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PDBsum entry 3rg6

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Photosynthesis PDB id
3rg6
Jmol
Contents
Protein chains
442 a.a.
115 a.a.
107 a.a.
HEADER    PHOTOSYNTHESIS                          07-APR-11   3RG6
TITLE     CRYSTAL STRUCTURE OF A CHAPERONE-BOUND ASSEMBLY INTERMEDIATE OF FORM I
TITLE    2 RUBISCO
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RBCX PROTEIN;
COMPND   9 CHAIN: C, D, E, F;
COMPND  10 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE   3 ORGANISM_TAXID: 269084;
SOURCE   4 STRAIN: ATCC 27144 / PCC 6301 / SAUG 1402/1;
SOURCE   5 GENE: CBBL, RBCA, RBCL, SYC0130_C;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: ANABAENA SP.;
SOURCE  13 ORGANISM_TAXID: 1167;
SOURCE  14 GENE: RBCX;
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS    PHOTOSYNTHESIS, ASSEMBLY CHAPERONE, TIM BARREL (RBCL), CARBON
KEYWDS   2 FIXATION (RBCL) COMPLEX ASSEMBLY, PROTEIN FOLDING, CHAPERONE (RBCX),
KEYWDS   3 RBCS (RBCL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.BRACHER,A.STARLING-WINDHOF,F.U.HARTL,M.HAYER-HARTL
REVDAT   4   16-JUL-14 3RG6    1       REMARK
REVDAT   3   17-AUG-11 3RG6    1       JRNL
REVDAT   2   03-AUG-11 3RG6    1       JRNL
REVDAT   1   20-JUL-11 3RG6    0
JRNL        AUTH   A.BRACHER,A.STARLING-WINDHOF,F.U.HARTL,M.HAYER-HARTL
JRNL        TITL   CRYSTAL STRUCTURE OF A CHAPERONE-BOUND ASSEMBLY INTERMEDIATE
JRNL        TITL 2 OF FORM I RUBISCO.
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   875 2011
JRNL        REFN                   ISSN 1545-9993
JRNL        PMID   21765418
JRNL        DOI    10.1038/NSMB.2090
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   C.LIU,A.L.YOUNG,A.STARLING-WINDHOF,A.BRACHER,
REMARK   1  AUTH 2 S.SASCHENBRECKER,B.V.RAO,K.V.RAO,O.BERNINGHAUSEN,T.MIELKE,
REMARK   1  AUTH 3 F.U.HARTL,R.BECKMANN,M.HAYER-HARTL
REMARK   1  TITL   COUPLED CHAPERONE ACTION IN FOLDING AND ASSEMBLY OF
REMARK   1  TITL 2 HEXADECAMERIC RUBISCO.
REMARK   1  REF    NATURE                        V. 463   197 2010
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1  PMID   20075914
REMARK   1  DOI    10.1038/NATURE08651
REMARK   1 REFERENCE 2
REMARK   1  AUTH   S.SASCHENBRECKER,A.BRACHER,K.V.RAO,B.V.RAO,F.U.HARTL,
REMARK   1  AUTH 2 M.HAYER-HARTL
REMARK   1  TITL   STRUCTURE AND FUNCTION OF RBCX, AN ASSEMBLY CHAPERONE FOR
REMARK   1  TITL 2 HEXADECAMERIC RUBISCO.
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V. 129  1189 2007
REMARK   1  REFN                   ISSN 0092-8674
REMARK   1  PMID   17574029
REMARK   1  DOI    10.1016/J.CELL.2007.04.025
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.NEWMAN,C.I.BRANDEN,T.A.JONES
REMARK   1  TITL   STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE
REMARK   1  TITL 2 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM SYNECHOCOCCUS
REMARK   1  TITL 3 PCC6301.
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   548 1993
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1  PMID   15299492
REMARK   1  DOI    10.1107/S090744499300530X
REMARK   2
REMARK   2 RESOLUTION.    3.20 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) : 3.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.5
REMARK   3   NUMBER OF REFLECTIONS             : 41214
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) : 0.217
REMARK   3   R VALUE            (WORKING SET) : 0.216
REMARK   3   FREE R VALUE                     : 0.245
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2067
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) : 3.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1439
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 42.74
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320
REMARK   3   BIN FREE R VALUE SET COUNT          : 71
REMARK   3   BIN FREE R VALUE                    : 0.3410
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 10078
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 89.96
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.33000
REMARK   3    B22 (A**2) : 3.33000
REMARK   3    B33 (A**2) : -6.66000
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): 0.429
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.320
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.556
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10302 ; 0.007 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14002 ; 1.073 ; 1.949
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1311 ; 5.178 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   462 ;34.153 ;23.658
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1591 ;20.117 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    68 ;17.329 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1573 ; 0.074 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7910 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5007 ; 0.209 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7049 ; 0.302 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   326 ; 0.156 ; 0.200
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):    31 ; 0.221 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.183 ; 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):  6686 ; 0.174 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10411 ; 0.331 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4045 ; 0.546 ; 3.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3591 ; 0.954 ; 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 : 3
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     18       A      61      4
REMARK   3           1     B     18       B      61      4
REMARK   3           2     A     72       A     329      4
REMARK   3           2     B     72       B     329      4
REMARK   3           3     A    334       A     401      4
REMARK   3           3     B    334       B     401      4
REMARK   3           4     A    405       A     469      4
REMARK   3           4     B    405       B     469      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3333 ; 0.230 ; 0.500
