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PDBsum entry 3alq

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Cytokine/cytokine receptor PDB id
3alq
Jmol
Contents
Protein chains
(+ 0 more) 141 a.a.
(+ 0 more) 162 a.a.
Metals
_CO ×6
Waters ×11
HEADER    CYTOKINE/CYTOKINE RECEPTOR              06-AUG-10   3ALQ
TITLE     CRYSTAL STRUCTURE OF TNF-TNFR2 COMPLEX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 FRAGMENT: SOLUBLE FORM;
COMPND   5 SYNONYM: TNF-ALPHA, TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER
COMPND   6 2, TNF-A, CACHECTIN;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 1B;
COMPND  11 CHAIN: R, S, T, U, V, W;
COMPND  12 FRAGMENT: RESIDUES IN UNP 33-205;
COMPND  13 SYNONYM: TUMOR NECROSIS FACTOR RECEPTOR 2, TNF-R2, TUMOR NECROSIS
COMPND  14 FACTOR-BINDING PROTEIN 2, TBPII, TBP-2;
COMPND  15 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: TNF, TNFA, TNFSF2;
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: PYAS (MODIFIED FROM PUC18);
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 GENE: TNFBR, TNFR2, TNFRSF1B;
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PYAS (MODIFIED FROM PUC18)
KEYWDS    LIGAND-RECEPTOR COMPLEX, CYTOKINE, CYTOKINE-CYTOKINE RECEPTOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.MUKAI,T.NAKAMURA,Y.YAMAGATA,Y.TSUTSUMI
REVDAT   2   01-DEC-10 3ALQ    1       JRNL
REVDAT   1   17-NOV-10 3ALQ    0
JRNL        AUTH   Y.MUKAI,T.NAKAMURA,M.YOSHIKAWA,Y.YOSHIOKA,S.I.TSUNODA,
JRNL        AUTH 2 S.NAKAGAWA,Y.YAMAGATA,Y.TSUTSUMI
JRNL        TITL   SOLUTION OF THE STRUCTURE OF THE TNF-TNFR2 COMPLEX
JRNL        REF    SCI.SIGNAL.                   V.   3  RA83 2010
JRNL        REFN                   ESSN 1937-9145
JRNL        PMID   21081755
JRNL        DOI    10.1126/SCISIGNAL.2000954
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.96
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.320
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 43981
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220
REMARK   3   R VALUE            (WORKING SET) : 0.213
REMARK   3   FREE R VALUE                     : 0.281
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.090
REMARK   3   FREE R VALUE TEST SET COUNT      : 4438
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 49.9668 -  9.3025    1.00     1470   151  0.2383 0.2933
REMARK   3     2  9.3025 -  7.3914    1.00     1385   147  0.2169 0.2917
REMARK   3     3  7.3914 -  6.4593    1.00     1395   143  0.2253 0.2912
REMARK   3     4  6.4593 -  5.8697    1.00     1331   157  0.2271 0.2525
REMARK   3     5  5.8697 -  5.4496    1.00     1325   175  0.2119 0.3237
REMARK   3     6  5.4496 -  5.1286    1.00     1320   164  0.1981 0.2590
REMARK   3     7  5.1286 -  4.8720    1.00     1340   149  0.1853 0.2588
REMARK   3     8  4.8720 -  4.6601    1.00     1308   151  0.1593 0.2270
REMARK   3     9  4.6601 -  4.4808    1.00     1317   171  0.1556 0.2362
REMARK   3    10  4.4808 -  4.3263    1.00     1339   133  0.1655 0.2029
REMARK   3    11  4.3263 -  4.1910    1.00     1323   153  0.1757 0.2323
REMARK   3    12  4.1910 -  4.0713    1.00     1345   136  0.1761 0.2482
REMARK   3    13  4.0713 -  3.9642    1.00     1286   154  0.1825 0.2646
REMARK   3    14  3.9642 -  3.8675    1.00     1331   146  0.1885 0.2557
REMARK   3    15  3.8675 -  3.7796    1.00     1327   146  0.1879 0.2423
REMARK   3    16  3.7796 -  3.6992    1.00     1326   129  0.1958 0.2693
