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PDBsum entry 4gg6

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Immune system PDB id
4gg6
Jmol
Contents
Protein chains
180 a.a.
163 a.a.
173 a.a.
187 a.a.
243 a.a.
177 a.a.
13 a.a.
Ligands
NAG ×3
HEADER    IMMUNE SYSTEM                           06-AUG-12   4GG6
TITLE     PROTEIN COMPLEX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ ALPHA 1 CHAIN;
COMPND   3 CHAIN: A, C;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAINS, UNP RESIDUES 24-206;
COMPND   5 SYNONYM: DC-1 ALPHA CHAIN, DC-ALPHA, HLA-DCA, MHC CLASS II DQA1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ BETA 1 CHAIN;
COMPND   9 CHAIN: B, D;
COMPND  10 FRAGMENT: EXTRACELLULAR DOMAINS, UNP RESIDUES 33-224;
COMPND  11 SYNONYM: MHC CLASS II ANTIGEN DQB1;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: T-CELL RECEPTOR, SP3.4 ALPHA CHAIN;
COMPND  15 CHAIN: E, G;
COMPND  16 FRAGMENT: EXTRACELLULAR DOMAINS;
COMPND  17 ENGINEERED: YES;
COMPND  18 MUTATION: YES;
COMPND  19 MOL_ID: 4;
COMPND  20 MOLECULE: T-CELL RECEPTOR, SP3.4 BETA CHAIN;
COMPND  21 CHAIN: F, H;
COMPND  22 FRAGMENT: EXTRACELLULAR DOMAINS;
COMPND  23 ENGINEERED: YES;
COMPND  24 MUTATION: YES;
COMPND  25 MOL_ID: 5;
COMPND  26 MOLECULE: PEPTIDE FROM ALPHA/BETA-GLIADIN MM1;
COMPND  27 CHAIN: I, J;
COMPND  28 FRAGMENT: DEAMIDATED ALPHA-I GLIADIN PEPTIDE, UNP RESIDUES 243-260;
COMPND  29 SYNONYM: PROLAMIN;
COMPND  30 ENGINEERED: YES;
COMPND  31 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DQA1;
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBACDUAL;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 GENE: HLA-DQB, HLA-DQB1;
SOURCE  16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBACDUAL;
SOURCE  21 MOL_ID: 3;
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  23 ORGANISM_TAXID: 9606;
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE  28 MOL_ID: 4;
SOURCE  29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  30 ORGANISM_TAXID: 9606;
SOURCE  31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  33 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  34 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE  35 MOL_ID: 5;
SOURCE  36 SYNTHETIC: YES;
SOURCE  37 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;
SOURCE  38 ORGANISM_COMMON: WHEAT;
SOURCE  39 ORGANISM_TAXID: 4565;
SOURCE  40 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS    IMMUNE RECEPTOR-LIGAND COMPLEX, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.E.BROUGHTON,A.THEODOSSIS,J.PETERSEN,H.H.REID,J.ROSSJOHN
REVDAT   1   24-OCT-12 4GG6    0
JRNL        AUTH   S.E.BROUGHTON,J.PETERSEN,A.THEODOSSIS,S.W.SCALLY,K.L.LOH,
JRNL        AUTH 2 A.THOMPSON,J.VAN BERGEN,Y.KOOY-WINKELAAR,K.N.HENDERSON,
JRNL        AUTH 3 T.BEDDOE,J.A.TYE-DIN,S.I.MANNERING,A.W.PURCELL,J.MCCLUSKEY,
JRNL        AUTH 4 R.P.ANDERSON,F.KONING,H.H.REID,J.ROSSJOHN
JRNL        TITL   BIASED T CELL RECEPTOR USAGE DIRECTED AGAINST HUMAN
JRNL        TITL 2 LEUKOCYTE ANTIGEN DQ8-RESTRICTED GLIADIN PEPTIDES IS
JRNL        TITL 3 ASSOCIATED WITH CELIAC DISEASE
JRNL        REF    IMMUNITY                                   2012
JRNL        REFN                   ISSN 1074-7613
JRNL        PMID   23063329
JRNL        DOI    10.1016/J.IMMUNI.2012.07.013
REMARK   2
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
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) : 35.88
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.0
REMARK   3   NUMBER OF REFLECTIONS             : 30631
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) : 0.248
REMARK   3   R VALUE            (WORKING SET) : 0.246
REMARK   3   FREE R VALUE                     : 0.285
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1646
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) : 2276
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.50
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240
REMARK   3   BIN FREE R VALUE SET COUNT          : 113
REMARK   3   BIN FREE R VALUE                    : 0.3480
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 11877
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 42
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) : 43.24
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.78000
REMARK   3    B22 (A**2) : 0.61000
REMARK   3    B33 (A**2) : 1.17000
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): 0.597
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.445
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.408
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.877
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.837
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12251 ; 0.006 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16794 ; 0.975 ; 1.939
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1549 ; 5.311 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   532 ;34.130 ;23.816
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1627 ;15.191 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;16.665 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1905 ; 0.062 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9539 ; 0.004 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7852 ; 0.115 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12533 ; 0.224 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4399 ; 0.362 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4261 ; 0.621 ; 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 : 6
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      1       A     155      2
REMARK   3           1     C      1       C     155      2
REMARK   3           2     A    156       A     162      5
REMARK   3           2     C    156       C     162      5
REMARK   3           3     A    163       A     182      2
REMARK   3           3     C    163       C     182      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):    700 ; 0.020 ; 0.050
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    662 ; 0.020 ; 0.500
REMARK   3   LOOSE POSITIONAL   1    A    (A):      7 ; 0.020 ; 5.000
REMARK   3   TIGHT THERMAL      1    A (A**2):    700 ; 0.020 ; 0.500
REMARK   3   MEDIUM THERMAL     1    A (A**2):    662 ; 0.030 ; 2.000
REMARK   3   LOOSE THERMAL      1    A (A**2):      7 ; 0.020 ;10.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : B D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 9
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B      3       B     101      2
REMARK   3           1     D      3       D     101      2
REMARK   3           2     B    102       B     115      5
REMARK   3           2     D    102       D     115      5
REMARK   3           3     B    116       B     131      2
REMARK   3           3     D    116       D     131      2
REMARK   3           4     B    132       B     142      5
REMARK   3           4     D    132       D     142      5
REMARK   3           5     B    143       B     161      2
REMARK   3           5     D    143       D     161      2
REMARK   3           6     B    162       B     171      5
REMARK   3           6     D    162       D     171      5
REMARK   3           7     B    172       B     185      2
REMARK   3           7     D    172       D     185      2
REMARK   3           8     B    186       B     189      5
REMARK   3           8     D    186       D     189      5
REMARK   3           9     B      2       B       2      5
REMARK   3           9     D      2       D       2      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    B    (A):    592 ; 0.300 ; 0.050
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    612 ; 0.390 ; 0.500
REMARK   3   LOOSE POSITIONAL   2    B    (A):     30 ; 1.060 ; 5.000
REMARK   3   TIGHT THERMAL      2    B (A**2):    592 ; 0.110 ; 0.500
REMARK   3   MEDIUM THERMAL     2    B (A**2):    612 ; 0.180 ; 2.000
REMARK   3   LOOSE THERMAL      2    B (A**2):     30 ; 0.130 ;10.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : E G
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 8
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     E      3       E     127      2
REMARK   3           1     G      3       G     127      2
REMARK   3           2     E    128       E     131      5
REMARK   3           2     G    128       G     131      5
REMARK   3           3     E    151       E     180      2
REMARK   3           3     G    151       G     180      2
REMARK   3           4     E    190       E     201      5
REMARK   3           4     G    190       G     201      5
REMARK   3           5     E    132       E     143      2
REMARK   3           5     G    132       G     143      2
REMARK   3           6     E    144       E     150      5
REMARK   3           6     G    144       G     150      5
REMARK   3           7     E    184       E     189      2
REMARK   3           7     G    184       G     189      2
REMARK   3           8     E    181       E     183      5
REMARK   3           8     G    181       G     183      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   3    E    (A):    692 ; 0.020 ; 0.050
REMARK   3   MEDIUM POSITIONAL  3    E    (A):    594 ; 0.030 ; 0.500
REMARK   3   LOOSE POSITIONAL   3    E    (A):      4 ; 0.020 ; 5.000
REMARK   3   TIGHT THERMAL      3    E (A**2):    692 ; 0.020 ; 0.500
REMARK   3   MEDIUM THERMAL     3    E (A**2):    594 ; 0.030 ; 2.000
REMARK   3   LOOSE THERMAL      3    E (A**2):      4 ; 0.020 ;10.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 4
REMARK   3     CHAIN NAMES                    : F H
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     F      2       F     244      2
