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PDBsum entry 2nzj

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Signaling protein PDB id
2nzj
Jmol
Contents
Protein chains
155 a.a.
160 a.a.
159 a.a.
Ligands
GDP ×4
Metals
_MG ×4
_CL ×2
Waters ×16
HEADER    SIGNALING PROTEIN                       23-NOV-06   2NZJ
TITLE     THE CRYSTAL STRUCTURE OF REM1 IN COMPLEX WITH GDP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GTP-BINDING PROTEIN REM 1;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: RAD AND GEM-LIKE GTP-BINDING PROTEIN 1, GTPASE-REGULATING
COMPND   5 ENDOTHELIAL CELL SPROUTING;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: REM1, GES, REM;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3/ROSETTA;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS    REM1, GDP/GTP BINDING, GTP HYDROLYSIS, RAD AND GEM LIKE GTP BINDING
KEYWDS   2 PROTEIN 1, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS   3 SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.P.TURNBULL,E.PAPAGRIGORIOU,E.UGOCHUKWU,J.M.ELKINS,M.SOUNDARARAJAN,
AUTHOR   2 X.YANG,F.GORREC,C.UMEANO,E.SALAH,N.BURGESS,C.JOHANSSON,G.BERRIDGE,
AUTHOR   3 O.GILEADI,J.BRAY,B.MARSDEN,S.WATTS,F.VON DELFT,J.WEIGELT,A.EDWARDS,
AUTHOR   4 C.H.ARROWSMITH,M.SUNDSTROM,D.DOYLE,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR   5 (SGC)
REVDAT   4   13-JUL-11 2NZJ    1       VERSN
REVDAT   3   24-FEB-09 2NZJ    1       VERSN
REVDAT   2   19-DEC-06 2NZJ    1       AUTHOR
REVDAT   1   12-DEC-06 2NZJ    0
JRNL        AUTH   A.P.TURNBULL,E.PAPAGRIGORIOU,E.UGOCHUKWU,J.M.ELKINS,
JRNL        AUTH 2 M.SOUNDARARAJAN,X.YANG,F.GORREC,C.UMEANO,E.SALAH,N.BURGESS,
JRNL        AUTH 3 C.JOHANSSON,G.BERRIDGE,O.GILEADI,J.BRAY,B.MARSDEN,S.WATTS,
JRNL        AUTH 4 F.VON DELFT,J.WEIGELT,A.EDWARDS,C.H.ARROWSMITH,M.SUNDSTROM,
JRNL        AUTH 5 D.DOYLE
JRNL        TITL   THE CRYSTAL STRUCTURE OF REM1 IN COMPLEX WITH GDP
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.50 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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7
REMARK   3   NUMBER OF REFLECTIONS             : 24187
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) : 0.227
REMARK   3   R VALUE            (WORKING SET) : 0.225
REMARK   3   FREE R VALUE                     : 0.280
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1284
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) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1653
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.02
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050
REMARK   3   BIN FREE R VALUE SET COUNT          : 99
REMARK   3   BIN FREE R VALUE                    : 0.3370
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4651
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 118
REMARK   3   SOLVENT ATOMS            : 16
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.02000
REMARK   3    B22 (A**2) : -1.74000
REMARK   3    B33 (A**2) : 1.72000
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): 0.564
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.321
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.243
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.523
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4827 ; 0.012 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  3087 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6572 ; 1.359 ; 1.987
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7489 ; 0.925 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   616 ; 6.662 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   186 ;33.775 ;22.796
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   743 ;14.922 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;16.082 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   795 ; 0.068 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5353 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  1009 ; 0.002 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   864 ; 0.208 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3126 ; 0.197 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2336 ; 0.178 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2588 ; 0.085 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   118 ; 0.159 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    11 ; 0.121 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.156 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    53 ; 0.237 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.147 ; 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):  3156 ; 0.499 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1294 ; 0.094 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4913 ; 0.880 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1928 ; 1.213 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1659 ; 1.887 ; 4.500