REMARK   3    17  3.6992 -  3.6252    1.00     1344   138  0.2112 0.2569
REMARK   3    18  3.6252 -  3.5568    1.00     1273   135  0.1988 0.2967
REMARK   3    19  3.5568 -  3.4933    1.00     1339   153  0.2111 0.3033
REMARK   3    20  3.4933 -  3.4341    1.00     1313   160  0.2240 0.2848
REMARK   3    21  3.4341 -  3.3787    1.00     1283   126  0.2271 0.2919
REMARK   3    22  3.3787 -  3.3268    1.00     1326   161  0.2304 0.3257
REMARK   3    23  3.3268 -  3.2778    1.00     1282   146  0.2374 0.3297
REMARK   3    24  3.2778 -  3.2317    1.00     1293   141  0.2341 0.3298
REMARK   3    25  3.2317 -  3.1880    1.00     1341   143  0.2523 0.2998
REMARK   3    26  3.1880 -  3.1466    1.00     1298   132  0.2606 0.3306
REMARK   3    27  3.1466 -  3.1073    0.99     1260   154  0.2632 0.3675
REMARK   3    28  3.1073 -  3.0699    0.98     1294   171  0.2648 0.3465
REMARK   3    29  3.0699 -  3.0342    0.95     1237   146  0.2884 0.3550
REMARK   3    30  3.0342 -  3.0001    0.92     1192   127  0.2752 0.3272
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.33
REMARK   3   B_SOL              : 25.48
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.490
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 23.58240
REMARK   3    B22 (A**2) : -9.51320
REMARK   3    B33 (A**2) : -14.06920
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.004          14288
REMARK   3   ANGLE     :  0.759          19505
REMARK   3   CHIRALITY :  0.050           2169
REMARK   3   PLANARITY :  0.003           2562
REMARK   3   DIHEDRAL  : 15.078           5135
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3ALQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB029405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-06
REMARK 200  TEMPERATURE           (KELVIN) : 95
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL41XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45945
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.18300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.60300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.510
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 2E7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
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       37.23500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      123.41750
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.67800
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      123.41750
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.23500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.67800
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, S, T, R
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E, V, W, U
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     VAL A     1
REMARK 465     ARG A     2
REMARK 465     SER A     3
REMARK 465     SER A     4
REMARK 465     SER A     5
REMARK 465     ARG A     6
REMARK 465     THR A     7
REMARK 465     PRO A     8
REMARK 465     ARG A   103
REMARK 465     GLU A   104
REMARK 465     THR A   105
REMARK 465     PRO A   106
REMARK 465     GLU A   107
REMARK 465     GLY A   108
REMARK 465     ALA A   109
REMARK 465     GLU A   110
REMARK 465     VAL B     1
REMARK 465     ARG B     2
REMARK 465     SER B     3
REMARK 465     SER B     4
REMARK 465     SER B     5
REMARK 465     ARG B     6
REMARK 465     THR B     7
REMARK 465     PRO B     8
REMARK 465     ARG B   103
REMARK 465     GLU B   104
REMARK 465     THR B   105
REMARK 465     PRO B   106