REMARK   3           1     H      2       H     244      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   4    F    (A):    972 ; 0.020 ; 0.050
REMARK   3   MEDIUM POSITIONAL  4    F    (A):    833 ; 0.020 ; 0.500
REMARK   3   TIGHT THERMAL      4    F (A**2):    972 ; 0.020 ; 0.500
REMARK   3   MEDIUM THERMAL     4    F (A**2):    833 ; 0.030 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 5
REMARK   3     CHAIN NAMES                    : I J
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     I      1       I      13      2
REMARK   3           1     J      1       J      13      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   5    I    (A):     52 ; 0.140 ; 0.050
REMARK   3   MEDIUM POSITIONAL  5    I    (A):     44 ; 0.320 ; 0.500
REMARK   3   TIGHT THERMAL      5    I (A**2):     52 ; 0.080 ; 0.500
REMARK   3   MEDIUM THERMAL     5    I (A**2):     44 ; 0.190 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 6
REMARK   3     CHAIN NAMES                    : C A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C    201       C     201      2
REMARK   3           1     A    201       A     202      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  6    C    (A):     14 ; 0.140 ; 0.500
REMARK   3   MEDIUM THERMAL     6    C (A**2):     14 ; 0.090 ; 2.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 14
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 :   E     3        E   113
REMARK   3    ORIGIN FOR THE GROUP (A): -73.3610  67.9750 -43.8610
REMARK   3    T TENSOR
REMARK   3      T11:   0.2132 T22:   0.1307
REMARK   3      T33:   0.1314 T12:  -0.0093
REMARK   3      T13:   0.0484 T23:  -0.0151
REMARK   3    L TENSOR
REMARK   3      L11:   6.4179 L22:   1.6710
REMARK   3      L33:   1.0184 L12:  -0.1773
REMARK   3      L13:   1.2032 L23:   0.1396
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0524 S12:  -0.1949 S13:  -0.1689
REMARK   3      S21:  -0.0641 S22:   0.0565 S23:   0.0866
REMARK   3      S31:   0.1088 S32:  -0.1312 S33:  -0.0041
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 :   E   114        E   201
REMARK   3    ORIGIN FOR THE GROUP (A):  -94.856   64.634  -59.594
REMARK   3    T TENSOR
REMARK   3      T11:   0.3616 T22:   0.5127
REMARK   3      T33:   0.3976 T12:  -0.0336
REMARK   3      T13:  -0.0064 T23:  -0.0225
REMARK   3    L TENSOR
REMARK   3      L11:   2.4578 L22:   3.4219
REMARK   3      L33:   6.9454 L12:   0.7427
REMARK   3      L13:   0.0320 L23:   2.6856
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0916 S12:   0.1003 S13:  -0.4071
REMARK   3      S21:   0.2871 S22:  -0.1290 S23:   0.4812
REMARK   3      S31:   0.7783 S32:  -0.9409 S33:   0.2206
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 :   F     2        F   117
REMARK   3    ORIGIN FOR THE GROUP (A): -61.4310  69.0350 -63.7780
REMARK   3    T TENSOR
REMARK   3      T11:   0.2382 T22:   0.3892
REMARK   3      T33:   0.1496 T12:   0.0036
REMARK   3      T13:   0.0239 T23:   0.0150
REMARK   3    L TENSOR
REMARK   3      L11:   3.4012 L22:   3.2626
REMARK   3      L33:   3.4309 L12:   1.4816
REMARK   3      L13:   3.3845 L23:   1.8092
REMARK   3    S TENSOR
REMARK   3      S11:   0.1609 S12:   0.4975 S13:  -0.1569
REMARK   3      S21:  -0.1188 S22:  -0.0100 S23:  -0.3015
REMARK   3      S31:   0.1188 S32:   0.4265 S33:  -0.1509
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 :   F   118        F   244
REMARK   3    ORIGIN FOR THE GROUP (A):  -88.891   70.644  -72.204
REMARK   3    T TENSOR
REMARK   3      T11:   0.2765 T22:   0.1942
REMARK   3      T33:   0.1556 T12:  -0.0056
REMARK   3      T13:  -0.0583 T23:  -0.0291
REMARK   3    L TENSOR
REMARK   3      L11:   3.1219 L22:   1.7964
REMARK   3      L33:   6.4725 L12:  -1.2522
REMARK   3      L13:  -2.7323 L23:   2.3785
REMARK   3    S TENSOR
REMARK   3      S11:   0.0165 S12:   0.3583 S13:  -0.0587
REMARK   3      S21:  -0.2701 S22:  -0.1785 S23:   0.2578
REMARK   3      S31:  -0.2712 S32:  -0.3788 S33:   0.1620
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 :   G     3        G   113
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4080  30.6060 -36.4230
REMARK   3    T TENSOR
REMARK   3      T11:   0.2311 T22:   0.2202
REMARK   3      T33:   0.3289 T12:  -0.0174
REMARK   3      T13:  -0.0534 T23:   0.0991
REMARK   3    L TENSOR
REMARK   3      L11:   5.0136 L22:   1.9588
REMARK   3      L33:   1.4431 L12:   0.4124
REMARK   3      L13:   0.6514 L23:  -0.5432
REMARK   3    S TENSOR
REMARK   3      S11:   0.0463 S12:  -0.4413 S13:   0.1577
REMARK   3      S21:   0.0301 S22:  -0.1402 S23:  -0.2772
REMARK   3      S31:  -0.0930 S32:   0.3516 S33:   0.0938
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 :   G   114        G   189
REMARK   3    ORIGIN FOR THE GROUP (A):   37.886   32.703  -50.120
REMARK   3    T TENSOR
REMARK   3      T11:   0.5619 T22:   0.7408
REMARK   3      T33:   0.7438 T12:  -0.0440
REMARK   3      T13:   0.0231 T23:   0.0426
REMARK   3    L TENSOR
REMARK   3      L11:   2.5188 L22:   1.6943
REMARK   3      L33:   2.4628 L12:   0.6196
REMARK   3      L13:   0.3620 L23:  -0.1618
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1573 S12:  -0.1793 S13:   0.4703
REMARK   3      S21:   0.2348 S22:   0.0183 S23:  -0.7944
REMARK   3      S31:  -0.5586 S32:   0.7666 S33:   0.1391
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 :   H     2        H   117
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6070  28.8400 -56.5520
REMARK   3    T TENSOR
REMARK   3      T11:   0.3098 T22:   0.2837
REMARK   3      T33:   0.2299 T12:  -0.0612
REMARK   3      T13:   0.0162 T23:   0.0552
REMARK   3    L TENSOR
REMARK   3      L11:   4.9584 L22:   2.0197
REMARK   3      L33:   4.0985 L12:   1.2534
REMARK   3      L13:  -3.5501 L23:  -1.2056
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0151 S12:   0.6602 S13:   0.1128
REMARK   3      S21:  -0.2746 S22:   0.0585 S23:  -0.0185
REMARK   3      S31:  -0.0624 S32:  -0.1423 S33:  -0.0433
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 :   H   118        H   244
REMARK   3    ORIGIN FOR THE GROUP (A):   33.080   27.647  -64.612
REMARK   3    T TENSOR
REMARK   3      T11:   0.4753 T22:   0.5202
REMARK   3      T33:   0.4221 T12:   0.1310
REMARK   3      T13:   0.1959 T23:   0.1772
REMARK   3    L TENSOR
REMARK   3      L11:   5.0128 L22:   2.3357
REMARK   3      L33:   3.8113 L12:  -1.1695
REMARK   3      L13:   1.3813 L23:  -1.6226
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0080 S12:   0.9690 S13:   0.0102
REMARK   3      S21:  -0.3565 S22:  -0.4844 S23:  -0.4567
REMARK   3      S31:   0.3447 S32:   0.6043 S33:   0.4924
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 4
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A    85
REMARK   3    RESIDUE RANGE :   B     3        B    92
REMARK   3    RESIDUE RANGE :   J     1        J    13
REMARK   3    RESIDUE RANGE :   A   201        A   201
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1650  23.9670 -31.9980
REMARK   3    T TENSOR
REMARK   3      T11:   0.1318 T22:   0.1322
REMARK   3      T33:   0.1167 T12:   0.0201
REMARK   3      T13:   0.0485 T23:   0.1010
REMARK   3    L TENSOR
REMARK   3      L11:   2.9699 L22:   3.5939
REMARK   3      L33:   2.0590 L12:   0.3834
REMARK   3      L13:   0.2138 L23:  -0.5793
REMARK   3    S TENSOR
REMARK   3      S11:   0.0696 S12:  -0.0428 S13:   0.2495
REMARK   3      S21:   0.1748 S22:  -0.0087 S23:  -0.0331
REMARK   3      S31:  -0.2191 S32:   0.0522 S33:  -0.0609
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    86        A   180
REMARK   3    RESIDUE RANGE :   A   202        A   202
REMARK   3    ORIGIN FOR THE GROUP (A): -38.5310  31.2280 -32.6900
REMARK   3    T TENSOR
REMARK   3      T11:   0.3916 T22:   0.3988
REMARK   3      T33:   0.4671 T12:   0.1454
REMARK   3      T13:   0.1455 T23:   0.2100
REMARK   3    L TENSOR
REMARK   3      L11:   2.6436 L22:   4.0255
REMARK   3      L33:   1.0462 L12:  -1.3456
REMARK   3      L13:  -0.6449 L23:   0.2981
REMARK   3    S TENSOR
REMARK   3      S11:   0.3751 S12:   0.0630 S13:   0.1920
REMARK   3      S21:  -0.2361 S22:  -0.0672 S23:   0.7926
REMARK   3      S31:  -0.5212 S32:  -0.5062 S33:  -0.3079
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 :   B    93        B   188
REMARK   3    ORIGIN FOR THE GROUP (A): -35.0560  38.1600 -10.2560
REMARK   3    T TENSOR
REMARK   3      T11:   0.7673 T22:   0.6571
REMARK   3      T33:   0.7236 T12:   0.1599
REMARK   3      T13:   0.3802 T23:  -0.2307
REMARK   3    L TENSOR
REMARK   3      L11:   0.5429 L22:   1.6607
REMARK   3      L33:   7.1176 L12:  -0.2553
REMARK   3      L13:  -1.4576 L23:   2.6746
REMARK   3    S TENSOR
REMARK   3      S11:   0.3701 S12:  -0.1427 S13:   0.4490
REMARK   3      S21:   0.2697 S22:   0.2358 S23:   0.1436
REMARK   3      S31:  -0.3903 S32:   0.0509 S33:  -0.6059
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     1        C    85
REMARK   3    RESIDUE RANGE :   D     2        D    92
REMARK   3    RESIDUE RANGE :   I     1        I    13
REMARK   3    ORIGIN FOR THE GROUP (A): -42.4220  74.2030 -39.6200
REMARK   3    T TENSOR
REMARK   3      T11:   0.1235 T22:   0.2202
REMARK   3      T33:   0.1901 T12:   0.0254
REMARK   3      T13:  -0.0318 T23:  -0.1003
REMARK   3    L TENSOR
REMARK   3      L11:   1.8936 L22:   2.9274
REMARK   3      L33:   0.6695 L12:   0.5540
REMARK   3      L13:   0.3379 L23:   0.0551
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0713 S12:  -0.0875 S13:   0.1612
REMARK   3      S21:   0.0777 S22:   0.1261 S23:   0.0544
REMARK   3      S31:  -0.0007 S32:   0.0028 S33:  -0.0548
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C    86        C   180
REMARK   3    RESIDUE RANGE :   C   201        C   201
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6680  67.3730 -41.0090
