.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT   2   01-OCT-14 3NAV    1       VERSN  AUTHOR
REVDAT   1   30-JUN-10 3NAV    0
JRNL        AUTH   B.NOCEK,M.MAKOWSKA-GRZYSKA,K.KWON,W.ANDERSON,A.JOACHIMIAK,
JRNL        AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL        AUTH 3 (CSGID)
JRNL        TITL   CRYSTAL STRUCTURE OF AN ALPHA SUBUNIT OF TRYPTOPHAN SYNTHASE
JRNL        TITL 2 FROM VIBRIO CHOLERAE O1 BIOVAR EL TOR STR. N16961
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.10 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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 27827
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) : 0.182
REMARK   3   R VALUE            (WORKING SET) : 0.179
REMARK   3   FREE R VALUE                     : 0.233
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1491
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2028
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.58
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1930
REMARK   3   BIN FREE R VALUE SET COUNT          : 104
REMARK   3   BIN FREE R VALUE                    : 0.2770
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3882
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 4
REMARK   3   SOLVENT ATOMS            : 381
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 31.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.31
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.91000
REMARK   3    B22 (A**2) : -1.00000
REMARK   3    B33 (A**2) : 0.09000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.196
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.134
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.182
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3965 ; 0.020 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  2634 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5396 ; 1.668 ; 1.979
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6483 ; 1.170 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   517 ; 6.231 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;37.029 ;25.273
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   632 ;14.876 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;20.284 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   628 ; 0.097 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4456 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   731 ; 0.001 ; 0.020
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):  2597 ; 1.030 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1034 ; 0.201 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4157 ; 1.889 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1368 ; 2.645 ; 3.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1238 ; 4.429 ; 4.500
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER 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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 30
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     0        A     4
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7165  17.6073  18.5461
REMARK   3    T TENSOR
REMARK   3      T11:   0.4348 T22:   0.1272
REMARK   3      T33:   0.1986 T12:  -0.0226
REMARK   3      T13:   0.0623 T23:  -0.0151
REMARK   3    L TENSOR
REMARK   3      L11:   5.2696 L22:   0.3159
REMARK   3      L33:   2.2062 L12:   0.5861
REMARK   3      L13:   3.5762 L23:  -0.5421
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0953 S12:   0.1292 S13:   0.3951
REMARK   3      S21:  -0.0729 S22:  -0.0478 S23:   0.1078
REMARK   3      S31:  -0.0506 S32:   0.2334 S33:   0.1431
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     5        A    21
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1701  10.3718  14.2814
REMARK   3    T TENSOR
REMARK   3      T11:   0.2609 T22:   0.2033
REMARK   3      T33:   0.1972 T12:   0.0055
REMARK   3      T13:  -0.0043 T23:  -0.0005
REMARK   3    L TENSOR
REMARK   3      L11:   0.7552 L22:   2.5201
REMARK   3      L33:   1.5979 L12:  -0.1566
REMARK   3      L13:   0.3761 L23:  -1.7015
REMARK   3    S TENSOR
REMARK   3      S11:   0.0385 S12:  -0.0160 S13:   0.0292