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 : 2
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     81       A     101      2
REMARK   3           1     B     81       B     101      2
REMARK   3           1     C     81       C     101      2
REMARK   3           1     D     81       D     101      2
REMARK   3           2     A    117       A     136      2
REMARK   3           2     B    117       B     136      2
REMARK   3           2     C    117       C     136      2
REMARK   3           2     D    117       D     136      2
REMARK   3           3     A    154       A     170      2
REMARK   3           3     B    154       B     170      2
REMARK   3           3     C    154       C     170      2
REMARK   3           3     D    154       D     170      2
REMARK   3           4     A    189       A     199      2
REMARK   3           4     B    189       B     199      2
REMARK   3           4     C    189       C     199      2
REMARK   3           4     D    189       D     199      2
REMARK   3           5     A    220       A     244      2
REMARK   3           5     B    220       B     244      2
REMARK   3           5     C    220       C     244      2
REMARK   3           5     D    220       D     244      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):    554 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):    554 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    C    (A):    554 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    D    (A):    554 ;  0.04 ;  0.05
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    631 ;  0.24 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    631 ;  0.33 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    631 ;  0.25 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    631 ;  0.28 ;  0.50
REMARK   3   TIGHT THERMAL      1    A (A**2):    554 ;  0.07 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):    554 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    C (A**2):    554 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    D (A**2):    554 ;  0.07 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):    631 ;  0.38 ;  2.00
REMARK   3   MEDIUM THERMAL     1    B (A**2):    631 ;  0.41 ;  2.00
REMARK   3   MEDIUM THERMAL     1    C (A**2):    631 ;  0.41 ;  2.00
REMARK   3   MEDIUM THERMAL     1    D (A**2):    631 ;  0.38 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : C D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C    182       C     188      2
REMARK   3           1     D    182       D     188      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    C    (A):     42 ;  0.03 ;  0.05
REMARK   3   MEDIUM POSITIONAL  2    C    (A):     30 ;  0.61 ;  0.50
REMARK   3   TIGHT THERMAL      2    C (A**2):     42 ;  0.07 ;  0.50
REMARK   3   MEDIUM THERMAL     2    C (A**2):     30 ;  0.26 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 12
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   110
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1213   8.5536 -19.7061
REMARK   3    T TENSOR
REMARK   3      T11:   0.1769 T22:   0.1386
REMARK   3      T33:   0.1929 T12:  -0.0062
REMARK   3      T13:  -0.0390 T23:  -0.0161
REMARK   3    L TENSOR
REMARK   3      L11:   2.7754 L22:   3.3211
REMARK   3      L33:   1.7750 L12:   3.0356
REMARK   3      L13:  -1.4760 L23:  -1.6448
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0443 S12:  -0.3524 S13:   0.0471
REMARK   3      S21:   0.2036 S22:   0.0265 S23:   0.1761
REMARK   3      S31:   0.0678 S32:   0.0209 S33:   0.0178
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   111        A   172
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1698   8.1241 -24.7781
REMARK   3    T TENSOR
REMARK   3      T11:   0.3825 T22:   0.2012
REMARK   3      T33:   0.3623 T12:  -0.0010
REMARK   3      T13:  -0.0263 T23:  -0.0141
REMARK   3    L TENSOR
REMARK   3      L11:   2.2222 L22:   2.4599
REMARK   3      L33:   2.2981 L12:   2.0888
REMARK   3      L13:  -1.7439 L23:  -0.9598
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1169 S12:  -0.1458 S13:  -0.1781
REMARK   3      S21:  -0.3044 S22:   0.0614 S23:   0.0933