REMARK 465     GLU B   107
REMARK 465     GLY B   108
REMARK 465     ALA B   109
REMARK 465     GLU B   110
REMARK 465     VAL C     1
REMARK 465     ARG C     2
REMARK 465     SER C     3
REMARK 465     SER C     4
REMARK 465     SER C     5
REMARK 465     ARG C     6
REMARK 465     THR C     7
REMARK 465     PRO C     8
REMARK 465     ARG C   103
REMARK 465     GLU C   104
REMARK 465     THR C   105
REMARK 465     PRO C   106
REMARK 465     GLU C   107
REMARK 465     GLY C   108
REMARK 465     ALA C   109
REMARK 465     GLU C   110
REMARK 465     VAL D     1
REMARK 465     ARG D     2
REMARK 465     SER D     3
REMARK 465     SER D     4
REMARK 465     SER D     5
REMARK 465     ARG D     6
REMARK 465     THR D     7
REMARK 465     PRO D     8
REMARK 465     ARG D   103
REMARK 465     GLU D   104
REMARK 465     THR D   105
REMARK 465     PRO D   106
REMARK 465     GLU D   107
REMARK 465     GLY D   108
REMARK 465     ALA D   109
REMARK 465     GLU D   110
REMARK 465     VAL E     1
REMARK 465     ARG E     2
REMARK 465     SER E     3
REMARK 465     SER E     4
REMARK 465     SER E     5
REMARK 465     ARG E     6
REMARK 465     THR E     7
REMARK 465     PRO E     8
REMARK 465     ARG E   103
REMARK 465     GLU E   104
REMARK 465     THR E   105
REMARK 465     PRO E   106
REMARK 465     GLU E   107
REMARK 465     GLY E   108
REMARK 465     ALA E   109
REMARK 465     GLU E   110
REMARK 465     VAL F     1
REMARK 465     ARG F     2
REMARK 465     SER F     3
REMARK 465     SER F     4
REMARK 465     SER F     5
REMARK 465     ARG F     6
REMARK 465     THR F     7
REMARK 465     PRO F     8
REMARK 465     ARG F   103
REMARK 465     GLU F   104
REMARK 465     THR F   105
REMARK 465     PRO F   106
REMARK 465     GLU F   107
REMARK 465     GLY F   108
REMARK 465     ALA F   109
REMARK 465     GLU F   110
REMARK 465     ALA R    11
REMARK 465     PRO R    12
REMARK 465     GLU R    13
REMARK 465     PRO R    14
REMARK 465     GLY R    15
REMARK 465     SER R    16
REMARK 465     THR R   179
REMARK 465     SER R   180
REMARK 465     THR R   181
REMARK 465     SER R   182
REMARK 465     PRO R   183
REMARK 465     ALA S    11
REMARK 465     PRO S    12
REMARK 465     GLU S    13
REMARK 465     PRO S    14
REMARK 465     THR S   179
REMARK 465     SER S   180
REMARK 465     THR S   181
REMARK 465     SER S   182
REMARK 465     PRO S   183
REMARK 465     ALA T    11
REMARK 465     PRO T    12
REMARK 465     GLU T    13
REMARK 465     PRO T    14
REMARK 465     GLY T    15
REMARK 465     SER T    16
REMARK 465     THR T   179
REMARK 465     SER T   180
REMARK 465     THR T   181
REMARK 465     SER T   182
REMARK 465     PRO T   183
REMARK 465     ALA U    11
REMARK 465     PRO U    12
REMARK 465     GLU U    13
REMARK 465     PRO U    14
REMARK 465     GLY U    15
REMARK 465     SER U    16
REMARK 465     THR U    17
REMARK 465     THR U   179
REMARK 465     SER U   180
REMARK 465     THR U   181
REMARK 465     SER U   182
REMARK 465     PRO U   183
REMARK 465     ALA V    11
REMARK 465     PRO V    12
REMARK 465     GLU V    13
REMARK 465     PRO V    14
REMARK 465     GLY V    15
REMARK 465     SER V    16
REMARK 465     THR V    17
REMARK 465     THR V   179
REMARK 465     SER V   180
REMARK 465     THR V   181
REMARK 465     SER V   182
REMARK 465     PRO V   183
REMARK 465     ALA W    11
REMARK 465     PRO W    12
REMARK 465     GLU W    13
REMARK 465     PRO W    14
REMARK 465     GLY W    15
REMARK 465     SER W    16