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3333 ; 0.200 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : C E
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C      2       C     115      4
REMARK   3           1     E      2       E     115      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    851 ; 0.310 ; 0.500
REMARK   3   MEDIUM THERMAL     2    C (A**2):    851 ; 0.080 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : D E
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     D      1       D     105      4
REMARK   3           1     E      1       E     105      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  3    D    (A):    767 ; 0.450 ; 0.500
REMARK   3   MEDIUM THERMAL     3    D (A**2):    767 ; 0.140 ; 2.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 8
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    18        A    63
REMARK   3    RESIDUE RANGE :   A    71        A   401
REMARK   3    RESIDUE RANGE :   A   405        A   458
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6360  15.8845  12.9478
REMARK   3    T TENSOR
REMARK   3      T11:  -0.3890 T22:  -0.2752
REMARK   3      T33:  -0.4432 T12:   0.1658
REMARK   3      T13:   0.0135 T23:  -0.0976
REMARK   3    L TENSOR
REMARK   3      L11:   1.8660 L22:   1.0938
REMARK   3      L33:   2.2522 L12:  -0.2968
REMARK   3      L13:   0.3152 L23:  -0.4237
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0164 S12:  -0.0827 S13:   0.2249
REMARK   3      S21:   0.0744 S22:  -0.0844 S23:   0.2114
REMARK   3      S31:  -0.4846 S32:  -0.6422 S33:   0.1008
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 4
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    18        B    61
REMARK   3    RESIDUE RANGE :   B    71        B   331
REMARK   3    RESIDUE RANGE :   B   334        B   401
REMARK   3    RESIDUE RANGE :   B   405        B   458
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0778  27.4682 -12.9232
REMARK   3    T TENSOR
REMARK   3      T11:  -0.3255 T22:  -0.4028
REMARK   3      T33:  -0.4283 T12:   0.2425
REMARK   3      T13:  -0.0975 T23:   0.0061
REMARK   3    L TENSOR
REMARK   3      L11:   1.0614 L22:   2.0594
REMARK   3      L33:   2.3648 L12:  -0.3267
REMARK   3      L13:  -0.6672 L23:   0.3694
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1050 S12:   0.0552 S13:   0.1233
REMARK   3      S21:  -0.0869 S22:   0.0661 S23:   0.2651
REMARK   3      S31:  -0.4312 S32:  -0.6930 S33:   0.0388
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 :   C     1        C   115
REMARK   3    ORIGIN FOR THE GROUP (A): -50.1541  53.0446 -31.7337
REMARK   3    T TENSOR
REMARK   3      T11:   0.8662 T22:   0.6381
REMARK   3      T33:   0.6761 T12:   0.4944
REMARK   3      T13:  -0.1853 T23:   0.2909
REMARK   3    L TENSOR
REMARK   3      L11:   1.2369 L22:   5.8512
REMARK   3      L33:   5.8975 L12:  -0.6401
REMARK   3      L13:  -0.4124 L23:   0.5489
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0572 S12:   0.2916 S13:   0.8923
REMARK   3      S21:  -0.8046 S22:   0.2318 S23:   0.0203
REMARK   3      S31:  -1.4238 S32:   0.2529 S33:  -0.1745
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 :   D     1        D   107
REMARK   3    ORIGIN FOR THE GROUP (A): -50.2352  41.7221 -25.9675
REMARK   3    T TENSOR
REMARK   3      T11:   0.3975 T22:   0.4701
REMARK   3      T33:   0.0591 T12:   0.6281
REMARK   3      T13:  -0.2072 T23:   0.0879
REMARK   3    L TENSOR
REMARK   3      L11:   1.2269 L22:   7.1088
REMARK   3      L33:   4.9943 L12:  -1.0506
REMARK   3      L13:   0.0774 L23:  -0.4010
REMARK   3    S TENSOR
REMARK   3      S11:   0.1730 S12:   0.3717 S13:   0.5485
REMARK   3      S21:  -0.1830 S22:   0.1110 S23:   0.0813
REMARK   3      S31:  -1.1126 S32:  -0.4685 S33:  -0.2840
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 :   E     2        E   115
REMARK   3    ORIGIN FOR THE GROUP (A): -62.8986  39.2355  31.7365
REMARK   3    T TENSOR
REMARK   3      T11:   0.7522 T22:   0.7163
REMARK   3      T33:   0.7850 T12:   0.3223
REMARK   3      T13:   0.3817 T23:  -0.0550
REMARK   3    L TENSOR
REMARK   3      L11:   5.2186 L22:   1.1958
REMARK   3      L33:   5.7587 L12:  -0.0839
REMARK   3      L13:   0.8382 L23:  -0.2804
REMARK   3    S TENSOR
REMARK   3      S11:   0.2753 S12:  -0.7037 S13:  -0.3035
REMARK   3      S21:   0.3306 S22:   0.1203 S23:   1.1047
REMARK   3      S31:   0.7854 S32:  -1.4320 S33:  -0.3956
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 :   F     1        F   106
REMARK   3    ORIGIN FOR THE GROUP (A): -51.4581  40.7804  25.8693
REMARK   3    T TENSOR
REMARK   3      T11:   0.4374 T22:   0.0046
REMARK   3      T33:   0.1187 T12:   0.5801
REMARK   3      T13:   0.1440 T23:  -0.1773
REMARK   3    L TENSOR
REMARK   3      L11:   8.0618 L22:   3.9222
REMARK   3      L33:   4.6827 L12:   1.1716
REMARK   3      L13:   0.2191 L23:   0.2565
REMARK   3    S TENSOR
REMARK   3      S11:   0.0451 S12:  -0.3198 S13:  -0.0075
REMARK   3      S21:   0.1914 S22:   0.0767 S23:   1.0180
REMARK   3      S31:  -0.0407 S32:  -0.7894 S33:  -0.1218
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   459        A   469
REMARK   3    ORIGIN FOR THE GROUP (A): -49.2786  37.9518  36.4137
REMARK   3    T TENSOR
REMARK   3      T11:   0.0122 T22:   0.0017
REMARK   3      T33:   0.0246 T12:   0.0313
REMARK   3      T13:  -0.0580 T23:  -0.0125
REMARK   3    L TENSOR
REMARK   3      L11:  78.9139 L22:  17.4776
REMARK   3      L33:  20.9288 L12: -15.0324
REMARK   3      L13: -16.4215 L23:   3.1017
REMARK   3    S TENSOR
REMARK   3      S11:   0.5681 S12:   3.3852 S13:  -3.0380
REMARK   3      S21:   0.8414 S22:  -0.6307 S23:   1.7318
REMARK   3      S31:   0.4818 S32:  -0.5664 S33:   0.0626
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 :   B   459        B   469
REMARK   3    ORIGIN FOR THE GROUP (A): -46.6758  39.8841 -36.3528
REMARK   3    T TENSOR
REMARK   3      T11:   0.0078 T22:   0.0039
REMARK   3      T33:   0.0048 T12:   0.0013
REMARK   3      T13:  -0.0088 T23:   0.0089
REMARK   3    L TENSOR
REMARK   3      L11:  17.2703 L22:  73.8894