REMARK   3      S31:   0.3039 S32:  -0.0030 S33:   0.0554
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   173        A   248
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2002  17.1990 -30.0004
REMARK   3    T TENSOR
REMARK   3      T11:   0.0694 T22:  -0.0424
REMARK   3      T33:   0.0908 T12:  -0.0224
REMARK   3      T13:  -0.0040 T23:  -0.0036
REMARK   3    L TENSOR
REMARK   3      L11:   3.4588 L22:   3.1918
REMARK   3      L33:   4.3591 L12:   0.7661
REMARK   3      L13:  -1.1514 L23:  -0.9848
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1116 S12:   0.2132 S13:   0.1810
REMARK   3      S21:  -0.4498 S22:   0.1531 S23:   0.2218
REMARK   3      S31:   0.2238 S32:  -0.0714 S33:  -0.0414
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 :   B     0        B   111
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3818   7.5387 -67.1037
REMARK   3    T TENSOR
REMARK   3      T11:   0.2882 T22:   0.2160
REMARK   3      T33:   0.2160 T12:  -0.0163
REMARK   3      T13:   0.0487 T23:   0.0008
REMARK   3    L TENSOR
REMARK   3      L11:   3.7792 L22:   5.7782
REMARK   3      L33:   0.8289 L12:  -4.1289
REMARK   3      L13:  -0.4254 L23:   1.4596
REMARK   3    S TENSOR
REMARK   3      S11:   0.2157 S12:   0.6322 S13:  -0.2884
REMARK   3      S21:  -0.7467 S22:  -0.2890 S23:  -0.2099
REMARK   3      S31:   0.0165 S32:   0.1736 S33:   0.0733
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 :   B   112        B   171
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1876   8.1494 -59.7147
REMARK   3    T TENSOR
REMARK   3      T11:   0.4063 T22:   0.2395
REMARK   3      T33:   0.3924 T12:  -0.0145
REMARK   3      T13:   0.0299 T23:  -0.0238
REMARK   3    L TENSOR
REMARK   3      L11:   3.6171 L22:   2.1298
REMARK   3      L33:   1.5704 L12:  -1.3509
REMARK   3      L13:  -2.1528 L23:   0.4489
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1924 S12:   0.1203 S13:  -0.5552
REMARK   3      S21:   0.1231 S22:  -0.0322 S23:  -0.1023
REMARK   3      S31:   0.2304 S32:   0.0022 S33:   0.2247
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 :   B   172        B   248
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8694  17.1766 -54.4655
REMARK   3    T TENSOR
REMARK   3      T11:   0.0929 T22:  -0.0555
REMARK   3      T33:   0.0892 T12:  -0.0182
REMARK   3      T13:   0.0240 T23:  -0.0382
REMARK   3    L TENSOR
REMARK   3      L11:   3.7546 L22:   3.5573
REMARK   3      L33:   3.6518 L12:  -1.0868
REMARK   3      L13:  -1.3302 L23:   0.0921
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0197 S12:  -0.4050 S13:   0.0862
REMARK   3      S21:   0.2485 S22:   0.0914 S23:  -0.2041
REMARK   3      S31:   0.1725 S32:   0.2141 S33:  -0.0717
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 :   C     0        C   111
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2705  35.8734 -60.1600
REMARK   3    T TENSOR
REMARK   3      T11:   0.2388 T22:   0.2343
REMARK   3      T33:   0.2093 T12:   0.0310
REMARK   3      T13:  -0.0029 T23:  -0.0487
REMARK   3    L TENSOR
REMARK   3      L11:   1.4026 L22:   4.9497
REMARK   3      L33:   0.8450 L12:   0.3464
REMARK   3      L13:   0.7766 L23:  -0.9212
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0792 S12:  -0.2707 S13:  -0.1968
REMARK   3      S21:   0.6383 S22:   0.2183 S23:  -0.1282
REMARK   3      S31:  -0.0603 S32:  -0.1695 S33:  -0.1391
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 :   C   112        C   171
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0816  36.0170 -65.5464
REMARK   3    T TENSOR
REMARK   3      T11:   0.3910 T22:   0.2751
REMARK   3      T33:   0.3303 T12:   0.0298
REMARK   3      T13:  -0.0497 T23:   0.0085
REMARK   3    L TENSOR
REMARK   3      L11:   0.1957 L22:   5.6515
REMARK   3      L33:   1.5731 L12:  -0.8272
REMARK   3      L13:  -0.3818 L23:   0.2786
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0522 S12:   0.0968 S13:  -0.2760
REMARK   3      S21:   0.1121 S22:   0.0391 S23:  -0.3434
REMARK   3      S31:   0.1823 S32:   0.2056 S33:   0.0131
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 :   C   172        C   247
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8628  45.3423 -70.6130
REMARK   3    T TENSOR
REMARK   3      T11:   0.1258 T22:  -0.0120
REMARK   3      T33:   0.0432 T12:   0.0319
REMARK   3      T13:  -0.0183 T23:   0.0599
REMARK   3    L TENSOR
REMARK   3      L11:   3.8344 L22:   7.5708
REMARK   3      L33:   2.7945 L12:   1.6996
REMARK   3      L13:  -0.4913 L23:   0.8024