REMARK   3      S21:  -0.2394 S22:   0.0239 S23:   0.0975
REMARK   3      S31:  -0.0165 S32:  -0.0994 S33:  -0.0624
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    22        A    48
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9746  -1.8249  24.4572
REMARK   3    T TENSOR
REMARK   3      T11:   0.2096 T22:   0.2115
REMARK   3      T33:   0.2038 T12:   0.0085
REMARK   3      T13:   0.0016 T23:  -0.0057
REMARK   3    L TENSOR
REMARK   3      L11:   0.5274 L22:   1.0091
REMARK   3      L33:   1.0616 L12:   0.1307
REMARK   3      L13:   0.3464 L23:  -0.2778
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0105 S12:   0.0694 S13:   0.0070
REMARK   3      S21:  -0.0204 S22:  -0.0320 S23:  -0.0933
REMARK   3      S31:   0.0854 S32:   0.1017 S33:   0.0425
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    49        A    64
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6035  -0.3579  39.8796
REMARK   3    T TENSOR
REMARK   3      T11:   0.2174 T22:   0.2260
REMARK   3      T33:   0.2096 T12:   0.0078
REMARK   3      T13:  -0.0115 T23:   0.0200
REMARK   3    L TENSOR
REMARK   3      L11:   0.6982 L22:   0.6814
REMARK   3      L33:   0.4433 L12:  -0.0409
REMARK   3      L13:  -0.7716 L23:   0.3228
REMARK   3    S TENSOR
REMARK   3      S11:   0.0166 S12:  -0.0086 S13:   0.0379
REMARK   3      S21:   0.0841 S22:   0.0192 S23:  -0.0027
REMARK   3      S31:   0.0060 S32:  -0.0314 S33:  -0.0358
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    65        A    82
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1149  -1.3012  37.3743
REMARK   3    T TENSOR
REMARK   3      T11:   0.2010 T22:   0.2118
REMARK   3      T33:   0.2065 T12:   0.0084
REMARK   3      T13:  -0.0010 T23:  -0.0019
REMARK   3    L TENSOR
REMARK   3      L11:   0.4657 L22:   1.1855
REMARK   3      L33:   0.2824 L12:   0.3192
REMARK   3      L13:   0.3023 L23:  -0.0660
REMARK   3    S TENSOR
REMARK   3      S11:   0.0089 S12:  -0.0584 S13:  -0.0483
REMARK   3      S21:   0.0260 S22:  -0.0147 S23:  -0.0518
REMARK   3      S31:   0.0136 S32:  -0.0069 S33:   0.0059
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    83        A    97
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6324   6.9624  21.3382
REMARK   3    T TENSOR
REMARK   3      T11:   0.2027 T22:   0.2579
REMARK   3      T33:   0.2042 T12:   0.0081
REMARK   3      T13:   0.0363 T23:   0.0044
REMARK   3    L TENSOR
REMARK   3      L11:   0.4889 L22:   1.3221
REMARK   3      L33:   1.0688 L12:   1.0113
REMARK   3      L13:  -0.4040 L23:   0.4622
REMARK   3    S TENSOR
REMARK   3      S11:   0.0088 S12:   0.0270 S13:  -0.0340
REMARK   3      S21:  -0.0882 S22:   0.0316 S23:  -0.1039
REMARK   3      S31:  -0.0662 S32:   0.1142 S33:  -0.0404
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    98        A   120
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4233  13.3881  36.6816
REMARK   3    T TENSOR
REMARK   3      T11:   0.2187 T22:   0.1998
REMARK   3      T33:   0.2046 T12:   0.0025
REMARK   3      T13:   0.0020 T23:   0.0010
REMARK   3    L TENSOR
REMARK   3      L11:   0.7650 L22:   0.9001
REMARK   3      L33:   1.0456 L12:   0.3238
REMARK   3      L13:   0.3426 L23:   0.2867
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0114 S12:  -0.0541 S13:   0.0145
REMARK   3      S21:   0.0277 S22:  -0.0032 S23:  -0.0609
REMARK   3      S31:  -0.0202 S32:  -0.0159 S33:   0.0146
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   121        A   142
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0984  17.4874  36.1836
REMARK   3    T TENSOR
REMARK   3      T11:   0.2246 T22:   0.1960
REMARK   3      T33:   0.2031 T12:   0.0067
REMARK   3      T13:   0.0088 T23:   0.0052
REMARK   3    L TENSOR
REMARK   3      L11:   0.9820 L22:   0.4192
REMARK   3      L33:   1.2013 L12:  -0.0328
REMARK   3      L13:  -0.6277 L23:  -0.1152
REMARK   3    S TENSOR
REMARK   3      S11:   0.0256 S12:   0.0237 S13:   0.0099
REMARK   3      S21:   0.0726 S22:   0.0140 S23:  -0.0138
REMARK   3      S31:  -0.0489 S32:  -0.0904 S33:  -0.0397
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   143        A   153