REMARK   3    T TENSOR
REMARK   3      T11:   0.2233 T22:   0.4729
REMARK   3      T33:   0.5103 T12:  -0.0132
REMARK   3      T13:  -0.0053 T23:  -0.1109
REMARK   3    L TENSOR
REMARK   3      L11:   0.5920 L22:   4.0517
REMARK   3      L33:   0.6673 L12:  -0.8543
REMARK   3      L13:  -0.3246 L23:  -0.7008
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0522 S12:  -0.1831 S13:   0.1256
REMARK   3      S21:  -0.2710 S22:  -0.2124 S23:  -0.9563
REMARK   3      S31:   0.1545 S32:   0.3108 S33:   0.2647
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D    93        D   189
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5760  59.3490 -17.6830
REMARK   3    T TENSOR
REMARK   3      T11:   0.4501 T22:   0.5676
REMARK   3      T33:   0.4385 T12:   0.0223
REMARK   3      T13:  -0.1976 T23:  -0.1907
REMARK   3    L TENSOR
REMARK   3      L11:   5.2840 L22:   0.5154
REMARK   3      L33:   4.1525 L12:  -0.6508
REMARK   3      L13:   4.0780 L23:  -0.8624
REMARK   3    S TENSOR
REMARK   3      S11:   0.4142 S12:  -0.2532 S13:  -0.1582
REMARK   3      S21:   0.2767 S22:  -0.1097 S23:  -0.2452
REMARK   3      S31:   0.1314 S32:   0.4940 S33:  -0.3045
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL
REMARK   4
REMARK   4 4GG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB074141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON
REMARK 200  BEAMLINE                       : MX1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95666
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32429
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : 0.17300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.1000
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) : 3.31
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.55400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
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 1KGC AND 2NNA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M MES PH 6.5,
REMARK 280  17% PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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       55.85400
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.15200
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.16250
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.15200
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.85400
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.16250
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
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H, J
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F, I
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLU A    -1
REMARK 465     ASP A   158
REMARK 465     GLU A   159
REMARK 465     GLU A   181
REMARK 465     SER A   182
REMARK 465     SER A   183
REMARK 465     ALA A   184
REMARK 465     ASP A   185
REMARK 465     LEU A   186
REMARK 465     VAL A   187
REMARK 465     PRO A   188
REMARK 465     ARG A   189
REMARK 465     GLY B   -14
REMARK 465     GLY B   -13
REMARK 465     GLY B   -12
REMARK 465     GLY B   -11
REMARK 465     SER B   -10
REMARK 465     ILE B    -9
REMARK 465     GLU B    -8
REMARK 465     GLY B    -7
REMARK 465     ARG B    -6
REMARK 465     GLY B    -5
REMARK 465     SER B    -4
REMARK 465     GLY B    -3
REMARK 465     GLY B    -2
REMARK 465     GLY B    -1
REMARK 465     SER B     0
REMARK 465     ARG B     1
REMARK 465     ASP B     2
REMARK 465     ARG B   105
REMARK 465     THR B   106
REMARK 465     GLU B   107
REMARK 465     ALA B   108
REMARK 465     LEU B   109
REMARK 465     ASN B   110
REMARK 465     HIS B   111
REMARK 465     HIS B   112
REMARK 465     ASN B   113
REMARK 465     ARG B   133
REMARK 465     ASN B   134
REMARK 465     ASP B   135
REMARK 465     GLN B   136
REMARK 465     GLU B   137
REMARK 465     MET B   163
REMARK 465     THR B   164
REMARK 465     PRO B   165
REMARK 465     GLN B   166
REMARK 465     ARG B   167
REMARK 465     GLY B   168
REMARK 465     ASP B   169
REMARK 465     VAL B   170
REMARK 465     TYR B   171
REMARK 465     ARG B   189
REMARK 465     ALA B   190
REMARK 465     GLN B   191
REMARK 465     SER B   192
REMARK 465     SER B   193
REMARK 465     SER B   194
REMARK 465     ALA B   195
REMARK 465     ASP B   196
REMARK 465     LEU B   197
REMARK 465     VAL B   198
REMARK 465     PRO B   199
REMARK 465     ARG B   200
REMARK 465     GLU C    -1
REMARK 465     ASP C   158
REMARK 465     GLU C   181
REMARK 465     SER C   182
REMARK 465     SER C   183
REMARK 465     ALA C   184
REMARK 465     ASP C   185
REMARK 465     LEU C   186
REMARK 465     VAL C   187
REMARK 465     PRO C   188
REMARK 465     ARG C   189
REMARK 465     GLY D   -14
REMARK 465     GLY D   -13
REMARK 465     GLY D   -12
REMARK 465     GLY D   -11
REMARK 465     SER D   -10
REMARK 465     ILE D    -9
REMARK 465     GLU D    -8
REMARK 465     GLY D    -7
REMARK 465     ARG D    -6
REMARK 465     GLY D    -5
REMARK 465     SER D    -4
REMARK 465     GLY D    -3
REMARK 465     GLY D    -2
REMARK 465     GLY D    -1
REMARK 465     SER D     0
REMARK 465     ARG D     1
REMARK 465     ARG D   105
REMARK 465     THR D   106
REMARK 465     GLU D   107
REMARK 465     ALA D   108
REMARK 465     LEU D   109
REMARK 465     ASN D   110
REMARK 465     HIS D   111
REMARK 465     HIS D   112
REMARK 465     ASN D   113
REMARK 465     ARG D   133
REMARK 465     ASN D   134
REMARK 465     ASP D   135
REMARK 465     THR D   164
REMARK 465     PRO D   165
REMARK 465     GLN D   166
REMARK 465     ALA D   190
REMARK 465     GLN D   191
REMARK 465     SER D   192
REMARK 465     SER D   193
REMARK 465     SER D   194
REMARK 465     ALA D   195
REMARK 465     ASP D   196
REMARK 465     LEU D   197
REMARK 465     VAL D   198
REMARK 465     PRO D   199
REMARK 465     ARG D   200
REMARK 465     MET E     0
REMARK 465     ASP E     1
REMARK 465     ALA E     2
REMARK 465     LYS E   144
REMARK 465     SER E   145
REMARK 465     SER E   146
REMARK 465     ASP E   147
REMARK 465     GLN E   164
REMARK 465     SER E   165
REMARK 465     LYS E   166
REMARK 465     ASN E   206
REMARK 465     ASN E   207
REMARK 465     SER E   208
REMARK 465     ILE E   209
REMARK 465     ILE E   210
REMARK 465     SER E   218
REMARK 465     PRO E   219
REMARK 465     GLU E   220
REMARK 465     SER E   221
REMARK 465     SER E   222
REMARK 465     ASP F     1
REMARK 465     ASP F   257
REMARK 465     MET G     0
REMARK 465     ASP G     1
REMARK 465     ALA G     2
REMARK 465     LYS G   144
REMARK 465     SER G   145
REMARK 465     SER G   146
REMARK 465     ASP G   147
REMARK 465     SER G   163
REMARK 465     GLN G   164
REMARK 465     SER G   165
REMARK 465     LYS G   166
REMARK 465     SER G   197
REMARK 465     ASP G   198
REMARK 465     ASN G   206
REMARK 465     ASN G   207
REMARK 465     SER G   208
REMARK 465     ILE G   209
REMARK 465     ILE G   210
REMARK 465     PRO G   211
REMARK 465     GLU G   212
REMARK 465     ASP G   213
REMARK 465     THR G   214
REMARK 465     PHE G   215
REMARK 465     PHE G   216
REMARK 465     PRO G   217
REMARK 465     SER G   218
REMARK 465     PRO G   219
REMARK 465     GLU G   220
REMARK 465     SER G   221
REMARK 465     SER G   222
REMARK 465     ASP H     1
REMARK 465     ASP H   257
REMARK 465     GLN I    -3
REMARK 465     GLN I    -2
REMARK 465     TYR I    -1
REMARK 465     PRO I     0
REMARK 465     GLN I    14
REMARK 465     GLN J    -3
REMARK 465     GLN J    -2
REMARK 465     TYR J    -1
REMARK 465     PRO J     0
REMARK 465     GLN J    14
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     ASP A   0    CG   OD1  OD2
REMARK 470     ILE A   1    CG1  CG2  CD1
REMARK 470     VAL A   2    CG1  CG2
REMARK 470     GLU A  40    CG   CD   OE1  OE2
REMARK 470     ARG A  49    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  53    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A  67    CG   CD   CE   NZ
REMARK 470     VAL A  97    CG1  CG2
REMARK 470     LEU A  99    CG   CD1  CD2
REMARK 470     GLN A 101    CG   CD   OE1  NE2
REMARK 470     SER A 123    OG
REMARK 470     HIS A 126    CG   ND1  CD2  CE1  NE2
REMARK 470     VAL A 128    CG1  CG2
REMARK 470     GLU A 130    CG   CD   OE1  OE2
REMARK 470     LEU A 154    CG   CD1  CD2
REMARK 470     SER A 156    OG
REMARK 470     ILE A 160    CG1  CG2  CD1
REMARK 470     GLU A 172    CG   CD   OE1  OE2
REMARK 470     LYS A 176    CG   CD   CE   NZ
REMARK 470     HIS A 177    CG   ND1  CD2  CE1  NE2
REMARK 470     GLU A 179    CG   CD   OE1  OE2
REMARK 470     ASN B  19    CG   OD1  ND2
REMARK 470     GLU B  22    CG   CD   OE1  OE2
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B  65    CG   CD   CE   NZ
REMARK 470     ARG B  88    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B  94    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B  96    CG   CD   OE1  OE2
REMARK 470     SER B 102    OG
REMARK 470     SER B 104    OG
REMARK 470     LEU B 114    CG   CD1  CD2
REMARK 470     LEU B 115    CG   CD1  CD2
REMARK 470     GLN B 126    CG   CD   OE1  NE2
REMARK 470     LYS B 128    CG   CD   CE   NZ
REMARK 470     PHE B 132    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU B 138    CG   CD   OE1  OE2
REMARK 470     THR B 139    OG1  CG2
REMARK 470     VAL B 143    CG1  CG2
REMARK 470     MET B 160    CG   SD   CE
REMARK 470     GLU B 162    CG   CD   OE1  OE2
REMARK 470     THR B 172    OG1  CG2
REMARK 470     HIS B 174    CG   ND1  CD2  CE1  NE2
REMARK 470     GLN B 181    CG   CD   OE1  NE2
REMARK 470     ASN B 182    CG   OD1  ND2
REMARK 470     ILE B 184    CG1  CG2  CD1
REMARK 470     ILE B 185    CG1  CG2  CD1
REMARK 470     GLU B 187    CG   CD   OE1  OE2
REMARK 470     ASP C   0    CG   OD1  OD2
REMARK 470     ILE C   1    CG1  CG2  CD1