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1158 S12:   0.2446 S13:   0.0946
REMARK   3      S21:  -0.5997 S22:   0.0697 S23:   0.2609
REMARK   3      S31:   0.0500 S32:   0.0817 S33:   0.0461
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 :   D     0        D   111
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7117  36.2788 -20.8268
REMARK   3    T TENSOR
REMARK   3      T11:   0.3604 T22:   0.1882
REMARK   3      T33:   0.1801 T12:  -0.0630
REMARK   3      T13:  -0.1139 T23:   0.0145
REMARK   3    L TENSOR
REMARK   3      L11:   6.0176 L22:   7.3054
REMARK   3      L33:   4.3383 L12:  -3.5267
REMARK   3      L13:   1.4627 L23:  -0.4565
REMARK   3    S TENSOR
REMARK   3      S11:   0.5568 S12:   0.1222 S13:  -0.2330
REMARK   3      S21:  -1.0308 S22:  -0.1449 S23:   0.1356
REMARK   3      S31:   0.3779 S32:  -0.0915 S33:  -0.4119
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 :   D   112        D   170
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9869  35.5745 -17.1984
REMARK   3    T TENSOR
REMARK   3      T11:   0.4299 T22:   0.2966
REMARK   3      T33:   0.3117 T12:  -0.0396
REMARK   3      T13:  -0.0224 T23:  -0.0165
REMARK   3    L TENSOR
REMARK   3      L11:   0.5537 L22:   8.1265
REMARK   3      L33:   2.7155 L12:  -0.7056
REMARK   3      L13:  -0.8693 L23:  -0.6399
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0695 S12:   0.0564 S13:  -0.2993
REMARK   3      S21:  -0.4363 S22:  -0.0925 S23:   0.2665
REMARK   3      S31:   0.2587 S32:  -0.2184 S33:   0.1619
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 :   D   171        D   246
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4911  44.6339 -10.9189
REMARK   3    T TENSOR
REMARK   3      T11:   0.1506 T22:   0.0037
REMARK   3      T33:   0.0281 T12:  -0.0323
REMARK   3      T13:  -0.0615 T23:  -0.0471
REMARK   3    L TENSOR
REMARK   3      L11:   4.0189 L22:  10.4685
REMARK   3      L33:   3.5848 L12:  -2.7086
REMARK   3      L13:  -0.7240 L23:  -1.7964
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1408 S12:  -0.2296 S13:   0.2003
REMARK   3      S21:   0.7089 S22:   0.2771 S23:  -0.4495
REMARK   3      S31:   0.0059 S32:  -0.2642 S33:  -0.1362
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 2NZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB040497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999
REMARK 200  MONOCHROMATOR                  : SI (111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25510
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 2G3Y, 2GJS, 2DPX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34 % (W/V) PEG3350, 0.26M NACL, 0.1 M
REMARK 280  HEPES, PH 7.7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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       21.82000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.78250
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.14200
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.78250
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.82000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.14200
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -43.64000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -51.14200
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -82.78250
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    -1
REMARK 465     GLN A   104
REMARK 465     GLU A   105
REMARK 465     ARG A   106
REMARK 465     ASP A   107
REMARK 465     LEU A   108
REMARK 465     GLU A   137
REMARK 465     ALA A   138
REMARK 465     GLU A   139
REMARK 465     LYS A   140
REMARK 465     LEU A   141
REMARK 465     ASP A   142
REMARK 465     LYS A   143
REMARK 465     HIS A   183
REMARK 465     GLN A   184
REMARK 465     ALA A   185
REMARK 465     ASP A   186
REMARK 465     ASP A   249
REMARK 465     SER A   250
REMARK 465     ALA A   251
REMARK 465     SER B    -1
REMARK 465     ALA B   138
REMARK 465     GLU B   139
REMARK 465     LYS B   140
REMARK 465     LEU B   141
REMARK 465     ASP B   142
REMARK 465     LYS B   143
REMARK 465     HIS B   183
REMARK 465     GLN B   184
REMARK 465     ALA B   185
REMARK 465     ASP B   186
REMARK 465     HIS B   187
REMARK 465     ASP B   249
REMARK 465     SER B   250
REMARK 465     ALA B   251
REMARK 465     SER C    -1
REMARK 465     GLN C   104
REMARK 465     GLU C   105
REMARK 465     ARG C   106
REMARK 465     ASP C   107
REMARK 465     LEU C   108
REMARK 465     ALA C   138
REMARK 465     GLU C   139
REMARK 465     LYS C   140
REMARK 465     LEU C   141
REMARK 465     ASP C   142
REMARK 465     LYS C   143