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0097  19.5537  30.6690
REMARK   3    T TENSOR
REMARK   3      T11:   0.2301 T22:   0.2105
REMARK   3      T33:   0.2137 T12:   0.0042
REMARK   3      T13:  -0.0033 T23:   0.0092
REMARK   3    L TENSOR
REMARK   3      L11:   9.6221 L22:   1.1558
REMARK   3      L33:  -0.1202 L12:   3.7730
REMARK   3      L13:  -0.7510 L23:  -0.0020
REMARK   3    S TENSOR
REMARK   3      S11:   0.0230 S12:  -0.1713 S13:   0.2013
REMARK   3      S21:  -0.0225 S22:  -0.0462 S23:   0.1282
REMARK   3      S31:  -0.0351 S32:   0.0336 S33:   0.0232
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   154        A   173
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6359  20.3880  32.5312
REMARK   3    T TENSOR
REMARK   3      T11:   0.2010 T22:   0.2047
REMARK   3      T33:   0.2106 T12:   0.0095
REMARK   3      T13:  -0.0396 T23:   0.0169
REMARK   3    L TENSOR
REMARK   3      L11:   3.9158 L22:   3.2007
REMARK   3      L33:   2.3573 L12:  -2.2430
REMARK   3      L13:  -3.0532 L23:   1.5275
REMARK   3    S TENSOR
REMARK   3      S11:   0.0788 S12:  -0.0547 S13:   0.0505
REMARK   3      S21:  -0.0109 S22:  -0.0465 S23:  -0.0415
REMARK   3      S31:   0.0403 S32:  -0.0692 S33:  -0.0323
REMARK   3
REMARK   3   TLS GROUP : 11
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   174        A   193
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.3060   8.3072  30.1621
REMARK   3    T TENSOR
REMARK   3      T11:   0.3549 T22:   0.3868
REMARK   3      T33:   0.4232 T12:  -0.2971
REMARK   3      T13:  -0.0540 T23:  -0.0269
REMARK   3    L TENSOR
REMARK   3      L11:  -1.7639 L22:  -3.3511
REMARK   3      L33:   3.1988 L12:  -3.2112
REMARK   3      L13:  -0.8133 L23:   2.7612
REMARK   3    S TENSOR
REMARK   3      S11:   0.4942 S12:  -0.5707 S13:   0.5576
REMARK   3      S21:   0.0015 S22:  -0.0284 S23:  -0.0463
REMARK   3      S31:   0.9667 S32:  -0.3466 S33:  -0.4658
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   194        A   211
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9654  17.2483  25.4422
REMARK   3    T TENSOR
REMARK   3      T11:   0.1981 T22:   0.2432
REMARK   3      T33:   0.2047 T12:  -0.0018
REMARK   3      T13:  -0.0463 T23:   0.0151
REMARK   3    L TENSOR
REMARK   3      L11:   2.0254 L22:   4.8228
REMARK   3      L33:   1.0550 L12:  -1.1494
REMARK   3      L13:  -0.3146 L23:  -0.0127
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0164 S12:   0.2065 S13:   0.0897
REMARK   3      S21:  -0.2923 S22:   0.0878 S23:   0.3048
REMARK   3      S31:   0.1196 S32:  -0.1788 S33:  -0.0714
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   212        A   235
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5714   2.2871  22.8498
REMARK   3    T TENSOR
REMARK   3      T11:   0.2059 T22:   0.2170
REMARK   3      T33:   0.1946 T12:   0.0065
REMARK   3      T13:  -0.0025 T23:  -0.0014
REMARK   3    L TENSOR
REMARK   3      L11:  -0.1913 L22:   3.6534
REMARK   3      L33:   1.5457 L12:   0.2507
REMARK   3      L13:  -0.0148 L23:   0.8461
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0084 S12:   0.0085 S13:  -0.0503
REMARK   3      S21:  -0.1296 S22:  -0.0226 S23:   0.0442
REMARK   3      S31:  -0.0350 S32:  -0.1320 S33:   0.0310
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   236        A   250
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1928 -12.3611  27.6759
REMARK   3    T TENSOR
REMARK   3      T11:   0.2458 T22:   0.1743
REMARK   3      T33:   0.2363 T12:   0.0053
REMARK   3      T13:  -0.0291 T23:  -0.0056
REMARK   3    L TENSOR
REMARK   3      L11:   3.6745 L22:   1.9926
REMARK   3      L33:   1.8949 L12:  -1.3368
REMARK   3      L13:  -1.0626 L23:  -0.0220
REMARK   3    S TENSOR
REMARK   3      S11:   0.0761 S12:  -0.1609 S13:  -0.3137
REMARK   3      S21:  -0.0670 S22:  -0.0514 S23:   0.0223
REMARK   3      S31:   0.2834 S32:   0.0029 S33:  -0.0247
REMARK   3
REMARK   3   TLS GROUP : 15
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   251        A   268
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2162  -4.9690  16.9316