REMARK 470     VAL C   2    CG1  CG2
REMARK 470     ARG C  49    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C  50    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG C  53    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS C  67    CG   CD   CE   NZ
REMARK 470     ASN C  78    CG   OD1  ND2
REMARK 470     LEU C  99    CG   CD1  CD2
REMARK 470     SER C 123    OG
REMARK 470     VAL C 128    CG1  CG2
REMARK 470     GLU C 130    CG   CD   OE1  OE2
REMARK 470     LEU C 154    CG   CD1  CD2
REMARK 470     SER C 156    OG
REMARK 470     GLU C 159    CG   CD   OE1  OE2
REMARK 470     ILE C 160    CG1  CG2  CD1
REMARK 470     LYS C 164    CG   CD   CE   NZ
REMARK 470     GLU C 172    CG   CD   OE1  OE2
REMARK 470     LYS C 176    CG   CD   CE   NZ
REMARK 470     ASP D   2    CG   OD1  OD2
REMARK 470     ASN D  19    CG   OD1  ND2
REMARK 470     GLU D  22    CG   CD   OE1  OE2
REMARK 470     ARG D  23    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D  59    CG   CD   OE1  OE2
REMARK 470     LYS D  65    CG   CD   CE   NZ
REMARK 470     ARG D  88    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D  94    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D  96    CG   CD   OE1  OE2
REMARK 470     SER D 102    OG
REMARK 470     SER D 104    OG
REMARK 470     LEU D 114    CG   CD1  CD2
REMARK 470     LEU D 115    CG   CD1  CD2
REMARK 470     GLN D 126    CG   CD   OE1  NE2
REMARK 470     LYS D 128    CG   CD   CE   NZ
REMARK 470     ARG D 130    CG   CD   NE   CZ   NH1  NH2
REMARK 470     PHE D 132    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLN D 136    CG   CD   OE1  NE2
REMARK 470     GLU D 137    CG   CD   OE1  OE2
REMARK 470     GLU D 138    CG   CD   OE1  OE2
REMARK 470     VAL D 143    CG1  CG2
REMARK 470     GLU D 162    CG   CD   OE1  OE2
REMARK 470     ARG D 167    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 176    CG   CD   OE1  OE2
REMARK 470     GLN D 181    CG   CD   OE1  NE2
REMARK 470     ARG D 189    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS E   3    CG   CD   CE   NZ
REMARK 470     SER E  13    OG
REMARK 470     SER E  47    OG
REMARK 470     SER E  64    OG
REMARK 470     ARG E  74    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU E  82    CG   CD   OE1  OE2
REMARK 470     ASP E 114    CG   OD1  OD2
REMARK 470     LYS E 120    CG   CD   CE   NZ
REMARK 470     GLN E 127    CG   CD   OE1  NE2
REMARK 470     ARG E 141    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS E 148    CG   CD   CE   NZ
REMARK 470     GLN E 159    CG   CD   OE1  NE2
REMARK 470     ASN E 161    CG   OD1  ND2
REMARK 470     SER E 168    OG
REMARK 470     LYS E 175    CG   CD   CE   NZ
REMARK 470     ASN E 188    CG   OD1  ND2
REMARK 470     LYS E 196    CG   CD   CE   NZ
REMARK 470     SER E 197    OG
REMARK 470     ASP E 198    CG   OD1  OD2
REMARK 470     ASN E 203    CG   OD1  ND2
REMARK 470     PHE E 205    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU E 212    CG   CD   OE1  OE2
REMARK 470     ASP E 213    CG   OD1  OD2
REMARK 470     SER F   2    OG
REMARK 470     LYS F   9    CG   CD   CE   NZ
REMARK 470     ARG F  18    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG F  22    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER F  24    OG
REMARK 470     LEU F  46    CG   CD1  CD2
REMARK 470     ASP F  47    CG   OD1  OD2
REMARK 470     GLU F  64    CG   CD   OE1  OE2
REMARK 470     LYS F  68    CG   CD   CE   NZ
REMARK 470     GLN F  79    CG   CD   OE1  NE2
REMARK 470     GLU F  88    CG   CD   OE1  OE2
REMARK 470     SER F  92    OG
REMARK 470     GLU F 128    CG   CD   OE1  OE2
REMARK 470     ASP F 129    CG   OD1  OD2
REMARK 470     LYS F 131    CG   CD   CE   NZ
REMARK 470     GLU F 145    CG   CD   OE1  OE2
REMARK 470     GLU F 147    CG   CD   OE1  OE2
REMARK 470     SER F 149    OG
REMARK 470     LYS F 177    CG   CD   CE   NZ
REMARK 470     GLN F 188    CG   CD   OE1  NE2
REMARK 470     ASN F 197    CG   OD1  ND2
REMARK 470     THR F 212    OG1  CG2
REMARK 470     GLN F 215    CG   CD   OE1  NE2
REMARK 470     ARG F 218    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER F 231    OG
REMARK 470     GLU F 232    CG   CD   OE1  OE2
REMARK 470     ASN F 233    CG   OD1  ND2
REMARK 470     GLU F 235    CG   CD   OE1  OE2
REMARK 470     ARG F 255    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS G   3    CG   CD   CE   NZ
REMARK 470     GLU G  12    CG   CD   OE1  OE2
REMARK 470     SER G  47    OG
REMARK 470     SER G  64    OG
REMARK 470     ARG G  74    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP G 114    CG   OD1  OD2
REMARK 470     LYS G 120    CG   CD   CE   NZ
REMARK 470     GLN G 127    CG   CD   OE1  NE2
REMARK 470     ILE G 130    CG1  CG2  CD1
REMARK 470     GLN G 139    CG   CD   OE1  NE2
REMARK 470     ARG G 141    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS G 148    CG   CD   CE   NZ
REMARK 470     GLN G 159    CG   CD   OE1  NE2
REMARK 470     THR G 160    OG1  CG2
REMARK 470     ASN G 161    CG   OD1  ND2
REMARK 470     VAL G 162    CG1  CG2
REMARK 470     ASP G 167    CG   OD1  OD2
REMARK 470     SER G 168    OG
REMARK 470     VAL G 170    CG1  CG2
REMARK 470     LYS G 175    CG   CD   CE   NZ
REMARK 470     ARG G 181    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS G 196    CG   CD   CE   NZ
REMARK 470     PHE G 199    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ASN G 203    CG   OD1  ND2
REMARK 470     PHE G 205    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     SER H   2    OG
REMARK 470     LYS H   9    CG   CD   CE   NZ
REMARK 470     ARG H  18    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG H  22    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU H  46    CG   CD1  CD2
REMARK 470     ASP H  47    CG   OD1  OD2
REMARK 470     GLU H  64    CG   CD   OE1  OE2
REMARK 470     LYS H  68    CG   CD   CE   NZ
REMARK 470     GLU H  74    CG   CD   OE1  OE2
REMARK 470     GLU H  88    CG   CD   OE1  OE2
REMARK 470     SER H  92    OG
REMARK 470     ASP H 129    CG   OD1  OD2
REMARK 470     LEU H 130    CG   CD1  CD2
REMARK 470     LYS H 131    CG   CD   CE   NZ
REMARK 470     GLU H 145    CG   CD   OE1  OE2
REMARK 470     GLU H 147    CG   CD   OE1  OE2
REMARK 470     SER H 149    OG
REMARK 470     GLN H 152    CG   CD   OE1  NE2
REMARK 470     LYS H 177    CG   CD   CE   NZ
REMARK 470     GLN H 188    CG   CD   OE1  NE2
REMARK 470     GLN H 193    CG   CD   OE1  NE2
REMARK 470     ASN H 197    CG   OD1  ND2
REMARK 470     GLN H 215    CG   CD   OE1  NE2
REMARK 470     ARG H 218    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER H 231    OG
REMARK 470     GLU H 232    CG   CD   OE1  OE2
REMARK 470     ASN H 233    CG   OD1  ND2
REMARK 470     GLU H 235    CG   CD   OE1  OE2
REMARK 470     GLN H 238    CG   CD   OE1  NE2
REMARK 470     ASP H 239    CG   OD1  OD2
REMARK 470     ARG H 255    CG   CD   NE   CZ   NH1  NH2
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    ASN A 124     -115.56     68.34
REMARK 500    ASN B  33      -96.18     55.28
REMARK 500    PRO B  52       -2.03    -59.54
REMARK 500    VAL B  78      -58.93   -121.64
REMARK 500    CYS B  79      -73.32    -65.62
REMARK 500    THR B  89      -92.50   -102.75
REMARK 500    ASP B 121       92.03     59.43
REMARK 500    PRO B 124     -159.08    -83.94
REMARK 500    PRO B 178      -29.63    -36.81
REMARK 500    GLN B 181      -77.83    -64.39
REMARK 500    PRO C 115       70.31    -69.84
REMARK 500    ASN C 124     -115.55     66.97
REMARK 500    PRO D   4      120.76    -29.56
REMARK 500    ASN D  33     -103.89     53.50
REMARK 500    PRO D  52        1.46    -64.92
REMARK 500    VAL D  78      -71.86   -117.14
REMARK 500    CYS D  79      -73.76    -52.71
REMARK 500    THR D  89      -80.64   -108.15
REMARK 500    ASP D 121       74.92     58.99
REMARK 500    ASP D 152       44.97   -101.99
REMARK 500    GLU E  16      -21.74     75.54
REMARK 500    HIS E  25       77.34   -164.23
REMARK 500    THR E  27       30.80    -98.51
REMARK 500    SER E  64     -132.12     46.19
REMARK 500    ALA E 100     -177.47   -171.88
REMARK 500    ALA E 113      -71.68    -48.04
REMARK 500    ASP E 114       93.73    -57.89
REMARK 500    GLN E 159       37.86    -74.35
REMARK 500    LYS E 186       30.50    -93.40
REMARK 500    GLU E 212      -85.92   -120.86
REMARK 500    LEU F  53      -71.57   -100.21
REMARK 500    ASN F  70       44.94   -103.79
REMARK 500    LEU F  85       -6.19     82.62
REMARK 500    GLN F 152       27.02     48.23
REMARK 500    ASP F 166       28.51    -77.73
REMARK 500    GLU G  16      -23.37     75.08
REMARK 500    HIS G  25       75.03   -165.88
REMARK 500    SER G  64     -131.23     46.00
REMARK 500    ALA G 113      -70.73    -47.16
REMARK 500    ASP G 114       92.68    -60.10
REMARK 500    GLN G 159       38.72    -76.48
REMARK 500    LEU H  53      -72.40   -101.90
REMARK 500    ASN H  70       44.86   -104.58
REMARK 500    LEU H  85       -5.54     83.50
REMARK 500    GLN H 152       26.07     48.94
REMARK 500    ASP H 166       30.11    -77.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 201
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1. SEQUENCE CONFLICTS OF ENTITY 1 AND 2 ARE ALL NATURAL VARIANTS
REMARK 999 ACCORDING TO DATABASE UNIPROT P01909 (ENTITY 1) AND P01920 (ENTITY
REMARK 999 2) RESPECTIVELY. 2. RESIDUES NUMBERING FOR CHAIN A,C,E,G,F AND H
REMARK 999 HAVE BEEN CHANGED TO CONFORM WITH THE NUMBERING CONVENTION IN THE
REMARK 999 IMGT DATABASE. 3. THE SEQUENCE DATABASE FOR ENTITY 3 AND 4
REMARK 999 CURRENTLY DO NOT EXIST. ACCORDING TO AUTHOR, RESIDUE 176 (T176C) IN
REMARK 999 ENTITY 3 AND RESIDUES 184 (S184C) AND 202 (C202A) IN ENTITY 4 ARE
REMARK 999 ENGINEERED MUTATIONS.