REMARK 465     ARG C   248
REMARK 465     ASP C   249
REMARK 465     SER C   250
REMARK 465     ALA C   251
REMARK 465     SER D    -1
REMARK 465     LYS D   103
REMARK 465     GLN D   104
REMARK 465     GLU D   105
REMARK 465     ARG D   106
REMARK 465     ASP D   107
REMARK 465     LEU D   108
REMARK 465     HIS D   109
REMARK 465     GLU D   110
REMARK 465     ALA D   138
REMARK 465     GLU D   139
REMARK 465     LYS D   140
REMARK 465     LEU D   141
REMARK 465     ASP D   142
REMARK 465     LYS D   143
REMARK 465     ARG D   247
REMARK 465     ARG D   248
REMARK 465     ASP D   249
REMARK 465     SER D   250
REMARK 465     ALA D   251
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     LYS A 103    CG   CD   CE   NZ
REMARK 470     GLN A 111    CG   CD   OE1  NE2
REMARK 470     GLU A 114    CG   CD   OE1  OE2
REMARK 470     GLU A 118    CG   CD   OE1  OE2
REMARK 470     GLU A 148    CD   OE1  OE2
REMARK 470     SER A 149    OG
REMARK 470     GLN A 152    CG   CD   OE1  NE2
REMARK 470     GLU A 174    CD   OE1  OE2
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2
REMARK 470     HIS A 187    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG A 201    CG   CD   NE   CZ   NH1  NH2
REMARK 470     PHE A 217    CE1  CE2  CZ
REMARK 470     ASP A 218    CG   OD1  OD2
REMARK 470     LYS A 220    NZ
REMARK 470     ARG A 246    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 247    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 248    CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 103    CG   CD   CE   NZ
REMARK 470     GLN B 104    CG   CD   OE1  NE2
REMARK 470     GLU B 105    CG   CD   OE1  OE2
REMARK 470     ASP B 107    CG   OD1  OD2
REMARK 470     GLN B 111    CB   CG   CD   OE1  NE2
REMARK 470     GLU B 114    CG   CD   OE1  OE2
REMARK 470     GLU B 118    CD   OE1  OE2
REMARK 470     GLU B 137    CG   CD   OE1  OE2
REMARK 470     SER B 144    OG
REMARK 470     GLN B 147    CG   CD   OE1  NE2
REMARK 470     GLU B 148    CG   CD   OE1  OE2
REMARK 470     GLN B 152    CG   CD   OE1  NE2
REMARK 470     SER B 171    OG
REMARK 470     GLU B 174    CG   CD   OE1  OE2
REMARK 470     ARG B 181    CD   NE   CZ   NH1  NH2
REMARK 470     THR B 182    OG1  CG2
REMARK 470     ARG B 201    CD   NE   CZ   NH1  NH2
REMARK 470     PHE B 217    CD1  CD2  CE1  CE2  CZ
REMARK 470     ARG B 247    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS C 103    CG   CD   CE   NZ
REMARK 470     GLU C 114    CD   OE1  OE2
REMARK 470     GLU C 137    CG   CD   OE1  OE2
REMARK 470     GLU C 148    CD   OE1  OE2
REMARK 470     LEU C 151    CG   CD1  CD2
REMARK 470     GLN C 152    CG   CD   OE1  NE2
REMARK 470     GLU C 174    CD   OE1  OE2
REMARK 470     ARG C 181    CD   NE   CZ   NH1  NH2
REMARK 470     ASP C 186    CG   OD1  OD2
REMARK 470     HIS C 187    ND1  CD2  CE1  NE2
REMARK 470     GLU C 208    CG   CD   OE1  OE2
REMARK 470     LYS C 220    NZ
REMARK 470     ARG C 246    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C 247    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN D 111    CG   CD   OE1  NE2
REMARK 470     LEU D 112    CG   CD1  CD2
REMARK 470     GLU D 114    CG   CD   OE1  OE2
REMARK 470     VAL D 116    CG1  CG2
REMARK 470     GLU D 137    CG   CD   OE1  OE2
REMARK 470     SER D 149    OG
REMARK 470     LEU D 151    CG   CD1  CD2
REMARK 470     GLN D 152    CD   OE1  NE2
REMARK 470     GLU D 170    CD   OE1  OE2
REMARK 470     GLU D 174    CD   OE1  OE2
REMARK 470     ARG D 181    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP D 186    CG   OD1  OD2
REMARK 470     HIS D 187    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS D 220    NZ
REMARK 470     LEU D 228    CD1  CD2
REMARK 470     ARG D 246    CG   CD   NE   CZ   NH1  NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 203   NE  -  CZ  -  NH1 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    ASP A 115       49.80   -109.46
REMARK 500    LEU A 199       49.32    -84.59
REMARK 500    ARG A 203      115.87    -29.23
REMARK 500    ALA B  79      163.47    178.91
REMARK 500    ARG B 203      125.69    -36.24
REMARK 500    LYS D 196       33.95     70.07
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 ALA B  101     GLY B  102                 -125.43
REMARK 500 LEU D  112     GLY D  113                  132.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 252  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A   2   O
REMARK 620 2 THR A  94   OG1  80.9
REMARK 620 3 HOH A   1   O    82.3  84.9
REMARK 620 4 HOH A   4   O    80.4 160.1  85.9