REMARK   3      L33:  39.8265 L12: -26.9248
REMARK   3      L13:  17.3178 L23: -33.6510
REMARK   3    S TENSOR
REMARK   3      S11:  -2.5300 S12:  -1.4737 S13:   1.2146
REMARK   3      S21:   2.2811 S22:   3.7128 S23:  -2.0892
REMARK   3      S31:  -2.5468 S32:  -0.9235 S33:  -1.1828
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3RG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064890.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97908
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41265
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.999
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.8
REMARK 200  DATA REDUNDANCY                : 3.200
REMARK 200  R MERGE                    (I) : 0.10900
REMARK 200  R SYM                      (I) : 0.10900
REMARK 200   FOR THE DATA SET  : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.37
REMARK 200  COMPLETENESS FOR SHELL     (%) : 48.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.31100
REMARK 200  R SYM FOR SHELL            (I) : 0.31100
REMARK 200   FOR SHELL         : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1RBL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 71.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-17 % 2-METHYL-2,4-PENTANEDIOL, 0.1
REMARK 280  M KCL, 0.1 M TRIS-HCL, PH 8.7, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000      122.37500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      122.37500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.83450
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      122.37500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      122.37500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.83450
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000      122.37500
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000      122.37500
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       49.83450
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000      122.37500
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000      122.37500
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       49.83450
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 300 REMARK: AUTHORS STATE THAT THIS COMPLEX COMPOSITION HAS BEEN
REMARK 300 VERIFIED BY ELECTRON MICROSCOPY AND SIZE EXCLUSION CHROMATOGRAPHY
REMARK 300 (SEE REFERENCE 1).
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: 24-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, B, E, F
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     PRO A     2
REMARK 465     LYS A     3
REMARK 465     THR A     4
REMARK 465     GLN A     5
REMARK 465     SER A     6
REMARK 465     ALA A     7
REMARK 465     ALA A     8
REMARK 465     GLY A     9
REMARK 465     TYR A    10
REMARK 465     LYS A    11
REMARK 465     ALA A    12
REMARK 465     GLY A    13
REMARK 465     VAL A    14
REMARK 465     LYS A    15
REMARK 465     ASP A    16
REMARK 465     TYR A    17
REMARK 465     THR A    64
REMARK 465     THR A    65
REMARK 465     VAL A    66
REMARK 465     TRP A    67
REMARK 465     THR A    68
REMARK 465     ASP A    69
REMARK 465     LEU A    70
REMARK 465     GLY A   402
REMARK 465     THR A   403
REMARK 465     LEU A   404
REMARK 465     ASP A   470
REMARK 465     LYS A   471
REMARK 465     LEU A   472
REMARK 465     MET C   -19
REMARK 465     GLY C   -18
REMARK 465     SER C   -17
REMARK 465     SER C   -16
REMARK 465     HIS C   -15
REMARK 465     HIS C   -14
REMARK 465     HIS C   -13
REMARK 465     HIS C   -12
REMARK 465     HIS C   -11
REMARK 465     HIS C   -10
REMARK 465     SER C    -9
REMARK 465     SER C    -8
REMARK 465     GLY C    -7
REMARK 465     LEU C    -6
REMARK 465     VAL C    -5
REMARK 465     PRO C    -4
REMARK 465     ARG C    -3
REMARK 465     GLY C    -2
REMARK 465     SER C    -1
REMARK 465     HIS C     0
REMARK 465     PRO C   116
REMARK 465     SER C   117
REMARK 465     PRO C   118
REMARK 465     GLU C   119
REMARK 465     SER C   120
REMARK 465     GLU C   121
REMARK 465     GLN C   122
REMARK 465     GLN C   123
REMARK 465     GLN C   124
REMARK 465     PHE C   125
REMARK 465     SER C   126
REMARK 465     ASP C   127
REMARK 465     PRO C   128
REMARK 465     ASP C   129
REMARK 465     TRP C   130
REMARK 465     ASP C   131
REMARK 465     ASN C   132
REMARK 465     LEU C   133
REMARK 465     ALA C   134
REMARK 465     SER C   135
REMARK 465     MET D   -19
REMARK 465     GLY D   -18
REMARK 465     SER D   -17
REMARK 465     SER D   -16
REMARK 465     HIS D   -15
REMARK 465     HIS D   -14
REMARK 465     HIS D   -13
REMARK 465     HIS D   -12
REMARK 465     HIS D   -11
REMARK 465     HIS D   -10
REMARK 465     SER D    -9
REMARK 465     SER D    -8
REMARK 465     GLY D    -7
REMARK 465     LEU D    -6
REMARK 465     VAL D    -5
REMARK 465     PRO D    -4
REMARK 465     ARG D    -3
REMARK 465     GLY D    -2
REMARK 465     SER D    -1
REMARK 465     HIS D     0
REMARK 465     MET D   108
REMARK 465     THR D   109
REMARK 465     GLN D   110
REMARK 465     VAL D   111
REMARK 465     SER D   112
REMARK 465     LEU D   113
REMARK 465     SER D   114
REMARK 465     HIS D   115
REMARK 465     PRO D   116
REMARK 465     SER D   117
REMARK 465     PRO D   118
REMARK 465     GLU D   119
REMARK 465     SER D   120
REMARK 465     GLU D   121
REMARK 465     GLN D   122
REMARK 465     GLN D   123
REMARK 465     GLN D   124
REMARK 465     PHE D   125
REMARK 465     SER D   126
REMARK 465     ASP D   127
REMARK 465     PRO D   128
REMARK 465     ASP D   129
REMARK 465     TRP D   130
REMARK 465     ASP D   131
REMARK 465     ASN D   132
REMARK 465     LEU D   133
REMARK 465     ALA D   134
REMARK 465     SER D   135
REMARK 465     MET B     1
REMARK 465     PRO B     2
REMARK 465     LYS B     3
REMARK 465     THR B     4
REMARK 465     GLN B     5
REMARK 465     SER B     6
REMARK 465     ALA B     7
REMARK 465     ALA B     8
REMARK 465     GLY B     9
REMARK 465     TYR B    10
REMARK 465     LYS B    11
REMARK 465     ALA B    12
REMARK 465     GLY B    13
REMARK 465     VAL B    14
REMARK 465     LYS B    15