DBREF  4GG6 A   -1   181  UNP    P01909   DQA1_HUMAN      24    206
DBREF  4GG6 B    1   192  UNP    P01920   DQB1_HUMAN      33    224
DBREF  4GG6 C   -1   181  UNP    P01909   DQA1_HUMAN      24    206
DBREF  4GG6 D    1   192  UNP    P01920   DQB1_HUMAN      33    224
DBREF  4GG6 E    0   222  PDB    4GG6     4GG6             0    222
DBREF  4GG6 F    1   257  PDB    4GG6     4GG6             1    257
DBREF  4GG6 G    0   222  PDB    4GG6     4GG6             0    222
DBREF  4GG6 H    1   257  PDB    4GG6     4GG6             1    257
DBREF  4GG6 I   -3    14  UNP    P18573   GDA9_WHEAT     243    260
DBREF  4GG6 J   -3    14  UNP    P18573   GDA9_WHEAT     243    260
SEQADV 4GG6 SER A   23  UNP  P01909    THR    49 SEE REMARK 999
SEQADV 4GG6 GLU A   31  UNP  P01909    GLN    57 SEE REMARK 999
SEQADV 4GG6 GLU A   37  UNP  P01909    GLY    63 SEE REMARK 999
SEQADV 4GG6 GLN A   44  UNP  P01909    CYS    70 SEE REMARK 999
SEQADV 4GG6 LEU A   47  UNP  P01909    VAL    73 SEE REMARK 999
SEQADV 4GG6 PHE A   48  UNP  P01909    LEU    74 SEE REMARK 999
SEQADV 4GG6 ARG A   50  UNP  P01909    GLN    76 SEE REMARK 999
SEQADV 4GG6 ARG A   52  UNP  P01909              SEE REMARK 999
SEQADV 4GG6 ILE A   72  UNP  P01909    SER    97 SEE REMARK 999
SEQADV 4GG6 VAL A   73  UNP  P01909    LEU    98 SEE REMARK 999
SEQADV 4GG6 THR A  104  UNP  P01909    ILE   129 SEE REMARK 999
SEQADV 4GG6 PHE A  153  UNP  P01909    LEU   178 SEE REMARK 999
SEQADV 4GG6 ASP A  158  UNP  P01909    GLU   183 SEE REMARK 999
SEQADV 4GG6 ILE A  160  UNP  P01909    SER   185 SEE REMARK 999
SEQADV 4GG6 GLU A  172  UNP  P01909    LYS   197 SEE REMARK 999
SEQADV 4GG6 SER A  182  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 SER A  183  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 ALA A  184  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 ASP A  185  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 LEU A  186  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 VAL A  187  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 PRO A  188  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 ARG A  189  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 GLY B  -14  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B  -13  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B  -12  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B  -11  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER B  -10  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ILE B   -9  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLU B   -8  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B   -7  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ARG B   -6  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B   -5  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER B   -4  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B   -3  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B   -2  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B   -1  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER B    0  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY B   13  UNP  P01920    ALA    45 SEE REMARK 999
SEQADV 4GG6 LEU B   26  UNP  P01920    TYR    58 SEE REMARK 999
SEQADV 4GG6 GLY B   45  UNP  P01920    GLU    77 SEE REMARK 999
SEQADV 4GG6 ALA B   57  UNP  P01920    ASP    89 SEE REMARK 999
SEQADV 4GG6 ARG B  167  UNP  P01920    HIS   199 SEE REMARK 999
SEQADV 4GG6 ILE B  185  UNP  P01920    THR   217 SEE REMARK 999
SEQADV 4GG6 SER B  193  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER B  194  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ALA B  195  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ASP B  196  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 LEU B  197  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 VAL B  198  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 PRO B  199  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ARG B  200  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER C   23  UNP  P01909    THR    49 SEE REMARK 999
SEQADV 4GG6 GLU C   31  UNP  P01909    GLN    57 SEE REMARK 999
SEQADV 4GG6 GLU C   37  UNP  P01909    GLY    63 SEE REMARK 999
SEQADV 4GG6 GLN C   44  UNP  P01909    CYS    70 SEE REMARK 999
SEQADV 4GG6 LEU C   47  UNP  P01909    VAL    73 SEE REMARK 999
SEQADV 4GG6 PHE C   48  UNP  P01909    LEU    74 SEE REMARK 999
SEQADV 4GG6 ARG C   50  UNP  P01909    GLN    76 SEE REMARK 999
SEQADV 4GG6 ARG C   52  UNP  P01909              SEE REMARK 999
SEQADV 4GG6 ILE C   72  UNP  P01909    SER    97 SEE REMARK 999
SEQADV 4GG6 VAL C   73  UNP  P01909    LEU    98 SEE REMARK 999
SEQADV 4GG6 THR C  104  UNP  P01909    ILE   129 SEE REMARK 999
SEQADV 4GG6 PHE C  153  UNP  P01909    LEU   178 SEE REMARK 999
SEQADV 4GG6 ASP C  158  UNP  P01909    GLU   183 SEE REMARK 999
SEQADV 4GG6 ILE C  160  UNP  P01909    SER   185 SEE REMARK 999
SEQADV 4GG6 GLU C  172  UNP  P01909    LYS   197 SEE REMARK 999
SEQADV 4GG6 SER C  182  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 SER C  183  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 ALA C  184  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 ASP C  185  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 LEU C  186  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 VAL C  187  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 PRO C  188  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 ARG C  189  UNP  P01909              EXPRESSION TAG
SEQADV 4GG6 GLY D  -14  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D  -13  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D  -12  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D  -11  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER D  -10  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ILE D   -9  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLU D   -8  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D   -7  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ARG D   -6  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D   -5  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER D   -4  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D   -3  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D   -2  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D   -1  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER D    0  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLY D   13  UNP  P01920    ALA    45 SEE REMARK 999
SEQADV 4GG6 LEU D   26  UNP  P01920    TYR    58 SEE REMARK 999
SEQADV 4GG6 GLY D   45  UNP  P01920    GLU    77 SEE REMARK 999
SEQADV 4GG6 ALA D   57  UNP  P01920    ASP    89 SEE REMARK 999
SEQADV 4GG6 ARG D  167  UNP  P01920    HIS   199 SEE REMARK 999
SEQADV 4GG6 ILE D  185  UNP  P01920    THR   217 SEE REMARK 999
SEQADV 4GG6 SER D  193  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 SER D  194  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ALA D  195  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ASP D  196  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 LEU D  197  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 VAL D  198  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 PRO D  199  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 ARG D  200  UNP  P01920              EXPRESSION TAG
SEQADV 4GG6 GLU I    3  UNP  P18573    GLN   249 ENGINEERED MUTATION
SEQADV 4GG6 GLU I   11  UNP  P18573    GLN   257 ENGINEERED MUTATION
SEQADV 4GG6 GLU J    3  UNP  P18573    GLN   249 ENGINEERED MUTATION
SEQADV 4GG6 GLU J   11  UNP  P18573    GLN   257 ENGINEERED MUTATION
SEQRES   1 A  192  GLU ASP ILE VAL ALA ASP HIS VAL ALA SER TYR GLY VAL
SEQRES   2 A  192  ASN LEU TYR GLN SER TYR GLY PRO SER GLY GLN TYR SER
SEQRES   3 A  192  HIS GLU PHE ASP GLY ASP GLU GLU PHE TYR VAL ASP LEU