REMARK 620 5 GDP A1001   O2B  90.4  88.1 170.6  98.8
REMARK 620 6 HOH A   3   O   172.9  93.9  92.5 104.2  94.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 252  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP B1002   O3B
REMARK 620 2 HOH B   8   O   148.3
REMARK 620 3 HOH B   5   O   102.7  89.2
REMARK 620 4 HOH B   6   O    51.6 102.1  83.1
REMARK 620 5 THR B  94   OG1 138.2  73.1  75.2 157.7
REMARK 620 6 HOH B   7   O   100.6  79.8 151.0 125.4  75.9
REMARK 620 7 GDP B1002   O2B  51.6 158.5  92.6  99.4  86.7  88.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 252  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C   9   O
REMARK 620 2 HOH C  10   O    82.7
REMARK 620 3 HOH C  11   O    97.9  80.7
REMARK 620 4 HOH C  12   O   152.7  70.2  82.0
REMARK 620 5 GDP C1003   O2B  92.8  80.7 157.1  79.3
REMARK 620 6 THR C  94   OG1 103.9 172.0  93.9 103.4 103.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 252  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D  14   O
REMARK 620 2 HOH D  16   O    83.6
REMARK 620 3 HOH D  13   O    97.6 166.3
REMARK 620 4 HOH D  15   O    93.9  95.6  97.9
REMARK 620 5 GDP D1004   O2B 163.0  80.1  97.1  92.3
REMARK 620 6 THR D  94   OG1  81.0  74.9  91.8 169.6  90.2
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 1004
DBREF  2NZJ A   79   251  UNP    O75628   REM1_HUMAN      79    251
DBREF  2NZJ B   79   251  UNP    O75628   REM1_HUMAN      79    251
DBREF  2NZJ C   79   251  UNP    O75628   REM1_HUMAN      79    251
DBREF  2NZJ D   79   251  UNP    O75628   REM1_HUMAN      79    251
SEQADV 2NZJ SER A   -1  UNP  O75628              CLONING ARTIFACT
SEQADV 2NZJ MET A    0  UNP  O75628              CLONING ARTIFACT
SEQADV 2NZJ SER B   -1  UNP  O75628              CLONING ARTIFACT
SEQADV 2NZJ MET B    0  UNP  O75628              CLONING ARTIFACT
SEQADV 2NZJ SER C   -1  UNP  O75628              CLONING ARTIFACT
SEQADV 2NZJ MET C    0  UNP  O75628              CLONING ARTIFACT
SEQADV 2NZJ SER D   -1  UNP  O75628              CLONING ARTIFACT
SEQADV 2NZJ MET D    0  UNP  O75628              CLONING ARTIFACT
SEQRES   1 A  175  SER MET ALA LEU TYR ARG VAL VAL LEU LEU GLY ASP PRO
SEQRES   2 A  175  GLY VAL GLY LYS THR SER LEU ALA SER LEU PHE ALA GLY
SEQRES   3 A  175  LYS GLN GLU ARG ASP LEU HIS GLU GLN LEU GLY GLU ASP
SEQRES   4 A  175  VAL TYR GLU ARG THR LEU THR VAL ASP GLY GLU ASP THR
SEQRES   5 A  175  THR LEU VAL VAL VAL ASP THR TRP GLU ALA GLU LYS LEU
SEQRES   6 A  175  ASP LYS SER TRP SER GLN GLU SER CYS LEU GLN GLY GLY
SEQRES   7 A  175  SER ALA TYR VAL ILE VAL TYR SER ILE ALA ASP ARG GLY
SEQRES   8 A  175  SER PHE GLU SER ALA SER GLU LEU ARG ILE GLN LEU ARG
SEQRES   9 A  175  ARG THR HIS GLN ALA ASP HIS VAL PRO ILE ILE LEU VAL
SEQRES  10 A  175  GLY ASN LYS ALA ASP LEU ALA ARG CYS ARG GLU VAL SER
SEQRES  11 A  175  VAL GLU GLU GLY ARG ALA CYS ALA VAL VAL PHE ASP CYS
SEQRES  12 A  175  LYS PHE ILE GLU THR SER ALA THR LEU GLN HIS ASN VAL
SEQRES  13 A  175  ALA GLU LEU PHE GLU GLY VAL VAL ARG GLN LEU ARG LEU
SEQRES  14 A  175  ARG ARG ARG ASP SER ALA
SEQRES   1 B  175  SER MET ALA LEU TYR ARG VAL VAL LEU LEU GLY ASP PRO
SEQRES   2 B  175  GLY VAL GLY LYS THR SER LEU ALA SER LEU PHE ALA GLY
SEQRES   3 B  175  LYS GLN GLU ARG ASP LEU HIS GLU GLN LEU GLY GLU ASP
SEQRES   4 B  175  VAL TYR GLU ARG THR LEU THR VAL ASP GLY GLU ASP THR
SEQRES   5 B  175  THR LEU VAL VAL VAL ASP THR TRP GLU ALA GLU LYS LEU
SEQRES   6 B  175  ASP LYS SER TRP SER GLN GLU SER CYS LEU GLN GLY GLY
SEQRES   7 B  175  SER ALA TYR VAL ILE VAL TYR SER ILE ALA ASP ARG GLY
SEQRES   8 B  175  SER PHE GLU SER ALA SER GLU LEU ARG ILE GLN LEU ARG
SEQRES   9 B  175  ARG THR HIS GLN ALA ASP HIS VAL PRO ILE ILE LEU VAL
SEQRES  10 B  175  GLY ASN LYS ALA ASP LEU ALA ARG CYS ARG GLU VAL SER
SEQRES  11 B  175  VAL GLU GLU GLY ARG ALA CYS ALA VAL VAL PHE ASP CYS
SEQRES  12 B  175  LYS PHE ILE GLU THR SER ALA THR LEU GLN HIS ASN VAL
SEQRES  13 B  175  ALA GLU LEU PHE GLU GLY VAL VAL ARG GLN LEU ARG LEU
SEQRES  14 B  175  ARG ARG ARG ASP SER ALA
SEQRES   1 C  175  SER MET ALA LEU TYR ARG VAL VAL LEU LEU GLY ASP PRO
SEQRES   2 C  175  GLY VAL GLY LYS THR SER LEU ALA SER LEU PHE ALA GLY
SEQRES   3 C  175  LYS GLN GLU ARG ASP LEU HIS GLU GLN LEU GLY GLU ASP
SEQRES   4 C  175  VAL TYR GLU ARG THR LEU THR VAL ASP GLY GLU ASP THR
SEQRES   5 C  175  THR LEU VAL VAL VAL ASP THR TRP GLU ALA GLU LYS LEU
SEQRES   6 C  175  ASP LYS SER TRP SER GLN GLU SER CYS LEU GLN GLY GLY
SEQRES   7 C  175  SER ALA TYR VAL ILE VAL TYR SER ILE ALA ASP ARG GLY