REMARK   3    T TENSOR
REMARK   3      T11:   0.2580 T22:   0.1888
REMARK   3      T33:   0.2033 T12:   0.0024
REMARK   3      T13:  -0.0169 T23:  -0.0290
REMARK   3    L TENSOR
REMARK   3      L11:   2.9963 L22:   2.3445
REMARK   3      L33:   0.7148 L12:  -1.7272
REMARK   3      L13:   0.0808 L23:  -0.5921
REMARK   3    S TENSOR
REMARK   3      S11:   0.1069 S12:   0.0896 S13:  -0.0749
REMARK   3      S21:  -0.2156 S22:  -0.0337 S23:   0.0455
REMARK   3      S31:   0.1606 S32:  -0.0666 S33:  -0.0732
REMARK   3
REMARK   3   TLS GROUP : 16
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     0        B     8
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5988   2.5995  73.2768
REMARK   3    T TENSOR
REMARK   3      T11:   0.2372 T22:   0.2461
REMARK   3      T33:   0.2341 T12:  -0.0048
REMARK   3      T13:  -0.0337 T23:  -0.0281
REMARK   3    L TENSOR
REMARK   3      L11:   0.9288 L22:   4.9177
REMARK   3      L33:   1.5932 L12:  -0.8595
REMARK   3      L13:  -1.7976 L23:  -1.7834
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0608 S12:  -0.1352 S13:   0.1832
REMARK   3      S21:   0.3047 S22:   0.0131 S23:  -0.3634
REMARK   3      S31:  -0.0133 S32:   0.0784 S33:   0.0477
REMARK   3
REMARK   3   TLS GROUP : 17
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     9        B    15
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6634  -6.1275  78.3317
REMARK   3    T TENSOR
REMARK   3      T11:   0.2390 T22:   0.2222
REMARK   3      T33:   0.1832 T12:   0.0132
REMARK   3      T13:  -0.0034 T23:   0.0194
REMARK   3    L TENSOR
REMARK   3      L11:   2.5716 L22:   3.3468
REMARK   3      L33:   5.5539 L12:   2.4323
REMARK   3      L13:   3.4870 L23:   1.2774
REMARK   3    S TENSOR
REMARK   3      S11:   0.1497 S12:  -0.0219 S13:  -0.0689
REMARK   3      S21:   0.0139 S22:   0.1351 S23:  -0.1864
REMARK   3      S31:  -0.0381 S32:  -0.1109 S33:  -0.2848
REMARK   3
REMARK   3   TLS GROUP : 18
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    16        B    52
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3323   5.8184  63.7419
REMARK   3    T TENSOR
REMARK   3      T11:   0.2147 T22:   0.2026
REMARK   3      T33:   0.1954 T12:  -0.0025
REMARK   3      T13:   0.0076 T23:  -0.0031
REMARK   3    L TENSOR
REMARK   3      L11:   0.5468 L22:   0.7377
REMARK   3      L33:   0.8583 L12:  -0.2620
REMARK   3      L13:   0.3971 L23:  -0.4936
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0347 S12:  -0.0195 S13:   0.0018
REMARK   3      S21:   0.0650 S22:   0.0413 S23:   0.0230
REMARK   3      S31:  -0.0417 S32:  -0.0900 S33:  -0.0065
REMARK   3
REMARK   3   TLS GROUP : 19
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    53        B    64
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0768   5.5185  44.6428
REMARK   3    T TENSOR
REMARK   3      T11:   0.2283 T22:   0.2253
REMARK   3      T33:   0.2183 T12:   0.0036
REMARK   3      T13:  -0.0107 T23:  -0.0002
REMARK   3    L TENSOR
REMARK   3      L11:   0.6146 L22:   0.3813
REMARK   3      L33:   1.1170 L12:   0.2915
REMARK   3      L13:   0.1347 L23:   0.8174
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0146 S12:   0.0742 S13:  -0.0303
REMARK   3      S21:   0.0639 S22:   0.0349 S23:  -0.0583
REMARK   3      S31:   0.0574 S32:   0.0576 S33:  -0.0203
REMARK   3
REMARK   3   TLS GROUP : 20
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    65        B    80
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6176  14.1116  51.2288
REMARK   3    T TENSOR
REMARK   3      T11:   0.2306 T22:   0.2117
REMARK   3      T33:   0.1946 T12:   0.0018
REMARK   3      T13:   0.0012 T23:   0.0030
REMARK   3    L TENSOR
REMARK   3      L11:   1.6402 L22:   1.2238
REMARK   3      L33:   0.3233 L12:   0.4159
REMARK   3      L13:   0.7716 L23:  -0.2360
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0648 S12:   0.1828 S13:  -0.0524
REMARK   3      S21:  -0.1062 S22:   0.1138 S23:   0.0377
REMARK   3      S31:  -0.0424 S32:   0.0649 S33:  -0.0490
REMARK   3
REMARK   3   TLS GROUP : 21
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    81        B    95