SEQRES   4 A  192  GLU ARG LYS GLU THR VAL TRP GLN LEU PRO LEU PHE ARG
SEQRES   5 A  192  ARG PHE ARG ARG PHE ASP PRO GLN PHE ALA LEU THR ASN
SEQRES   6 A  192  ILE ALA VAL LEU LYS HIS ASN LEU ASN ILE VAL ILE LYS
SEQRES   7 A  192  ARG SER ASN SER THR ALA ALA THR ASN GLU VAL PRO GLU
SEQRES   8 A  192  VAL THR VAL PHE SER LYS SER PRO VAL THR LEU GLY GLN
SEQRES   9 A  192  PRO ASN THR LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO
SEQRES  10 A  192  PRO VAL VAL ASN ILE THR TRP LEU SER ASN GLY HIS SER
SEQRES  11 A  192  VAL THR GLU GLY VAL SER GLU THR SER PHE LEU SER LYS
SEQRES  12 A  192  SER ASP HIS SER PHE PHE LYS ILE SER TYR LEU THR PHE
SEQRES  13 A  192  LEU PRO SER ALA ASP GLU ILE TYR ASP CYS LYS VAL GLU
SEQRES  14 A  192  HIS TRP GLY LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU
SEQRES  15 A  192  PRO GLU SER SER ALA ASP LEU VAL PRO ARG
SEQRES   1 B  215  GLY GLY GLY GLY SER ILE GLU GLY ARG GLY SER GLY GLY
SEQRES   2 B  215  GLY SER ARG ASP SER PRO GLU ASP PHE VAL TYR GLN PHE
SEQRES   3 B  215  LYS GLY MET CYS TYR PHE THR ASN GLY THR GLU ARG VAL
SEQRES   4 B  215  ARG LEU VAL THR ARG TYR ILE TYR ASN ARG GLU GLU TYR
SEQRES   5 B  215  ALA ARG PHE ASP SER ASP VAL GLY VAL TYR ARG ALA VAL
SEQRES   6 B  215  THR PRO LEU GLY PRO PRO ALA ALA GLU TYR TRP ASN SER
SEQRES   7 B  215  GLN LYS GLU VAL LEU GLU ARG THR ARG ALA GLU LEU ASP
SEQRES   8 B  215  THR VAL CYS ARG HIS ASN TYR GLN LEU GLU LEU ARG THR
SEQRES   9 B  215  THR LEU GLN ARG ARG VAL GLU PRO THR VAL THR ILE SER
SEQRES  10 B  215  PRO SER ARG THR GLU ALA LEU ASN HIS HIS ASN LEU LEU
SEQRES  11 B  215  VAL CYS SER VAL THR ASP PHE TYR PRO ALA GLN ILE LYS
SEQRES  12 B  215  VAL ARG TRP PHE ARG ASN ASP GLN GLU GLU THR THR GLY
SEQRES  13 B  215  VAL VAL SER THR PRO LEU ILE ARG ASN GLY ASP TRP THR
SEQRES  14 B  215  PHE GLN ILE LEU VAL MET LEU GLU MET THR PRO GLN ARG
SEQRES  15 B  215  GLY ASP VAL TYR THR CYS HIS VAL GLU HIS PRO SER LEU
SEQRES  16 B  215  GLN ASN PRO ILE ILE VAL GLU TRP ARG ALA GLN SER SER
SEQRES  17 B  215  SER ALA ASP LEU VAL PRO ARG
SEQRES   1 C  192  GLU ASP ILE VAL ALA ASP HIS VAL ALA SER TYR GLY VAL
SEQRES   2 C  192  ASN LEU TYR GLN SER TYR GLY PRO SER GLY GLN TYR SER
SEQRES   3 C  192  HIS GLU PHE ASP GLY ASP GLU GLU PHE TYR VAL ASP LEU
SEQRES   4 C  192  GLU ARG LYS GLU THR VAL TRP GLN LEU PRO LEU PHE ARG
SEQRES   5 C  192  ARG PHE ARG ARG PHE ASP PRO GLN PHE ALA LEU THR ASN
SEQRES   6 C  192  ILE ALA VAL LEU LYS HIS ASN LEU ASN ILE VAL ILE LYS
SEQRES   7 C  192  ARG SER ASN SER THR ALA ALA THR ASN GLU VAL PRO GLU
SEQRES   8 C  192  VAL THR VAL PHE SER LYS SER PRO VAL THR LEU GLY GLN
SEQRES   9 C  192  PRO ASN THR LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO
SEQRES  10 C  192  PRO VAL VAL ASN ILE THR TRP LEU SER ASN GLY HIS SER
SEQRES  11 C  192  VAL THR GLU GLY VAL SER GLU THR SER PHE LEU SER LYS
SEQRES  12 C  192  SER ASP HIS SER PHE PHE LYS ILE SER TYR LEU THR PHE
SEQRES  13 C  192  LEU PRO SER ALA ASP GLU ILE TYR ASP CYS LYS VAL GLU
SEQRES  14 C  192  HIS TRP GLY LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU
SEQRES  15 C  192  PRO GLU SER SER ALA ASP LEU VAL PRO ARG
SEQRES   1 D  215  GLY GLY GLY GLY SER ILE GLU GLY ARG GLY SER GLY GLY
SEQRES   2 D  215  GLY SER ARG ASP SER PRO GLU ASP PHE VAL TYR GLN PHE
SEQRES   3 D  215  LYS GLY MET CYS TYR PHE THR ASN GLY THR GLU ARG VAL
SEQRES   4 D  215  ARG LEU VAL THR ARG TYR ILE TYR ASN ARG GLU GLU TYR
SEQRES   5 D  215  ALA ARG PHE ASP SER ASP VAL GLY VAL TYR ARG ALA VAL
SEQRES   6 D  215  THR PRO LEU GLY PRO PRO ALA ALA GLU TYR TRP ASN SER
SEQRES   7 D  215  GLN LYS GLU VAL LEU GLU ARG THR ARG ALA GLU LEU ASP
SEQRES   8 D  215  THR VAL CYS ARG HIS ASN TYR GLN LEU GLU LEU ARG THR
SEQRES   9 D  215  THR LEU GLN ARG ARG VAL GLU PRO THR VAL THR ILE SER
SEQRES  10 D  215  PRO SER ARG THR GLU ALA LEU ASN HIS HIS ASN LEU LEU
SEQRES  11 D  215  VAL CYS SER VAL THR ASP PHE TYR PRO ALA GLN ILE LYS
SEQRES  12 D  215  VAL ARG TRP PHE ARG ASN ASP GLN GLU GLU THR THR GLY
SEQRES  13 D  215  VAL VAL SER THR PRO LEU ILE ARG ASN GLY ASP TRP THR
SEQRES  14 D  215  PHE GLN ILE LEU VAL MET LEU GLU MET THR PRO GLN ARG
SEQRES  15 D  215  GLY ASP VAL TYR THR CYS HIS VAL GLU HIS PRO SER LEU
SEQRES  16 D  215  GLN ASN PRO ILE ILE VAL GLU TRP ARG ALA GLN SER SER
SEQRES  17 D  215  SER ALA ASP LEU VAL PRO ARG
SEQRES   1 E  207  MET ASP ALA LYS THR THR GLN PRO ASN SER MET GLU SER
SEQRES   2 E  207  ASN GLU GLU GLU PRO VAL HIS LEU PRO CYS ASN HIS SER
SEQRES   3 E  207  THR ILE SER GLY THR ASP TYR ILE HIS TRP TYR ARG GLN
SEQRES   4 E  207  LEU PRO SER GLN GLY PRO GLU TYR VAL ILE HIS GLY LEU
SEQRES   5 E  207  THR SER ASN VAL ASN ASN ARG MET ALA SER LEU ALA ILE
SEQRES   6 E  207  ALA GLU ASP ARG LYS SER SER THR LEU ILE LEU HIS ARG
SEQRES   7 E  207  ALA THR LEU ARG ASP ALA ALA VAL TYR TYR CYS ILE LEU
SEQRES   8 E  207  ARG ASP GLY ARG GLY GLY ALA ASP GLY LEU THR PHE GLY
SEQRES   9 E  207  LYS GLY THR HIS LEU ILE ILE GLN PRO TYR ILE GLN ASN
SEQRES  10 E  207  PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER
SEQRES  11 E  207  SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER
SEQRES  12 E  207  GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR
SEQRES  13 E  207  ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER MET ASP
SEQRES  14 E  207  PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS SER
SEQRES  15 E  207  ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE
SEQRES  16 E  207  PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES   1 F  245  ASP SER GLY VAL THR GLN THR PRO LYS HIS LEU ILE THR
SEQRES   2 F  245  ALA THR GLY GLN ARG VAL THR LEU ARG CYS SER PRO ARG
SEQRES   3 F  245  SER GLY ASP LEU SER VAL TYR TRP TYR GLN GLN SER LEU
SEQRES   4 F  245  ASP GLN GLY LEU GLN PHE LEU ILE GLN TYR TYR ASN GLY
SEQRES   5 F  245  GLU GLU ARG ALA LYS GLY ASN ILE LEU GLU ARG PHE SER
SEQRES   6 F  245  ALA GLN GLN PHE PRO ASP LEU HIS SER GLU LEU ASN LEU
SEQRES   7 F  245  SER SER LEU GLU LEU GLY ASP SER ALA LEU TYR PHE CYS
SEQRES   8 F  245  ALA SER SER VAL ALA VAL SER ALA GLY THR TYR GLU GLN
SEQRES   9 F  245  TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU ASP
SEQRES  10 F  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES  11 F  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES  12 F  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES  13 F  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES  14 F  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES  15 F  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES  16 F  245  ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES  17 F  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES  18 F  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES  19 F  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES   1 G  207  MET ASP ALA LYS THR THR GLN PRO ASN SER MET GLU SER
SEQRES   2 G  207  ASN GLU GLU GLU PRO VAL HIS LEU PRO CYS ASN HIS SER
SEQRES   3 G  207  THR ILE SER GLY THR ASP TYR ILE HIS TRP TYR ARG GLN
SEQRES   4 G  207  LEU PRO SER GLN GLY PRO GLU TYR VAL ILE HIS GLY LEU
SEQRES   5 G  207  THR SER ASN VAL ASN ASN ARG MET ALA SER LEU ALA ILE
SEQRES   6 G  207  ALA GLU ASP ARG LYS SER SER THR LEU ILE LEU HIS ARG
SEQRES   7 G  207  ALA THR LEU ARG ASP ALA ALA VAL TYR TYR CYS ILE LEU
SEQRES   8 G  207  ARG ASP GLY ARG GLY GLY ALA ASP GLY LEU THR PHE GLY
SEQRES   9 G  207  LYS GLY THR HIS LEU ILE ILE GLN PRO TYR ILE GLN ASN
SEQRES  10 G  207  PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER
SEQRES  11 G  207  SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER
SEQRES  12 G  207  GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR
SEQRES  13 G  207  ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER MET ASP
SEQRES  14 G  207  PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS SER