SEQRES   8 C  175  SER PHE GLU SER ALA SER GLU LEU ARG ILE GLN LEU ARG
SEQRES   9 C  175  ARG THR HIS GLN ALA ASP HIS VAL PRO ILE ILE LEU VAL
SEQRES  10 C  175  GLY ASN LYS ALA ASP LEU ALA ARG CYS ARG GLU VAL SER
SEQRES  11 C  175  VAL GLU GLU GLY ARG ALA CYS ALA VAL VAL PHE ASP CYS
SEQRES  12 C  175  LYS PHE ILE GLU THR SER ALA THR LEU GLN HIS ASN VAL
SEQRES  13 C  175  ALA GLU LEU PHE GLU GLY VAL VAL ARG GLN LEU ARG LEU
SEQRES  14 C  175  ARG ARG ARG ASP SER ALA
SEQRES   1 D  175  SER MET ALA LEU TYR ARG VAL VAL LEU LEU GLY ASP PRO
SEQRES   2 D  175  GLY VAL GLY LYS THR SER LEU ALA SER LEU PHE ALA GLY
SEQRES   3 D  175  LYS GLN GLU ARG ASP LEU HIS GLU GLN LEU GLY GLU ASP
SEQRES   4 D  175  VAL TYR GLU ARG THR LEU THR VAL ASP GLY GLU ASP THR
SEQRES   5 D  175  THR LEU VAL VAL VAL ASP THR TRP GLU ALA GLU LYS LEU
SEQRES   6 D  175  ASP LYS SER TRP SER GLN GLU SER CYS LEU GLN GLY GLY
SEQRES   7 D  175  SER ALA TYR VAL ILE VAL TYR SER ILE ALA ASP ARG GLY
SEQRES   8 D  175  SER PHE GLU SER ALA SER GLU LEU ARG ILE GLN LEU ARG
SEQRES   9 D  175  ARG THR HIS GLN ALA ASP HIS VAL PRO ILE ILE LEU VAL
SEQRES  10 D  175  GLY ASN LYS ALA ASP LEU ALA ARG CYS ARG GLU VAL SER
SEQRES  11 D  175  VAL GLU GLU GLY ARG ALA CYS ALA VAL VAL PHE ASP CYS
SEQRES  12 D  175  LYS PHE ILE GLU THR SER ALA THR LEU GLN HIS ASN VAL
SEQRES  13 D  175  ALA GLU LEU PHE GLU GLY VAL VAL ARG GLN LEU ARG LEU
SEQRES  14 D  175  ARG ARG ARG ASP SER ALA
HET     MG  A 252       1
HET     MG  B 252       1
HET     MG  C 252       1
HET     MG  D 252       1
HET     CL  B 253       1
HET     CL  A 253       1
HET    GDP  A1001      28
HET    GDP  B1002      28
HET    GDP  C1003      28
HET    GDP  D1004      28
HETNAM      MG MAGNESIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL   5   MG    4(MG 2+)
FORMUL   9   CL    2(CL 1-)
FORMUL  11  GDP    4(C10 H15 N5 O11 P2)
FORMUL  15  HOH   *16(H2 O)
HELIX    1   1 GLY A   92  GLY A  102  1                                  11
HELIX    2   2 SER A  144  CYS A  150  1                                   7
HELIX    3   3 ASP A  165  THR A  182  1                                  18
HELIX    4   4 SER A  206  ASP A  218  1                                  13
HELIX    5   5 ASN A  231  ARG A  248  1                                  18
HELIX    6   6 GLY B   92  GLY B  102  1                                  11
HELIX    7   7 SER B  144  CYS B  150  1                                   7
HELIX    8   8 ASP B  165  THR B  182  1                                  18
HELIX    9   9 LEU B  199  ARG B  203  5                                   5
HELIX   10  10 SER B  206  ASP B  218  1                                  13
HELIX   11  11 ASN B  231  ARG B  248  1                                  18
HELIX   12  12 GLY C   92  GLY C  102  1                                  11
HELIX   13  13 SER C  144  SER C  149  1                                   6
HELIX   14  14 ASP C  165  ARG C  181  1                                  17
HELIX   15  15 LEU C  199  ARG C  203  5                                   5
HELIX   16  16 SER C  206  VAL C  216  1                                  11
HELIX   17  17 ASN C  231  ARG C  246  1                                  16
HELIX   18  18 GLY D   92  GLY D  102  1                                  11
HELIX   19  19 SER D  144  GLY D  153  1                                  10
HELIX   20  20 ASP D  165  ARG D  181  1                                  17
HELIX   21  21 LEU D  199  ARG D  203  5                                   5
HELIX   22  22 SER D  206  PHE D  217  1                                  12
HELIX   23  23 ASN D  231  ARG D  246  1                                  16
SHEET    1   A 6 VAL A 116  VAL A 123  0
SHEET    2   A 6 GLU A 126  VAL A 133 -1  O  THR A 128   N  LEU A 121
SHEET    3   A 6 LEU A  80  LEU A  86  1  N  VAL A  83   O  VAL A 133
SHEET    4   A 6 ALA A 156  SER A 162  1  O  VAL A 160   N  LEU A  86
SHEET    5   A 6 ILE A 190  ASN A 195  1  O  ASN A 195   N  TYR A 161
SHEET    6   A 6 LYS A 220  GLU A 223  1  O  LYS A 220   N  LEU A 192
SHEET    1   B 6 VAL B 116  VAL B 123  0
SHEET    2   B 6 GLU B 126  VAL B 133 -1  O  VAL B 132   N  TYR B 117
SHEET    3   B 6 LEU B  80  LEU B  86  1  N  VAL B  83   O  VAL B 131
SHEET    4   B 6 ALA B 156  SER B 162  1  O  VAL B 160   N  LEU B  86
SHEET    5   B 6 ILE B 190  ASN B 195  1  O  ASN B 195   N  TYR B 161
SHEET    6   B 6 LYS B 220  GLU B 223  1  O  LYS B 220   N  LEU B 192
SHEET    1   C 6 VAL C 116  VAL C 123  0
SHEET    2   C 6 GLU C 126  VAL C 133 -1  O  VAL C 132   N  TYR C 117