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8555  13.8693  68.6986
REMARK   3    T TENSOR
REMARK   3      T11:   0.2352 T22:   0.2178
REMARK   3      T33:   0.1884 T12:   0.0077
REMARK   3      T13:   0.0033 T23:  -0.0066
REMARK   3    L TENSOR
REMARK   3      L11:   1.3480 L22:   1.3379
REMARK   3      L33:   1.2454 L12:  -0.0944
REMARK   3      L13:  -0.5980 L23:   0.3286
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0350 S12:  -0.0846 S13:   0.0506
REMARK   3      S21:   0.1196 S22:   0.0907 S23:   0.0740
REMARK   3      S31:  -0.1310 S32:  -0.0751 S33:  -0.0557
REMARK   3
REMARK   3   TLS GROUP : 22
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    96        B   127
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5353  13.3334  58.0140
REMARK   3    T TENSOR
REMARK   3      T11:   0.2137 T22:   0.2190
REMARK   3      T33:   0.1823 T12:  -0.0127
REMARK   3      T13:  -0.0098 T23:  -0.0102
REMARK   3    L TENSOR
REMARK   3      L11:   1.0411 L22:   0.7851
REMARK   3      L33:   0.9286 L12:   0.0986
REMARK   3      L13:  -0.3267 L23:  -0.3637
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0299 S12:  -0.0251 S13:   0.0068
REMARK   3      S21:   0.0123 S22:  -0.0085 S23:  -0.0303
REMARK   3      S31:  -0.0885 S32:   0.0947 S33:   0.0384
REMARK   3
REMARK   3   TLS GROUP : 23
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   128        B   143
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9757   6.2868  53.0824
REMARK   3    T TENSOR
REMARK   3      T11:   0.1900 T22:   0.2833
REMARK   3      T33:   0.1869 T12:   0.0036
REMARK   3      T13:  -0.0215 T23:  -0.0052
REMARK   3    L TENSOR
REMARK   3      L11:   2.3206 L22:   1.2967
REMARK   3      L33:   2.0460 L12:   0.2881
REMARK   3      L13:   0.7566 L23:   0.8665
REMARK   3    S TENSOR
REMARK   3      S11:   0.0008 S12:   0.2933 S13:  -0.0211
REMARK   3      S21:   0.0300 S22:   0.1427 S23:  -0.0472
REMARK   3      S31:   0.0602 S32:   0.4334 S33:  -0.1435
REMARK   3
REMARK   3   TLS GROUP : 24
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   144        B   155
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5239   5.9049  60.9693
REMARK   3    T TENSOR
REMARK   3      T11:   0.1929 T22:   0.2696
REMARK   3      T33:   0.1614 T12:   0.0093
REMARK   3      T13:  -0.0294 T23:   0.0260
REMARK   3    L TENSOR
REMARK   3      L11:   2.4274 L22:   9.0380
REMARK   3      L33:   1.9377 L12:   2.8281
REMARK   3      L13:   0.5601 L23:   1.9587
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0295 S12:  -0.0606 S13:  -0.1409
REMARK   3      S21:   0.1396 S22:  -0.0097 S23:  -0.1318
REMARK   3      S31:   0.1152 S32:   0.3213 S33:   0.0391
REMARK   3
REMARK   3   TLS GROUP : 25
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   156        B   170
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1479  -6.1654  56.5572
REMARK   3    T TENSOR
REMARK   3      T11:   0.0701 T22:   0.3426
REMARK   3      T33:   0.5967 T12:   0.2944
REMARK   3      T13:   0.1654 T23:   0.2312
REMARK   3    L TENSOR
REMARK   3      L11:  -2.6027 L22:  19.3443
REMARK   3      L33:   3.4694 L12:   0.9825
REMARK   3      L13:  -7.1949 L23:  -4.8245
REMARK   3    S TENSOR
REMARK   3      S11:  -0.6423 S12:  -1.0185 S13:  -0.6811
REMARK   3      S21:  -1.7051 S22:  -1.4730 S23:  -0.8249
REMARK   3      S31:   0.0712 S32:   1.0623 S33:   2.1153
REMARK   3
REMARK   3   TLS GROUP : 26
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   171        B   180
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4776  -5.3664  60.0243
REMARK   3    T TENSOR
REMARK   3      T11:   0.2107 T22:   0.2109
REMARK   3      T33:   0.2494 T12:   0.0332
REMARK   3      T13:  -0.0055 T23:  -0.0090
REMARK   3    L TENSOR
REMARK   3      L11:   0.5661 L22:   1.1345
REMARK   3      L33:   2.7426 L12:   0.1208
REMARK   3      L13:  -0.3112 L23:  -1.3376
REMARK   3    S TENSOR
REMARK   3      S11:   0.0408 S12:   0.1212 S13:  -0.1527
REMARK   3      S21:  -0.0555 S22:  -0.0203 S23:   0.0013
REMARK   3      S31:   0.0845 S32:   0.0986 S33:  -0.0205
REMARK   3
REMARK   3   TLS GROUP : 27
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   192        B   204