REMARK 465     ASP B    16
REMARK 465     TYR B    17
REMARK 465     THR B    62
REMARK 465     TRP B    63
REMARK 465     THR B    64
REMARK 465     THR B    65
REMARK 465     VAL B    66
REMARK 465     TRP B    67
REMARK 465     THR B    68
REMARK 465     ASP B    69
REMARK 465     LEU B    70
REMARK 465     LEU B   332
REMARK 465     GLU B   333
REMARK 465     GLY B   402
REMARK 465     THR B   403
REMARK 465     LEU B   404
REMARK 465     ASP B   470
REMARK 465     LYS B   471
REMARK 465     LEU B   472
REMARK 465     MET E   -19
REMARK 465     GLY E   -18
REMARK 465     SER E   -17
REMARK 465     SER E   -16
REMARK 465     HIS E   -15
REMARK 465     HIS E   -14
REMARK 465     HIS E   -13
REMARK 465     HIS E   -12
REMARK 465     HIS E   -11
REMARK 465     HIS E   -10
REMARK 465     SER E    -9
REMARK 465     SER E    -8
REMARK 465     GLY E    -7
REMARK 465     LEU E    -6
REMARK 465     VAL E    -5
REMARK 465     PRO E    -4
REMARK 465     ARG E    -3
REMARK 465     GLY E    -2
REMARK 465     SER E    -1
REMARK 465     HIS E     0
REMARK 465     MET E     1
REMARK 465     PRO E   116
REMARK 465     SER E   117
REMARK 465     PRO E   118
REMARK 465     GLU E   119
REMARK 465     SER E   120
REMARK 465     GLU E   121
REMARK 465     GLN E   122
REMARK 465     GLN E   123
REMARK 465     GLN E   124
REMARK 465     PHE E   125
REMARK 465     SER E   126
REMARK 465     ASP E   127
REMARK 465     PRO E   128
REMARK 465     ASP E   129
REMARK 465     TRP E   130
REMARK 465     ASP E   131
REMARK 465     ASN E   132
REMARK 465     LEU E   133
REMARK 465     ALA E   134
REMARK 465     SER E   135
REMARK 465     MET F   -19
REMARK 465     GLY F   -18
REMARK 465     SER F   -17
REMARK 465     SER F   -16
REMARK 465     HIS F   -15
REMARK 465     HIS F   -14
REMARK 465     HIS F   -13
REMARK 465     HIS F   -12
REMARK 465     HIS F   -11
REMARK 465     HIS F   -10
REMARK 465     SER F    -9
REMARK 465     SER F    -8
REMARK 465     GLY F    -7
REMARK 465     LEU F    -6
REMARK 465     VAL F    -5
REMARK 465     PRO F    -4
REMARK 465     ARG F    -3
REMARK 465     GLY F    -2
REMARK 465     SER F    -1
REMARK 465     HIS F     0
REMARK 465     ARG F   107
REMARK 465     MET F   108
REMARK 465     THR F   109
REMARK 465     GLN F   110
REMARK 465     VAL F   111
REMARK 465     SER F   112
REMARK 465     LEU F   113
REMARK 465     SER F   114
REMARK 465     HIS F   115
REMARK 465     PRO F   116
REMARK 465     SER F   117
REMARK 465     PRO F   118
REMARK 465     GLU F   119
REMARK 465     SER F   120
REMARK 465     GLU F   121
REMARK 465     GLN F   122
REMARK 465     GLN F   123
REMARK 465     GLN F   124
REMARK 465     PHE F   125
REMARK 465     SER F   126
REMARK 465     ASP F   127
REMARK 465     PRO F   128
REMARK 465     ASP F   129
REMARK 465     TRP F   130
REMARK 465     ASP F   131
REMARK 465     ASN F   132
REMARK 465     LEU F   133
REMARK 465     ALA F   134
REMARK 465     SER F   135
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  18    CG   CD   CE   NZ
REMARK 470     THR A  62    OG1  CG2
REMARK 470     LEU A  71    CG   CD1  CD2
REMARK 470     THR A  72    OG1  CG2
REMARK 470     ASP A  73    CG   OD1  OD2
REMARK 470     GLN A  88    CG   CD   OE1  NE2
REMARK 470     LYS A 125    CG   CD   CE   NZ
REMARK 470     LYS A 172    CG   CD   CE   NZ
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 331    CG   CD   CE   NZ
REMARK 470     LYS A 336    CG   CD   CE   NZ
REMARK 470     TYR A 435    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ARG A 436    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 460    CG   CD   CE   NZ
REMARK 470     LYS A 463    CG   CD   CE   NZ
REMARK 470     LYS C   4    CG   CD   CE   NZ
REMARK 470     LYS C   8    CG   CD   CE   NZ
REMARK 470     LYS C  12    CG   CD   CE   NZ
REMARK 470     LYS C  54    CG   CD   CE   NZ
REMARK 470     GLU C  57    CG   CD   OE1  OE2
REMARK 470     GLU C  58    CG   CD   OE1  OE2
REMARK 470     LEU C  61    CG   CD1  CD2
REMARK 470     LYS C  63    CG   CD   CE   NZ
REMARK 470     GLU C  83    CG   CD   OE1  OE2
REMARK 470     GLN C  95    CG   CD   OE1  NE2
REMARK 470     GLU C  99    CG   CD   OE1  OE2
REMARK 470     GLU C 106    CG   CD   OE1  OE2
REMARK 470     ARG C 107    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN C 110    CG   CD   OE1  NE2
REMARK 470     HIS C 115    CG   ND1  CD2  CE1  NE2
REMARK 470     MET D   1    CG   SD   CE
REMARK 470     LYS D   4    CG   CD   CE   NZ
REMARK 470     LYS D   8    CG   CD   CE   NZ
REMARK 470     LYS D  12    CG   CD   CE   NZ
REMARK 470     SER D  45    OG
REMARK 470     LYS D  54    CG   CD   CE   NZ
REMARK 470     GLU D  62    CG   CD   OE1  OE2
REMARK 470     GLU D  83    CG   CD   OE1  OE2
REMARK 470     GLU D  87    CG   CD   OE1  OE2
REMARK 470     GLN D  95    CG   CD   OE1  NE2
REMARK 470     MET D  98    CG   SD   CE
REMARK 470     GLU D  99    CG   CD   OE1  OE2
REMARK 470     LYS D 100    CG   CD   CE   NZ
REMARK 470     ARG D 102    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN D 103    CG   CD   OE1  NE2
REMARK 470     GLU D 106    CG   CD   OE1  OE2
REMARK 470     ARG D 107    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B  18    CG   CD   CE   NZ
REMARK 470     LEU B  71    CG   CD1  CD2
REMARK 470     THR B  72    OG1  CG2
REMARK 470     ASP B  73    CG   OD1  OD2
REMARK 470     LYS B 125    CG   CD   CE   NZ
REMARK 470     LYS B 172    CG   CD   CE   NZ
REMARK 470     LYS B 174    CG   CD   CE   NZ
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 331    CG   CD   CE   NZ
REMARK 470     ASP B 335    CG   OD1  OD2
REMARK 470     LYS B 336    CG   CD   CE   NZ
REMARK 470     GLU B 389    CG   CD   OE1  OE2
REMARK 470     TYR B 435    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ARG B 436    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 460    CG   CD   CE   NZ
REMARK 470     LYS B 463    CG   CD   CE   NZ
REMARK 470     GLU B 465    CG   CD   OE1  OE2
REMARK 470     GLU B 467    CG   CD   OE1  OE2
REMARK 470     LYS E   4    CG   CD   CE   NZ
REMARK 470     LYS E   8    CG   CD   CE   NZ