SHEET    3   C 6 LEU C  80  LEU C  86  1  N  VAL C  83   O  VAL C 131
SHEET    4   C 6 ALA C 156  SER C 162  1  O  VAL C 160   N  LEU C  86
SHEET    5   C 6 ILE C 190  ASN C 195  1  O  ASN C 195   N  TYR C 161
SHEET    6   C 6 LYS C 220  GLU C 223  1  O  LYS C 220   N  LEU C 192
SHEET    1   D 6 VAL D 116  VAL D 123  0
SHEET    2   D 6 GLU D 126  VAL D 133 -1  O  VAL D 132   N  TYR D 117
SHEET    3   D 6 LEU D  80  LEU D  86  1  N  VAL D  83   O  VAL D 131
SHEET    4   D 6 ALA D 156  SER D 162  1  O  VAL D 160   N  LEU D  86
SHEET    5   D 6 ILE D 190  ASN D 195  1  O  ASN D 195   N  TYR D 161
SHEET    6   D 6 LYS D 220  GLU D 223  1  O  LYS D 220   N  LEU D 192
LINK        MG    MG A 252                 O   HOH A   2     1555   1555  2.04
LINK        MG    MG A 252                 OG1 THR A  94     1555   1555  2.16
LINK        MG    MG A 252                 O   HOH A   1     1555   1555  2.05
LINK        MG    MG A 252                 O   HOH A   4     1555   1555  1.88
LINK        MG    MG A 252                 O2B GDP A1001     1555   1555  2.13
LINK        MG    MG A 252                 O   HOH A   3     1555   1555  1.81
LINK        MG    MG B 252                 O3B GDP B1002     1555   1555  3.15
LINK        MG    MG B 252                 O   HOH B   8     1555   1555  1.96
LINK        MG    MG B 252                 O   HOH B   5     1555   1555  2.16
LINK        MG    MG B 252                 O   HOH B   6     1555   1555  1.98
LINK        MG    MG B 252                 OG1 THR B  94     1555   1555  2.35
LINK        MG    MG B 252                 O   HOH B   7     1555   1555  2.02
LINK        MG    MG B 252                 O2B GDP B1002     1555   1555  2.07
LINK        MG    MG C 252                 O   HOH C   9     1555   1555  1.97
LINK        MG    MG C 252                 O   HOH C  10     1555   1555  1.97
LINK        MG    MG C 252                 O   HOH C  11     1555   1555  2.12
LINK        MG    MG C 252                 O   HOH C  12     1555   1555  2.04
LINK        MG    MG C 252                 O2B GDP C1003     1555   1555  2.16
LINK        MG    MG C 252                 OG1 THR C  94     1555   1555  1.84
LINK        MG    MG D 252                 O   HOH D  14     1555   1555  1.84
LINK        MG    MG D 252                 O   HOH D  16     1555   1555  2.04
LINK        MG    MG D 252                 O   HOH D  13     1555   1555  1.81
LINK        MG    MG D 252                 O   HOH D  15     1555   1555  1.80
LINK        MG    MG D 252                 O2B GDP D1004     1555   1555  1.97
LINK        MG    MG D 252                 OG1 THR D  94     1555   1555  2.17
SITE     1 AC1  6 HOH A   1  HOH A   2  HOH A   3  HOH A   4
SITE     2 AC1  6 THR A  94  GDP A1001
SITE     1 AC2  6 HOH B   5  HOH B   6  HOH B   7  HOH B   8
SITE     2 AC2  6 THR B  94  GDP B1002
SITE     1 AC3  6 HOH C   9  HOH C  10  HOH C  11  HOH C  12
SITE     2 AC3  6 THR C  94  GDP C1003
SITE     1 AC4  6 HOH D  13  HOH D  14  HOH D  15  HOH D  16
SITE     2 AC4  6 THR D  94  GDP D1004
SITE     1 AC5  2 SER B 162  LYS B 196
SITE     1 AC6  2 SER A 162  LYS A 196
SITE     1 AC7 17 HOH A   2  HOH A   3  HOH A   4  GLY A  90
SITE     2 AC7 17 VAL A  91  GLY A  92  LYS A  93  THR A  94
SITE     3 AC7 17 SER A  95  ASN A 195  LYS A 196  ASP A 198
SITE     4 AC7 17 LEU A 199  SER A 225  ALA A 226  THR A 227
SITE     5 AC7 17  MG A 252
SITE     1 AC8 17 HOH B   5  HOH B   6  HOH B   7  PRO B  89
SITE     2 AC8 17 GLY B  90  VAL B  91  GLY B  92  LYS B  93
SITE     3 AC8 17 THR B  94  SER B  95  ASN B 195  LYS B 196
SITE     4 AC8 17 ASP B 198  SER B 225  ALA B 226  THR B 227
SITE     5 AC8 17  MG B 252
SITE     1 AC9 18 HOH C   9  HOH C  10  HOH C  12  PRO C  89
SITE     2 AC9 18 GLY C  90  VAL C  91  GLY C  92  LYS C  93
SITE     3 AC9 18 THR C  94  SER C  95  ASN C 195  LYS C 196
SITE     4 AC9 18 ASP C 198  LEU C 199  SER C 225  ALA C 226
SITE     5 AC9 18 THR C 227   MG C 252
SITE     1 BC1 17 HOH D  13  HOH D  15  HOH D  16  PRO D  89
SITE     2 BC1 17 GLY D  90  VAL D  91  GLY D  92  LYS D  93
SITE     3 BC1 17 THR D  94  SER D  95  ASN D 195  LYS D 196
SITE     4 BC1 17 ASP D 198  SER D 225  ALA D 226  THR D 227
SITE     5 BC1 17  MG D 252
CRYST1   43.640  102.284  165.565  90.00  90.00  90.00 P 21 21 21   16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.022915  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009777  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006040        0.00000
      
PROCHECK
Go to PROCHECK summary
 References