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8433 -13.9338  62.2115
REMARK   3    T TENSOR
REMARK   3      T11:   0.5875 T22:   0.0568
REMARK   3      T33:   0.3257 T12:   0.4914
REMARK   3      T13:   0.2307 T23:   0.0722
REMARK   3    L TENSOR
REMARK   3      L11:  16.9483 L22:  13.6652
REMARK   3      L33:   8.7507 L12:  19.9924
REMARK   3      L13:   6.3752 L23:   0.3971
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0138 S12:  -1.4497 S13:   0.4325
REMARK   3      S21:  -0.5340 S22:  -1.6849 S23:  -0.4911
REMARK   3      S31:   3.0710 S32:   1.2679 S33:   1.6987
REMARK   3
REMARK   3   TLS GROUP : 28
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   205        B   242
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4104  -7.8390  60.9968
REMARK   3    T TENSOR
REMARK   3      T11:   0.2557 T22:   0.1882
REMARK   3      T33:   0.2039 T12:  -0.0110
REMARK   3      T13:  -0.0124 T23:  -0.0138
REMARK   3    L TENSOR
REMARK   3      L11:   1.7233 L22:   0.8645
REMARK   3      L33:   0.5323 L12:  -0.5157
REMARK   3      L13:   0.6063 L23:  -0.4066
REMARK   3    S TENSOR
REMARK   3      S11:   0.0824 S12:   0.0536 S13:  -0.0515
REMARK   3      S21:  -0.0317 S22:  -0.0181 S23:   0.0061
REMARK   3      S31:   0.2117 S32:  -0.0342 S33:  -0.0643
REMARK   3
REMARK   3   TLS GROUP : 29
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   243        B   257
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3556   3.0591  61.0396
REMARK   3    T TENSOR
REMARK   3      T11:   0.1517 T22:   0.2685
REMARK   3      T33:   0.2864 T12:  -0.0364
REMARK   3      T13:   0.0070 T23:   0.0232
REMARK   3    L TENSOR
REMARK   3      L11:  -0.3478 L22:   3.4561
REMARK   3      L33:   3.9571 L12:  -0.6425
REMARK   3      L13:   0.5130 L23:  -0.2782
REMARK   3    S TENSOR
REMARK   3      S11:   0.0425 S12:  -0.0707 S13:  -0.1334
REMARK   3      S21:  -0.1352 S22:  -0.0223 S23:   0.4651
REMARK   3      S31:   0.0495 S32:  -0.2253 S33:  -0.0202
REMARK   3
REMARK   3   TLS GROUP : 30
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   258        B   268
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3545  -8.1936  69.9204
REMARK   3    T TENSOR
REMARK   3      T11:   0.2475 T22:   0.1970
REMARK   3      T33:   0.1917 T12:  -0.0331
REMARK   3      T13:   0.0052 T23:   0.0296
REMARK   3    L TENSOR
REMARK   3      L11:   8.2456 L22:   5.0383
REMARK   3      L33:   6.1646 L12:  -5.4479
REMARK   3      L13:   6.2328 L23:  -3.3654
REMARK   3    S TENSOR
REMARK   3      S11:   0.1128 S12:  -0.4695 S13:  -0.1526
REMARK   3      S21:   0.1264 S22:   0.1290 S23:   0.1483
REMARK   3      S31:   0.1519 S32:  -0.3001 S33:  -0.2419
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
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 3NAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059598.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-MAY-10
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               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29864
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : 0.09100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 8.300
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: 1XC4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM FLOURIDE  20% PEG 3350,
REMARK 280  PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.79700
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.59850
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.19000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.59850
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.79700
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.19000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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     SER A    -2
REMARK 465     ASN A    -1
REMARK 465     GLY A   181
REMARK 465     VAL A   182
REMARK 465     THR A   183
REMARK 465     GLY A   184
REMARK 465     ALA A   185
REMARK 465     GLU A   186
REMARK 465     THR A   187
REMARK 465     LYS A   188
REMARK 465     SER B    -2
REMARK 465     ASN B    -1
REMARK 465     GLY B   181