SEQRES  15 G  207  ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE
SEQRES  16 G  207  PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES   1 H  245  ASP SER GLY VAL THR GLN THR PRO LYS HIS LEU ILE THR
SEQRES   2 H  245  ALA THR GLY GLN ARG VAL THR LEU ARG CYS SER PRO ARG
SEQRES   3 H  245  SER GLY ASP LEU SER VAL TYR TRP TYR GLN GLN SER LEU
SEQRES   4 H  245  ASP GLN GLY LEU GLN PHE LEU ILE GLN TYR TYR ASN GLY
SEQRES   5 H  245  GLU GLU ARG ALA LYS GLY ASN ILE LEU GLU ARG PHE SER
SEQRES   6 H  245  ALA GLN GLN PHE PRO ASP LEU HIS SER GLU LEU ASN LEU
SEQRES   7 H  245  SER SER LEU GLU LEU GLY ASP SER ALA LEU TYR PHE CYS
SEQRES   8 H  245  ALA SER SER VAL ALA VAL SER ALA GLY THR TYR GLU GLN
SEQRES   9 H  245  TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU ASP
SEQRES  10 H  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES  11 H  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES  12 H  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES  13 H  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES  14 H  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES  15 H  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES  16 H  245  ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES  17 H  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES  18 H  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES  19 H  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES   1 I   18  GLN GLN TYR PRO SER GLY GLU GLY SER PHE GLN PRO SER
SEQRES   2 I   18  GLN GLU ASN PRO GLN
SEQRES   1 J   18  GLN GLN TYR PRO SER GLY GLU GLY SER PHE GLN PRO SER
SEQRES   2 J   18  GLN GLU ASN PRO GLN
MODRES 4GG6 ASN C  118  ASN  GLYCOSYLATION SITE
MODRES 4GG6 ASN A  118  ASN  GLYCOSYLATION SITE
MODRES 4GG6 ASN A   78  ASN  GLYCOSYLATION SITE
HET    NAG  A 201      14
HET    NAG  A 202      14
HET    NAG  C 201      14
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL  11  NAG    3(C8 H15 N O6)
HELIX    1   1 LEU A   45  ARG A   52  1                                   8
HELIX    2   2 ASP A   55  SER A   77  1                                  23
HELIX    3   3 GLY B   54  SER B   63  1                                  10
HELIX    4   4 GLN B   64  VAL B   78  1                                  15
HELIX    5   5 VAL B   78  THR B   89  1                                  12
HELIX    6   6 THR B   90  ARG B   93  5                                   4
HELIX    7   7 LEU C   45  ARG C   52  1                                   8
HELIX    8   8 ASP C   55  SER C   77  1                                  23
HELIX    9   9 GLY D   54  SER D   63  1                                  10
HELIX   10  10 GLN D   64  VAL D   78  1                                  15
HELIX   11  11 VAL D   78  THR D   89  1                                  12
HELIX   12  12 THR D   90  ARG D   93  5                                   4
HELIX   13  13 THR E   95  ALA E   99  5                                   5
HELIX   14  14 GLU F   95  SER F   99  5                                   5
HELIX   15  15 ASP F  129  VAL F  133  5                                   5
HELIX   16  16 SER F  144  GLN F  152  1                                   9
HELIX   17  17 ALA F  211  GLN F  215  1                                   5
HELIX   18  18 THR G   95  ALA G   99  5                                   5
HELIX   19  19 GLU H   95  SER H   99  5                                   5
HELIX   20  20 ASP H  129  VAL H  133  5                                   5
HELIX   21  21 SER H  144  GLN H  152  1                                   9
HELIX   22  22 ALA H  211  GLN H  215  1                                   5
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  TYR A  33   O  VAL A  42
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  HIS A  24   O  GLU A  31
SHEET    4   A 8 HIS A   5  GLN A  14 -1  N  GLN A  14   O  SER A  19
SHEET    5   A 8 VAL B   8  THR B  18 -1  O  PHE B  11   N  ASN A  11
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  VAL B  27   N  MET B  14
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   B 4 GLU A  88  SER A  93  0
SHEET    2   B 4 ASN A 103  ILE A 112 -1  O  ILE A 106   N  PHE A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  SER A 149   N  CYS A 107
SHEET    4   B 4 VAL A 132  GLU A 134 -1  N  SER A 133   O  TYR A 150
SHEET    1   C 4 GLU A  88  SER A  93  0
SHEET    2   C 4 ASN A 103  ILE A 112 -1  O  ILE A 106   N  PHE A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  SER A 149   N  CYS A 107
SHEET    4   C 4 LEU A 138  SER A 139 -1  N  LEU A 138   O  PHE A 146
SHEET    1   D 4 HIS A 126  SER A 127  0
SHEET    2   D 4 ASN A 118  SER A 123 -1  N  SER A 123   O  HIS A 126
SHEET    3   D 4 TYR A 161  GLU A 166 -1  O  LYS A 164   N  THR A 120
SHEET    4   D 4 LEU A 174  TRP A 178 -1  O  LEU A 174   N  VAL A 165
SHEET    1   E 4 THR B  98  SER B 102  0
SHEET    2   E 4 VAL B 116  THR B 120 -1  O  THR B 120   N  THR B  98
SHEET    3   E 4 PHE B 155  LEU B 161 -1  O  ILE B 157   N  VAL B 119
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   F 4 THR B  98  SER B 102  0
SHEET    2   F 4 VAL B 116  THR B 120 -1  O  THR B 120   N  THR B  98
SHEET    3   F 4 PHE B 155  LEU B 161 -1  O  ILE B 157   N  VAL B 119
SHEET    4   F 4 ILE B 148  ARG B 149 -1  N  ILE B 148   O  GLN B 156
SHEET    1   G 3 LYS B 128  TRP B 131  0
SHEET    2   G 3 CYS B 173  GLU B 176 -1  O  GLU B 176   N  LYS B 128
SHEET    3   G 3 ILE B 184  VAL B 186 -1  O  VAL B 186   N  CYS B 173
SHEET    1   H 8 GLU C  40  TRP C  43  0
SHEET    2   H 8 ASP C  29  ASP C  35 -1  N  TYR C  33   O  VAL C  42
SHEET    3   H 8 SER C  19  PHE C  26 -1  N  HIS C  24   O  GLU C  31
SHEET    4   H 8 HIS C   5  GLN C  14 -1  N  GLN C  14   O  SER C  19
SHEET    5   H 8 VAL D   8  THR D  18 -1  O  PHE D  11   N  ASN C  11
SHEET    6   H 8 ARG D  23  TYR D  32 -1  O  VAL D  27   N  MET D  14
SHEET    7   H 8 GLU D  35  ASP D  41 -1  O  GLU D  35   N  TYR D  32
SHEET    8   H 8 TYR D  47  ALA D  49 -1  O  ARG D  48   N  ARG D  39
SHEET    1   I 4 GLU C  88  SER C  93  0
SHEET    2   I 4 ASN C 103  ILE C 112 -1  O  ILE C 106   N  PHE C  92
SHEET    3   I 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105
SHEET    4   I 4 VAL C 132  GLU C 134 -1  N  SER C 133   O  TYR C 150
SHEET    1   J 4 GLU C  88  SER C  93  0
SHEET    2   J 4 ASN C 103  ILE C 112 -1  O  ILE C 106   N  PHE C  92
SHEET    3   J 4 PHE C 145  PHE C 153 -1  O  LEU C 151   N  LEU C 105
SHEET    4   J 4 LEU C 138  SER C 139 -1  N  LEU C 138   O  PHE C 146
SHEET    1   K 4 HIS C 126  SER C 127  0
SHEET    2   K 4 ASN C 118  SER C 123 -1  N  SER C 123   O  HIS C 126
SHEET    3   K 4 TYR C 161  GLU C 166 -1  O  LYS C 164   N  THR C 120
SHEET    4   K 4 LEU C 174  TRP C 178 -1  O  LEU C 174   N  VAL C 165
SHEET    1   L 4 THR D  98  SER D 102  0
SHEET    2   L 4 LEU D 115  PHE D 122 -1  O  VAL D 116   N  SER D 102
SHEET    3   L 4 PHE D 155  LEU D 161 -1  O  ILE D 157   N  VAL D 119
SHEET    4   L 4 VAL D 142  SER D 144 -1  N  VAL D 143   O  MET D 160
SHEET    1   M 4 THR D  98  SER D 102  0
SHEET    2   M 4 LEU D 115  PHE D 122 -1  O  VAL D 116   N  SER D 102
SHEET    3   M 4 PHE D 155  LEU D 161 -1  O  ILE D 157   N  VAL D 119
SHEET    4   M 4 ILE D 148  ARG D 149 -1  N  ILE D 148   O  GLN D 156
SHEET    1   N 3 LYS D 128  PHE D 132  0
SHEET    2   N 3 TYR D 171  GLU D 176 -1  O  HIS D 174   N  ARG D 130
SHEET    3   N 3 ILE D 184  TRP D 188 -1  O  TRP D 188   N  TYR D 171
SHEET    1   O 5 SER E  10  ASN E  14  0
SHEET    2   O 5 THR E 122  GLN E 127  1  O  ILE E 125   N  MET E  11
SHEET    3   O 5 ALA E 100  ASP E 108 -1  N  TYR E 102   O  THR E 122
SHEET    4   O 5 ASP E  37  GLN E  44 -1  N  TYR E  38   O  ARG E 107
SHEET    5   O 5 PRO E  50  GLY E  56 -1  O  GLY E  56   N  ILE E  39
SHEET    1   P 4 VAL E  19  ASN E  24  0