REMARK 470     LYS E  12    CG   CD   CE   NZ
REMARK 470     LYS E  48    CG   CD   CE   NZ
REMARK 470     LYS E  54    CG   CD   CE   NZ
REMARK 470     GLU E  57    CG   CD   OE1  OE2
REMARK 470     GLU E  58    CG   CD   OE1  OE2
REMARK 470     LEU E  61    CG   CD1  CD2
REMARK 470     LYS E  63    CG   CD   CE   NZ
REMARK 470     GLU E  83    CG   CD   OE1  OE2
REMARK 470     GLU E  87    CG   CD   OE1  OE2
REMARK 470     GLU E  99    CG   CD   OE1  OE2
REMARK 470     GLU E 106    CG   CD   OE1  OE2
REMARK 470     ARG E 107    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN E 110    CG   CD   OE1  NE2
REMARK 470     HIS E 115    CG   ND1  CD2  CE1  NE2
REMARK 470     MET F   1    CG   SD   CE
REMARK 470     LYS F   4    CG   CD   CE   NZ
REMARK 470     LYS F   8    CG   CD   CE   NZ
REMARK 470     LYS F  12    CG   CD   CE   NZ
REMARK 470     SER F  45    OG
REMARK 470     LYS F  54    CG   CD   CE   NZ
REMARK 470     GLU F  57    CG   CD   OE1  OE2
REMARK 470     GLU F  62    CG   CD   OE1  OE2
REMARK 470     LYS F  63    CG   CD   CE   NZ
REMARK 470     GLU F  83    CG   CD   OE1  OE2
REMARK 470     GLU F  87    CG   CD   OE1  OE2
REMARK 470     GLN F  95    CG   CD   OE1  NE2
REMARK 470     MET F  98    CG   SD   CE
REMARK 470     GLU F  99    CG   CD   OE1  OE2
REMARK 470     ARG F 102    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN F 103    CG   CD   OE1  NE2
REMARK 470     GLU F 106    CG   CD   OE1  OE2
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    SER A  59     -116.01    -96.58
REMARK 500    THR A  60      -71.83    -76.01
REMARK 500    MET A  74      -38.44    -28.15
REMARK 500    ASP A  75      -40.14    -19.30
REMARK 500    VAL A 121      -14.95    -49.52
REMARK 500    HIS A 150      -55.84   -139.33
REMARK 500    LYS A 174     -114.78    -65.82
REMARK 500    LEU A 175     -165.77    -75.34
REMARK 500    ASN A 204      -74.62   -119.96
REMARK 500    GLN A 209       72.24    167.69
REMARK 500    LEU A 332     -169.69   -101.71
REMARK 500    GLU A 333      162.44    -30.21
REMARK 500    PRO A 407       -7.48    -58.56
REMARK 500    GLU C  62      -73.99   -103.38
REMARK 500    ASN D   2      -75.92    -55.69
REMARK 500    ALA D  46      118.74    -36.46
REMARK 500    VAL D  49      -35.11    -27.44
REMARK 500    GLN D  50      -73.01    -25.90
REMARK 500    GLU D  62      -72.17    -86.56
REMARK 500    MET D  88      -39.93   -135.31
REMARK 500    SER B  59      -98.39    -96.69
REMARK 500    THR B  60      -74.54   -102.00
REMARK 500    GLU B  90      107.06    -48.70
REMARK 500    HIS B 150      -65.93   -138.26
REMARK 500    ILE B 152      -85.10     -0.93
REMARK 500    LYS B 174     -106.28    -77.78
REMARK 500    ASN B 204      -81.74   -108.52
REMARK 500    GLN B 209       76.71    178.08
REMARK 500    ARG B 292       50.69    -96.13
REMARK 500    MET B 294       -4.61     75.74
REMARK 500    ASP B 354       94.29   -162.54
REMARK 500    HIS B 380     -165.73   -103.89
REMARK 500    ASP B 394       78.81   -101.80
REMARK 500    PRO B 407       -7.24    -51.27
REMARK 500    GLU B 467      102.23    -59.63
REMARK 500    GLU E  62      -68.79   -124.27
REMARK 500    GLU F  62      -82.75    -81.26
REMARK 500    GLU F  87        0.73    -66.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WVW   RELATED DB: PDB
REMARK 900 CRYO-EM STRUCTURE MODEL OF THE SAME COMPLEX
REMARK 900 RELATED ID: 3HYB   RELATED DB: PDB
REMARK 900 RBCX DIMER COMPLEX STRUCTURE, CRYSTAL FORM II
REMARK 900 RELATED ID: 2PEO   RELATED DB: PDB
REMARK 900 RBCX DIMER COMPLEX STRUCTURE, CRYSTAL FORM I
REMARK 900 RELATED ID: EMD-1655   RELATED DB: EMDB
REMARK 900 CRYO-EM MAP OF THE SAME COMPLEX
REMARK 900 RELATED ID: 1RBL   RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COMPLETED RUBISCO HOLOENZYME, CLOSED FORM
DBREF  3RG6 A    1   472  UNP    P00880   RBL_SYNP6        1    472
DBREF  3RG6 C    1   135  UNP    Q44212   Q44212_9NOST     1    135
DBREF  3RG6 D    1   135  UNP    Q44212   Q44212_9NOST     1    135
DBREF  3RG6 B    1   472  UNP    P00880   RBL_SYNP6        1    472
DBREF  3RG6 E    1   135  UNP    Q44212   Q44212_9NOST     1    135
DBREF  3RG6 F    1   135  UNP    Q44212   Q44212_9NOST     1    135
SEQADV 3RG6 MET C  -19  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY C  -18  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER C  -17  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER C  -16  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS C  -15  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS C  -14  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS C  -13  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS C  -12  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS C  -11  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS C  -10  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER C   -9  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER C   -8  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY C   -7  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 LEU C   -6  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 VAL C   -5  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 PRO C   -4  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 ARG C   -3  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY C   -2  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER C   -1  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS C    0  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 MET D  -19  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY D  -18  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER D  -17  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER D  -16  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS D  -15  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS D  -14  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS D  -13  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS D  -12  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS D  -11  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS D  -10  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER D   -9  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER D   -8  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY D   -7  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 LEU D   -6  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 VAL D   -5  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 PRO D   -4  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 ARG D   -3  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY D   -2  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER D   -1  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS D    0  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 MET E  -19  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY E  -18  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER E  -17  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER E  -16  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS E  -15  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS E  -14  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS E  -13  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS E  -12  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS E  -11  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS E  -10  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER E   -9  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER E   -8  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY E   -7  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 LEU E   -6  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 VAL E   -5  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 PRO E   -4  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 ARG E   -3  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY E   -2  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER E   -1  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS E    0  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 MET F  -19  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY F  -18  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER F  -17  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER F  -16  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS F  -15  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS F  -14  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS F  -13  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS F  -12  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS F  -11  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS F  -10  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER F   -9  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER F   -8  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY F   -7  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 LEU F   -6  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 VAL F   -5  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 PRO F   -4  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 ARG F   -3  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 GLY F   -2  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 SER F   -1  UNP  Q44212              EXPRESSION TAG
SEQADV 3RG6 HIS F    0  UNP  Q44212              EXPRESSION TAG
SEQRES   1 A  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 A  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 A  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 A  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 A  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 A  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 A  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 A  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 A  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 A  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 A  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 A  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 A  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 A  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 A  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 A  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 A  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 A  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 A  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 A  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 A  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 A  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 A  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 A  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 A  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 A  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 A  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 A  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 A  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 A  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 A  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 A  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 A  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 A  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 A  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 A  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 A  472  MET ASP LYS LEU
SEQRES   1 C  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 C  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE
SEQRES   3 C  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR
SEQRES   4 C  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU
SEQRES   5 C  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER
SEQRES   6 C  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU
SEQRES   7 C  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET
SEQRES   8 C  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE
SEQRES   9 C  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN
SEQRES  10 C  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN
SEQRES  11 C  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN
SEQRES  12 C  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER
SEQRES   1 D  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 D  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE
SEQRES   3 D  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR
SEQRES   4 D  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU
SEQRES   5 D  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER
SEQRES   6 D  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU
SEQRES   7 D  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET
SEQRES   8 D  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE
SEQRES   9 D  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN
SEQRES  10 D  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN
SEQRES  11 D  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN
SEQRES  12 D  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER
SEQRES   1 B  472  MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES   2 B  472  VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES   3 B  472  THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES   4 B  472  SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES   5 B  472  ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES   6 B  472  VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES   7 B  472  GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES   8 B  472  ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES   9 B  472  PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES  10 B  472  VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES  11 B  472  ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES  12 B  472  THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES  13 B  472  ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES  14 B  472  THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES  15 B  472  GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES  16 B  472  PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES  17 B  472  GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES  18 B  472  ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES  19 B  472  HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES  20 B  472  MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES  21 B  472  ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES  22 B  472  ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES  23 B  472  LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES  24 B  472  ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES  25 B  472  LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES  26 B  472  GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES  27 B  472  THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES  28 B  472  GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES  29 B  472  TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES  30 B  472  GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES  31 B  472  PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES  32 B  472  LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES  33 B  472  ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES  34 B  472  GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES  35 B  472  ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES  36 B  472  LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES  37 B  472  MET ASP LYS LEU
SEQRES   1 E  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 E  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE
SEQRES   3 E  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR
SEQRES   4 E  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU
SEQRES   5 E  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER
SEQRES   6 E  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU
SEQRES   7 E  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET
SEQRES   8 E  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE
SEQRES   9 E  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN
SEQRES  10 E  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN
SEQRES  11 E  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN
SEQRES  12 E  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER
SEQRES   1 F  155  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 F  155  LEU VAL PRO ARG GLY SER HIS MET ASN LEU LYS GLN ILE
SEQRES   3 F  155  ALA LYS ASP THR ALA LYS THR LEU GLN SER TYR LEU THR
SEQRES   4 F  155  TYR GLN ALA LEU ARG THR VAL LEU ALA GLN LEU GLY GLU
SEQRES   5 F  155  THR ASN PRO PRO LEU ALA LEU TRP LEU HIS ASN PHE SER
SEQRES   6 F  155  ALA GLY LYS VAL GLN ASP GLY GLU LYS TYR ILE GLU GLU
SEQRES   7 F  155  LEU PHE LEU GLU LYS PRO ASP LEU ALA LEU ARG ILE MET
SEQRES   8 F  155  THR VAL ARG GLU HIS ILE ALA GLU GLU ILE ALA GLU PHE
SEQRES   9 F  155  LEU PRO GLU MET VAL VAL THR GLY ILE GLN GLN ALA ASN
SEQRES  10 F  155  MET GLU LYS ARG ARG GLN HIS LEU GLU ARG MET THR GLN
SEQRES  11 F  155  VAL SER LEU SER HIS PRO SER PRO GLU SER GLU GLN GLN
SEQRES  12 F  155  GLN PHE SER ASP PRO ASP TRP ASP ASN LEU ALA SER
HELIX    1   1 PRO A   46  SER A   59  1                                  14
HELIX    2   2 ASP A   73  TYR A   77  5                                   5
HELIX    3   3 PRO A  101  PHE A  105  5                                   5
HELIX    4   4 SER A  109  VAL A  118  1                                  10
HELIX    5   5 ASN A  120  PHE A  124  5                                   5
HELIX    6   6 PRO A  138  LYS A  143  1                                   6
HELIX    7   7 GLY A  151  ASN A  160  1                                  10
HELIX    8   8 SER A  178  GLY A  192  1                                  15
HELIX    9   9 ARG A  210  GLY A  230  1                                  21
HELIX   10  10 THR A  243  LEU A  257  1                                  15
HELIX   11  11 PHE A  266  GLY A  270  1                                   5
HELIX   12  12 GLY A  270  GLY A  285  1                                  16
HELIX   13  13 MET A  294  ARG A  300  1                                   7
HELIX   14  14 HIS A  307  GLY A  319  1                                  13