REMARK 465     THR W   179
REMARK 465     SER W   180
REMARK 465     THR W   181
REMARK 465     SER W   182
REMARK 465     PRO W   183
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    TYR A  87       80.67   -168.33
REMARK 500    ALA B  22       49.46   -106.13
REMARK 500    TYR B  87       82.07   -165.55
REMARK 500    ALA C  22       59.72    -64.92
REMARK 500    ARG C  31       47.97    -72.69
REMARK 500    ASP C  45       48.19     39.91
REMARK 500    SER C  60      136.96   -173.20
REMARK 500    PRO C  70      -99.91    -68.01
REMARK 500    HIS C  73       77.44   -158.60
REMARK 500    TYR C  87       85.36   -174.06
REMARK 500    LEU D  37       88.53   -170.24
REMARK 500    PRO D  51      -70.53    -70.91
REMARK 500    PRO D  70      169.75    -46.87
REMARK 500    SER D  71       -6.18    -59.21
REMARK 500    ALA D 145      -73.60    -35.62
REMARK 500    LEU E  37       98.91   -173.01
REMARK 500    SER E  60      145.71   -172.06
REMARK 500    TYR E  87       93.78   -166.51
REMARK 500    ASN F  30      -25.64   -142.73
REMARK 500    ARG F  31       49.70    -75.58
REMARK 500    LEU F  37       96.99   -174.97
REMARK 500    PRO F  70      -80.07    -59.68
REMARK 500    ARG F 138       77.24   -117.33
REMARK 500    GLN R  29       60.01     62.55
REMARK 500    MET R  30      168.24    179.71
REMARK 500    GLU R  57     -155.70    -91.45
REMARK 500    TRP R  67       48.00   -147.58
REMARK 500    THR R  89     -164.66   -119.38
REMARK 500    ARG R 122     -178.54    -66.01
REMARK 500    VAL R 127       98.46    -68.59
REMARK 500    ALA R 128      -73.70    -57.52
REMARK 500    PRO R 130     -153.46    -82.84
REMARK 500    THR R 132       20.41    -68.09
REMARK 500    GLU R 133      -86.00    -94.97
REMARK 500    THR R 134       33.15   -140.59
REMARK 500    SER R 148      106.85   -167.28
REMARK 500    ASN R 149       36.52    -88.67
REMARK 500    THR R 154      -54.52   -123.75
REMARK 500    CYS R 157       92.61    -65.30
REMARK 500    ALA R 167      -85.02    -87.71
REMARK 500    PRO R 169     -175.52    -55.46
REMARK 500    ARG S  19      161.22    -46.61
REMARK 500    THR S  48      -62.67    -97.82
REMARK 500    GLU S  57     -131.02    -99.68
REMARK 500    TRP S  67       48.69   -143.81
REMARK 500    GLN S  86      117.69   -165.35
REMARK 500    THR S  89     -167.34   -117.76
REMARK 500    ARG S 122     -179.39    -62.93
REMARK 500    PRO S 130      176.37    -55.72
REMARK 500    ASP S 136     -175.47    -66.24
REMARK 500
REMARK 500 THIS ENTRY HAS      89 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO R   2  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R  54   OD1
REMARK 620 2 HIS R  40   NE2  78.9
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO S   1  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S  40   NE2
REMARK 620 2 ASP S  54   OD1 105.0
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO U   4  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS U  40   NE2
REMARK 620 2 ASP U  54   OD1 108.1
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO T   3  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP T  54   OD1
REMARK 620 2 HIS T  40   NE2  92.3
REMARK 620 3 GLU T  57   OE2  61.6 131.2
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO V   5  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V  40   NE2
REMARK 620 2 ASP V  54   OD1 109.1
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CO W   6  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP W  54   OD1