SHEET    2   P 4 SER E  86  LEU E  91 -1  O  LEU E  89   N  LEU E  21
SHEET    3   P 4 SER E  77  ILE E  80 -1  N  SER E  77   O  ILE E  90
SHEET    4   P 4 ASN E  65  ASN E  67 -1  N  VAL E  66   O  LEU E  78
SHEET    1   Q 9 TYR E 171  ILE E 172  0
SHEET    2   Q 9 SER E 189  TRP E 193 -1  O  TRP E 193   N  TYR E 171
SHEET    3   Q 9 SER E 149  THR E 154 -1  N  PHE E 153   O  ALA E 190
SHEET    4   Q 9 ALA E 136  ASP E 142 -1  N  LEU E 140   O  VAL E 150
SHEET    5   Q 9 GLU F 137  GLU F 142 -1  O  GLU F 142   N  ARG E 141
SHEET    6   Q 9 LYS F 153  PHE F 163 -1  O  VAL F 157   N  PHE F 141
SHEET    7   Q 9 TYR F 201  SER F 210 -1  O  LEU F 203   N  ALA F 160
SHEET    8   Q 9 VAL F 183  THR F 185 -1  N  CYS F 184   O  ARG F 206
SHEET    9   Q 9 VAL E 177  LEU E 178 -1  N  VAL E 177   O  THR F 185
SHEET    1   R 8 TYR E 171  ILE E 172  0
SHEET    2   R 8 SER E 189  TRP E 193 -1  O  TRP E 193   N  TYR E 171
SHEET    3   R 8 SER E 149  THR E 154 -1  N  PHE E 153   O  ALA E 190
SHEET    4   R 8 ALA E 136  ASP E 142 -1  N  LEU E 140   O  VAL E 150
SHEET    5   R 8 GLU F 137  GLU F 142 -1  O  GLU F 142   N  ARG E 141
SHEET    6   R 8 LYS F 153  PHE F 163 -1  O  VAL F 157   N  PHE F 141
SHEET    7   R 8 TYR F 201  SER F 210 -1  O  LEU F 203   N  ALA F 160
SHEET    8   R 8 LEU F 190  LYS F 191 -1  N  LEU F 190   O  ALA F 202
SHEET    1   S 4 THR F   5  THR F   7  0
SHEET    2   S 4 VAL F  19  SER F  24 -1  O  ARG F  22   N  THR F   7
SHEET    3   S 4 SER F  87  LEU F  91 -1  O  LEU F  89   N  LEU F  21
SHEET    4   S 4 PHE F  76  GLN F  80 -1  N  SER F  77   O  ASN F  90
SHEET    1   T 6 HIS F  10  ALA F  14  0
SHEET    2   T 6 THR F 122  THR F 127  1  O  ARG F 123   N  LEU F  11
SHEET    3   T 6 ALA F 100  SER F 107 -1  N  TYR F 102   O  THR F 122
SHEET    4   T 6 SER F  38  SER F  45 -1  N  GLN F  44   O  LEU F 101
SHEET    5   T 6 GLY F  49  TYR F  57 -1  O  LEU F  53   N  TRP F  41
SHEET    6   T 6 GLU F  64  LYS F  68 -1  O  ARG F  66   N  GLN F  55
SHEET    1   U 4 HIS F  10  ALA F  14  0
SHEET    2   U 4 THR F 122  THR F 127  1  O  ARG F 123   N  LEU F  11
SHEET    3   U 4 ALA F 100  SER F 107 -1  N  TYR F 102   O  THR F 122
SHEET    4   U 4 TYR F 117  PHE F 118 -1  O  TYR F 117   N  SER F 106
SHEET    1   V 4 LYS F 177  VAL F 179  0
SHEET    2   V 4 VAL F 168  VAL F 174 -1  N  TRP F 172   O  VAL F 179
SHEET    3   V 4 HIS F 220  PHE F 227 -1  O  GLN F 226   N  GLU F 169
SHEET    4   V 4 GLN F 246  TRP F 253 -1  O  ALA F 250   N  CYS F 223
SHEET    1   W 5 SER G  10  ASN G  14  0
SHEET    2   W 5 THR G 122  GLN G 127  1  O  ILE G 125   N  MET G  11
SHEET    3   W 5 ALA G 100  ASP G 108 -1  N  TYR G 102   O  THR G 122
SHEET    4   W 5 ASP G  37  GLN G  44 -1  N  TYR G  38   O  ARG G 107
SHEET    5   W 5 PRO G  50  GLY G  56 -1  O  GLY G  56   N  ILE G  39
SHEET    1   X 4 VAL G  19  ASN G  24  0
SHEET    2   X 4 SER G  86  LEU G  91 -1  O  LEU G  89   N  LEU G  21
SHEET    3   X 4 SER G  77  ILE G  80 -1  N  SER G  77   O  ILE G  90
SHEET    4   X 4 ASN G  65  ASN G  67 -1  N  VAL G  66   O  LEU G  78
SHEET    1   Y 9 TYR G 171  ILE G 172  0
SHEET    2   Y 9 SER G 189  TRP G 193 -1  O  TRP G 193   N  TYR G 171
SHEET    3   Y 9 SER G 149  THR G 154 -1  N  PHE G 153   O  ALA G 190
SHEET    4   Y 9 ALA G 136  ASP G 142 -1  N  LEU G 140   O  VAL G 150
SHEET    5   Y 9 GLU H 137  GLU H 142 -1  O  GLU H 142   N  ARG G 141
SHEET    6   Y 9 LYS H 153  PHE H 163 -1  O  VAL H 157   N  PHE H 141
SHEET    7   Y 9 TYR H 201  SER H 210 -1  O  LEU H 203   N  ALA H 160
SHEET    8   Y 9 VAL H 183  THR H 185 -1  N  CYS H 184   O  ARG H 206
SHEET    9   Y 9 VAL G 177  LEU G 178 -1  N  VAL G 177   O  THR H 185
SHEET    1   Z 8 TYR G 171  ILE G 172  0
SHEET    2   Z 8 SER G 189  TRP G 193 -1  O  TRP G 193   N  TYR G 171
SHEET    3   Z 8 SER G 149  THR G 154 -1  N  PHE G 153   O  ALA G 190
SHEET    4   Z 8 ALA G 136  ASP G 142 -1  N  LEU G 140   O  VAL G 150
SHEET    5   Z 8 GLU H 137  GLU H 142 -1  O  GLU H 142   N  ARG G 141
SHEET    6   Z 8 LYS H 153  PHE H 163 -1  O  VAL H 157   N  PHE H 141
SHEET    7   Z 8 TYR H 201  SER H 210 -1  O  LEU H 203   N  ALA H 160
SHEET    8   Z 8 LEU H 190  LYS H 191 -1  N  LEU H 190   O  ALA H 202
SHEET    1  AA 4 THR H   5  THR H   7  0
SHEET    2  AA 4 VAL H  19  SER H  24 -1  O  ARG H  22   N  THR H   7
SHEET    3  AA 4 SER H  87  LEU H  91 -1  O  LEU H  89   N  LEU H  21
SHEET    4  AA 4 PHE H  76  GLN H  80 -1  N  SER H  77   O  ASN H  90
SHEET    1  AB 6 HIS H  10  ALA H  14  0
SHEET    2  AB 6 THR H 122  THR H 127  1  O  ARG H 123   N  LEU H  11
SHEET    3  AB 6 ALA H 100  SER H 107 -1  N  TYR H 102   O  THR H 122
SHEET    4  AB 6 SER H  38  SER H  45 -1  N  GLN H  44   O  LEU H 101
SHEET    5  AB 6 GLY H  49  TYR H  57 -1  O  LEU H  53   N  TRP H  41
SHEET    6  AB 6 GLU H  64  LYS H  68 -1  O  ARG H  66   N  GLN H  55
SHEET    1  AC 4 HIS H  10  ALA H  14  0
SHEET    2  AC 4 THR H 122  THR H 127  1  O  ARG H 123   N  LEU H  11
SHEET    3  AC 4 ALA H 100  SER H 107 -1  N  TYR H 102   O  THR H 122
SHEET    4  AC 4 TYR H 117  PHE H 118 -1  O  TYR H 117   N  SER H 106
SHEET    1  AD 4 LYS H 177  VAL H 179  0
SHEET    2  AD 4 VAL H 168  VAL H 174 -1  N  TRP H 172   O  VAL H 179
SHEET    3  AD 4 HIS H 220  PHE H 227 -1  O  GLN H 226   N  GLU H 169
SHEET    4  AD 4 GLN H 246  TRP H 253 -1  O  ALA H 250   N  CYS H 223
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.04
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.04
SSBOND   4 CYS C  107    CYS C  163                          1555   1555  2.03
SSBOND   5 CYS D   15    CYS D   79                          1555   1555  2.05
SSBOND   6 CYS D  117    CYS D  173                          1555   1555  2.04
SSBOND   7 CYS E   23    CYS E  104                          1555   1555  2.04
SSBOND   8 CYS E  151    CYS E  201                          1555   1555  2.04
SSBOND   9 CYS E  176    CYS F  184                          1555   1555  2.02
SSBOND  10 CYS F   23    CYS F  104                          1555   1555  2.04
SSBOND  11 CYS F  158    CYS F  223                          1555   1555  2.04
SSBOND  12 CYS G   23    CYS G  104                          1555   1555  2.04
SSBOND  13 CYS G  151    CYS G  201                          1555   1555  2.04
SSBOND  14 CYS G  176    CYS H  184                          1555   1555  2.01
SSBOND  15 CYS H   23    CYS H  104                          1555   1555  2.04
SSBOND  16 CYS H  158    CYS H  223                          1555   1555  2.03
LINK         ND2 ASN C 118                 C1  NAG C 201     1555   1555  1.45
LINK         ND2 ASN A 118                 C1  NAG A 202     1555   1555  1.45
LINK         ND2 ASN A  78                 C1  NAG A 201     1555   1555  1.46
CISPEP   1 GLY A   17    PRO A   18          0        -1.18
CISPEP   2 PHE A  113    PRO A  114          0        -0.79
CISPEP   3 TYR B  123    PRO B  124          0         2.90
CISPEP   4 GLY C   17    PRO C   18          0         0.33
CISPEP   5 PHE C  113    PRO C  114          0        -1.78
CISPEP   6 TYR D  123    PRO D  124          0        -1.27
CISPEP   7 THR F    7    PRO F    8          0        -6.67
CISPEP   8 TYR F  164    PRO F  165          0        -1.59
CISPEP   9 THR H    7    PRO H    8          0        -7.09
CISPEP  10 TYR H  164    PRO H  165          0        -2.77
SITE     1 AC1  2 ARG A  76  ASN A  78
SITE     1 AC2  2 ASN A 118  GLU A 166
SITE     1 AC3  2 ASN C 118  TRP C 168
CRYST1  111.708  134.325  140.304  90.00  90.00  90.00 P 21 21 21    8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.008952  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007445  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007127        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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