REMARK 465     VAL B   182
REMARK 465     THR B   183
REMARK 465     GLY B   184
REMARK 465     ALA B   185
REMARK 465     GLU B   186
REMARK 465     THR B   187
REMARK 465     LYS B   188
REMARK 465     ALA B   189
REMARK 465     ASN B   190
REMARK 465     MET B   191
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A  91    CG   CD   NE   CZ   NH1  NH2
REMARK 470     MET A 191    CG   SD   CE
REMARK 470     PRO B 192    CG   CD
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 B 192   N   -  CA  -  CB  ANGL. DEV. =   7.6 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    LYS B  75       33.03     72.27
REMARK 500    SER B 159      -91.24   -109.74
REMARK 500    ASP B 160      -60.68   -141.58
REMARK 500    ASP B 204       31.95     70.34
REMARK 500    ASN B 247       88.75   -156.88
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 A 408        DISTANCE =  5.57 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP04160   RELATED DB: TARGETDB
DBREF  3NAV A    1   268  UNP    C3LLL5   TRPA_VIBCM       1    268
DBREF  3NAV B    1   268  UNP    C3LLL5   TRPA_VIBCM       1    268
SEQADV 3NAV SER A   -2  UNP  C3LLL5              EXPRESSION TAG
SEQADV 3NAV ASN A   -1  UNP  C3LLL5              EXPRESSION TAG
SEQADV 3NAV ALA A    0  UNP  C3LLL5              EXPRESSION TAG
SEQADV 3NAV SER B   -2  UNP  C3LLL5              EXPRESSION TAG
SEQADV 3NAV ASN B   -1  UNP  C3LLL5              EXPRESSION TAG
SEQADV 3NAV ALA B    0  UNP  C3LLL5              EXPRESSION TAG
SEQRES   1 A  271  SER ASN ALA MET ASN ARG TYR GLN ALA LEU PHE GLN ARG
SEQRES   2 A  271  LEU SER ALA ALA GLN GLN GLY ALA PHE VAL PRO PHE VAL
SEQRES   3 A  271  THR ILE GLY ASP PRO ASN PRO GLU GLN SER LEU ALA ILE
SEQRES   4 A  271  MET GLN THR LEU ILE ASP ALA GLY ALA ASP ALA LEU GLU
SEQRES   5 A  271  LEU GLY MET PRO PHE SER ASP PRO LEU ALA ASP GLY PRO
SEQRES   6 A  271  THR ILE GLN GLY ALA ASN LEU ARG ALA LEU ALA ALA LYS
SEQRES   7 A  271  THR THR PRO ASP ILE CYS PHE GLU LEU ILE ALA GLN ILE
SEQRES   8 A  271  ARG ALA ARG ASN PRO GLU THR PRO ILE GLY LEU LEU MET
SEQRES   9 A  271  TYR ALA ASN LEU VAL TYR ALA ARG GLY ILE ASP ASP PHE
SEQRES  10 A  271  TYR GLN ARG CYS GLN LYS ALA GLY VAL ASP SER VAL LEU
SEQRES  11 A  271  ILE ALA ASP VAL PRO THR ASN GLU SER GLN PRO PHE VAL
SEQRES  12 A  271  ALA ALA ALA GLU LYS PHE GLY ILE GLN PRO ILE PHE ILE
SEQRES  13 A  271  ALA PRO PRO THR ALA SER ASP GLU THR LEU ARG ALA VAL
SEQRES  14 A  271  ALA GLN LEU GLY LYS GLY TYR THR TYR LEU LEU SER ARG
SEQRES  15 A  271  ALA GLY VAL THR GLY ALA GLU THR LYS ALA ASN MET PRO
SEQRES  16 A  271  VAL HIS ALA LEU LEU GLU ARG LEU GLN GLN PHE ASP ALA
SEQRES  17 A  271  PRO PRO ALA LEU LEU GLY PHE GLY ILE SER GLU PRO ALA
SEQRES  18 A  271  GLN VAL LYS GLN ALA ILE GLU ALA GLY ALA ALA GLY ALA
SEQRES  19 A  271  ILE SER GLY SER ALA VAL VAL LYS ILE ILE GLU THR HIS
SEQRES  20 A  271  LEU ASP ASN PRO ALA LYS GLN LEU THR GLU LEU ALA ASN
SEQRES  21 A  271  PHE THR GLN ALA MET LYS LYS ALA THR LYS ILE
SEQRES   1 B  271  SER ASN ALA MET ASN ARG TYR GLN ALA LEU PHE GLN ARG
SEQRES   2 B  271  LEU SER ALA ALA GLN GLN GLY ALA PHE VAL PRO PHE VAL
SEQRES   3 B  271  THR ILE GLY ASP PRO ASN PRO GLU GLN SER LEU ALA ILE
SEQRES   4 B  271  MET GLN THR LEU ILE ASP ALA GLY ALA ASP ALA LEU GLU
SEQRES   5 B  271  LEU GLY MET PRO PHE SER ASP PRO LEU ALA ASP GLY PRO
SEQRES   6 B  271  THR ILE GLN GLY ALA ASN LEU ARG ALA LEU ALA ALA LYS
SEQRES   7 B  271  THR THR PRO ASP ILE CYS PHE GLU LEU ILE ALA GLN ILE
SEQRES   8 B  271  ARG ALA ARG ASN PRO GLU THR PRO ILE GLY LEU LEU MET
SEQRES   9 B  271  TYR ALA ASN LEU VAL TYR ALA ARG GLY ILE ASP ASP PHE
SEQRES  10 B  271  TYR GLN ARG CYS GLN LYS ALA GLY VAL ASP SER VAL LEU
SEQRES  11 B  271  ILE ALA ASP VAL PRO THR ASN GLU SER GLN PRO PHE VAL
SEQRES  12 B  271  ALA ALA ALA GLU LYS PHE GLY ILE GLN PRO ILE PHE ILE
SEQRES  13 B  271  ALA PRO PRO THR ALA SER ASP GLU THR LEU ARG ALA VAL
SEQRES  14 B  271  ALA GLN LEU GLY LYS GLY TYR THR TYR LEU LEU SER ARG
SEQRES  15 B  271  ALA GLY VAL THR GLY ALA GLU THR LYS ALA ASN MET PRO
SEQRES  16 B  271  VAL HIS ALA LEU LEU GLU ARG LEU GLN GLN PHE ASP ALA