HELIX   15  15 GLY A  334  GLU A  348  1                                  15
HELIX   16  16 ASP A  354  GLY A  358  5                                   5
HELIX   17  17 HIS A  380  TRP A  382  5                                   3
HELIX   18  18 HIS A  383  GLY A  392  1                                  10
HELIX   19  19 GLY A  409  GLY A  431  1                                  23
HELIX   20  20 GLU A  437  LYS A  447  1                                  11
HELIX   21  21 SER A  449  LEU A  458  1                                  10
HELIX   22  22 ASN C    2  LEU C   30  1                                  29
HELIX   23  23 ASN C   34  SER C   45  1                                  12
HELIX   24  24 ASP C   51  LEU C   61  1                                  11
HELIX   25  25 LYS C   63  ALA C   82  1                                  20
HELIX   26  26 PHE C   84  LEU C  113  1                                  30
HELIX   27  27 MET D    1  ASN D   34  1                                  34
HELIX   28  28 ASN D   34  ALA D   46  1                                  13
HELIX   29  29 GLY D   47  GLN D   50  5                                   4
HELIX   30  30 ASP D   51  LYS D   63  1                                  13
HELIX   31  31 LYS D   63  ALA D   82  1                                  20
HELIX   32  32 LEU D   85  ARG D  107  1                                  23
HELIX   33  33 PRO B   46  SER B   59  1                                  14
HELIX   34  34 SER B  109  VAL B  118  1                                  10
HELIX   35  35 PRO B  138  LYS B  143  1                                   6
HELIX   36  36 GLY B  151  ASN B  160  1                                  10
HELIX   37  37 SER B  178  GLY B  192  1                                  15
HELIX   38  38 ARG B  210  GLY B  230  1                                  21
HELIX   39  39 THR B  243  LEU B  257  1                                  15
HELIX   40  40 ASP B  265  GLY B  270  1                                   6
HELIX   41  41 GLY B  270  ASN B  284  1                                  15
HELIX   42  42 HIS B  295  ARG B  300  1                                   6
HELIX   43  43 HIS B  307  GLY B  319  1                                  13
HELIX   44  44 GLY B  334  GLU B  348  1                                  15
HELIX   45  45 ASP B  354  GLY B  358  5                                   5
HELIX   46  46 HIS B  380  TRP B  382  5                                   3
HELIX   47  47 HIS B  383  GLY B  392  1                                  10
HELIX   48  48 GLY B  409  GLY B  431  1                                  23
HELIX   49  49 GLU B  437  GLY B  446  1                                  10
HELIX   50  50 SER B  449  LEU B  458  1                                  10
HELIX   51  51 ASN E    2  ASN E   34  1                                  33
HELIX   52  52 ASN E   34  ALA E   46  1                                  13
HELIX   53  53 ASP E   51  PHE E   60  1                                  10
HELIX   54  54 LYS E   63  ALA E   82  1                                  20
HELIX   55  55 PHE E   84  HIS E  115  1                                  32
HELIX   56  56 MET F    1  ASN F   34  1                                  34
HELIX   57  57 ASN F   34  ALA F   46  1                                  13
HELIX   58  58 GLY F   47  GLN F   50  5                                   4
HELIX   59  59 ASP F   51  LYS F   63  1                                  13
HELIX   60  60 LYS F   63  ALA F   82  1                                  20
HELIX   61  61 LEU F   85  GLU F  106  1                                  22
SHEET    1   A 5 LYS A  80  PRO A  86  0
SHEET    2   A 5 TYR A  94  TYR A 100 -1  O  PHE A  95   N  GLU A  85
SHEET    3   A 5 LEU A  33  PRO A  41 -1  N  LEU A  33   O  TYR A 100
SHEET    4   A 5 ILE A 127  ARG A 136 -1  O  ARG A 128   N  SER A  40
SHEET    5   A 5 GLY A 305  ILE A 306  1  O  GLY A 305   N  LEU A 132
SHEET    1   B 4 MET A 166  LEU A 167  0
SHEET    2   B 4 VAL A 396  LEU A 397  1  O  LEU A 397   N  MET A 166
SHEET    3   B 4 LEU A 372  ALA A 375  1  N  ALA A 375   O  VAL A 396
SHEET    4   B 4 HIS A 322  HIS A 324  1  N  LEU A 323   O  VAL A 374
SHEET    1   C 4 PHE A 196  LYS A 198  0
SHEET    2   C 4 GLY A 234  ASN A 238  1  O  TYR A 236   N  THR A 197
SHEET    3   C 4 ILE A 261  ASP A 265  1  O  MET A 263   N  LEU A 237
SHEET    4   C 4 LEU A 287  HIS A 291  1  O  HIS A 289   N  ILE A 262
SHEET    1   D 2 HIS A 350  ILE A 351  0
SHEET    2   D 2 GLN A 363  ASP A 364 -1  O  GLN A 363   N  ILE A 351
SHEET    1   E 5 LYS B  80  PRO B  86  0
SHEET    2   E 5 TYR B  94  TYR B 100 -1  O  ALA B  99   N  LYS B  80
SHEET    3   E 5 LEU B  33  PRO B  41 -1  N  LEU B  33   O  TYR B 100
SHEET    4   E 5 ILE B 127  ARG B 136 -1  O  ARG B 131   N  ARG B  38
SHEET    5   E 5 GLY B 305  ILE B 306  1  O  GLY B 305   N  LEU B 132
SHEET    1   F 9 MET B 166  THR B 170  0
SHEET    2   F 9 PHE B 196  LYS B 198  1  O  PHE B 196   N  LEU B 167
SHEET    3   F 9 GLY B 234  ASN B 238  1  O  TYR B 236   N  THR B 197
SHEET    4   F 9 ILE B 261  HIS B 264  1  O  MET B 263   N  LEU B 237
SHEET    5   F 9 LEU B 287  ILE B 290  1  O  HIS B 289   N  ILE B 262
SHEET    6   F 9 HIS B 322  HIS B 324  1  O  HIS B 322   N  ILE B 290
SHEET    7   F 9 LEU B 372  ALA B 375  1  O  VAL B 374   N  LEU B 323
SHEET    8   F 9 VAL B 396  GLN B 398  1  O  VAL B 396   N  ALA B 375
SHEET    9   F 9 MET B 166  THR B 170  1  N  MET B 166   O  LEU B 397
SHEET    1   G 2 HIS B 350  ILE B 351  0
SHEET    2   G 2 GLN B 363  ASP B 364 -1  O  GLN B 363   N  ILE B 351
SSBOND   1 CYS A  244    CYS B  244                          1555   1555  2.05
CISPEP   1 LYS A  172    PRO A  173          0         5.78
CISPEP   2 LYS B  172    PRO B  173          0         1.20
CRYST1  244.750  244.750   99.669  90.00  90.00  90.00 I 4          32
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      0.004086  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004086  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010033        0.00000
      
PROCHECK
Go to PROCHECK summary
 References