SEQRES  17 B  271  PRO PRO ALA LEU LEU GLY PHE GLY ILE SER GLU PRO ALA
SEQRES  18 B  271  GLN VAL LYS GLN ALA ILE GLU ALA GLY ALA ALA GLY ALA
SEQRES  19 B  271  ILE SER GLY SER ALA VAL VAL LYS ILE ILE GLU THR HIS
SEQRES  20 B  271  LEU ASP ASN PRO ALA LYS GLN LEU THR GLU LEU ALA ASN
SEQRES  21 B  271  PHE THR GLN ALA MET LYS LYS ALA THR LYS ILE
HET    EDO  A 601       4
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  EDO    C2 H6 O2
FORMUL   4  HOH   *381(H2 O)
HELIX    1   1 ASN A    2  ALA A   14  1                                  13
HELIX    2   2 ASN A   29  ALA A   43  1                                  15
HELIX    3   3 ASP A   56  ASP A   60  5                                   5
HELIX    4   4 PRO A   62  ALA A   74  1                                  13
HELIX    5   5 THR A   77  ASN A   92  1                                  16
HELIX    6   6 TYR A  102  ARG A  109  1                                   8
HELIX    7   7 GLY A  110  GLY A  122  1                                  13
HELIX    8   8 PRO A  132  GLU A  135  5                                   4
HELIX    9   9 SER A  136  PHE A  146  1                                  11
HELIX   10  10 SER A  159  GLY A  170  1                                  12
HELIX   11  11 ASN A  190  PHE A  203  1                                  14
HELIX   12  12 GLU A  216  ALA A  226  1                                  11
HELIX   13  13 GLY A  234  HIS A  244  1                                  11
HELIX   14  14 ASN A  247  ALA A  265  1                                  19
HELIX   15  15 ASN B    2  GLN B   15  1                                  14
HELIX   16  16 ASN B   29  ALA B   43  1                                  15
HELIX   17  17 GLY B   61  ALA B   74  1                                  14
HELIX   18  18 THR B   77  ASN B   92  1                                  16
HELIX   19  19 TYR B  102  ALA B  108  1                                   7
HELIX   20  20 GLY B  110  GLY B  122  1                                  13
HELIX   21  21 PRO B  132  GLU B  135  5                                   4
HELIX   22  22 SER B  136  PHE B  146  1                                  11
HELIX   23  23 ASP B  160  GLY B  170  1                                  11
HELIX   24  25 GLU B  216  ALA B  226  1                                  11
HELIX   25  26 SER B  235  HIS B  244  1                                  10
HELIX   26  27 ASN B  247  ALA B  265  1                                  19
SHEET    1   A 9 ALA A  18  THR A  24  0
SHEET    2   A 9 LEU A  48  GLY A  51  1  O  GLU A  49   N  PRO A  21
SHEET    3   A 9 ILE A  97  MET A 101  1  O  GLY A  98   N  LEU A  48
SHEET    4   A 9 SER A 125  ILE A 128  1  O  LEU A 127   N  MET A 101
SHEET    5   A 9 GLN A 149  ALA A 154  1  O  ILE A 151   N  VAL A 126
SHEET    6   A 9 THR A 174  LEU A 176  1  O  TYR A 175   N  PHE A 152
SHEET    7   A 9 ALA A 208  LEU A 210  1  O  LEU A 209   N  THR A 174
SHEET    8   A 9 GLY A 230  SER A 233  1  O  ILE A 232   N  LEU A 210
SHEET    9   A 9 ALA A  18  THR A  24  1  N  VAL A  20   O  ALA A 231
SHEET    1   B 9 GLN B 149  ILE B 151  0
SHEET    2   B 9 SER B 125  ILE B 128  1  N  VAL B 126   O  ILE B 151
SHEET    3   B 9 ILE B  97  MET B 101  1  N  MET B 101   O  LEU B 127
SHEET    4   B 9 LEU B  48  GLY B  51  1  N  LEU B  50   O  LEU B 100
SHEET    5   B 9 ALA B  18  THR B  24  1  N  PRO B  21   O  GLU B  49
SHEET    6   B 9 GLY B 230  SER B 233  1  O  ALA B 231   N  ALA B  18
SHEET    7   B 9 ALA B 208  LEU B 210  1  N  LEU B 210   O  ILE B 232
SHEET    8   B 9 THR B 174  LEU B 176  1  N  LEU B 176   O  LEU B 209
SHEET    9   B 9 ILE B 153  ALA B 154  1  N  ALA B 154   O  TYR B 175
CISPEP   1 ASP A   27    PRO A   28          0         1.62
CISPEP   2 ASP B   27    PRO B   28          0         2.57
SITE     1 AC1  3 ILE A  64  LEU A 100  HOH A 422
CRYST1   57.594   60.380  141.197  90.00  90.00  90.00 P 21 21 21    8
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      0.017363  0.000000  0.000000        0.00000
SCALE2      0.000000  0.016562  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007082        0.00000
      
PROCHECK
Go to PROCHECK summary
 References