REMARK 620 2 HIS W  40   NE2  86.7
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO R 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO S 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO T 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO U 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO V 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO W 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TNR   RELATED DB: PDB
REMARK 900 RELATED ID: 1TNF   RELATED DB: PDB
REMARK 900 RELATED ID: 2E7A   RELATED DB: PDB
REMARK 900 RELATED ID: 2ZJC   RELATED DB: PDB
REMARK 900 RELATED ID: 2ZPX   RELATED DB: PDB
DBREF  3ALQ A    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  3ALQ B    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  3ALQ C    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  3ALQ D    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  3ALQ E    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  3ALQ F    1   157  UNP    P01375   TNFA_HUMAN      77    233
DBREF  3ALQ R   11   183  UNP    P20333   TNR1B_HUMAN     33    205
DBREF  3ALQ S   11   183  UNP    P20333   TNR1B_HUMAN     33    205
DBREF  3ALQ T   11   183  UNP    P20333   TNR1B_HUMAN     33    205
DBREF  3ALQ U   11   183  UNP    P20333   TNR1B_HUMAN     33    205
DBREF  3ALQ V   11   183  UNP    P20333   TNR1B_HUMAN     33    205
DBREF  3ALQ W   11   183  UNP    P20333   TNR1B_HUMAN     33    205
SEQADV 3ALQ MET A   11  UNP  P01375    LYS    87 ENGINEERED MUTATION
SEQADV 3ALQ SER A   65  UNP  P01375    LYS   141 ENGINEERED MUTATION
SEQADV 3ALQ PRO A   90  UNP  P01375    LYS   166 ENGINEERED MUTATION
SEQADV 3ALQ ARG A   98  UNP  P01375    LYS   174 ENGINEERED MUTATION
SEQADV 3ALQ ASN A  112  UNP  P01375    LYS   188 ENGINEERED MUTATION
SEQADV 3ALQ PRO A  128  UNP  P01375    LYS   204 ENGINEERED MUTATION
SEQADV 3ALQ MET B   11  UNP  P01375    LYS    87 ENGINEERED MUTATION
SEQADV 3ALQ SER B   65  UNP  P01375    LYS   141 ENGINEERED MUTATION
SEQADV 3ALQ PRO B   90  UNP  P01375    LYS   166 ENGINEERED MUTATION
SEQADV 3ALQ ARG B   98  UNP  P01375    LYS   174 ENGINEERED MUTATION
SEQADV 3ALQ ASN B  112  UNP  P01375    LYS   188 ENGINEERED MUTATION
SEQADV 3ALQ PRO B  128  UNP  P01375    LYS   204 ENGINEERED MUTATION
SEQADV 3ALQ MET C   11  UNP  P01375    LYS    87 ENGINEERED MUTATION
SEQADV 3ALQ SER C   65  UNP  P01375    LYS   141 ENGINEERED MUTATION
SEQADV 3ALQ PRO C   90  UNP  P01375    LYS   166 ENGINEERED MUTATION
SEQADV 3ALQ ARG C   98  UNP  P01375    LYS   174 ENGINEERED MUTATION
SEQADV 3ALQ ASN C  112  UNP  P01375    LYS   188 ENGINEERED MUTATION
SEQADV 3ALQ PRO C  128  UNP  P01375    LYS   204 ENGINEERED MUTATION
SEQADV 3ALQ MET D   11  UNP  P01375    LYS    87 ENGINEERED MUTATION
SEQADV 3ALQ SER D   65  UNP  P01375    LYS   141 ENGINEERED MUTATION
SEQADV 3ALQ PRO D   90  UNP  P01375    LYS   166 ENGINEERED MUTATION
SEQADV 3ALQ ARG D   98  UNP  P01375    LYS   174 ENGINEERED MUTATION
SEQADV 3ALQ ASN D  112  UNP  P01375    LYS   188 ENGINEERED MUTATION
SEQADV 3ALQ PRO D  128  UNP  P01375    LYS   204 ENGINEERED MUTATION
SEQADV 3ALQ MET E   11  UNP  P01375    LYS    87 ENGINEERED MUTATION
SEQADV 3ALQ SER E   65  UNP  P01375    LYS   141 ENGINEERED MUTATION
SEQADV 3ALQ PRO E   90  UNP  P01375    LYS   166 ENGINEERED MUTATION
SEQADV 3ALQ ARG E   98  UNP  P01375    LYS   174 ENGINEERED MUTATION
SEQADV 3ALQ ASN E  112  UNP  P01375    LYS   188 ENGINEERED MUTATION
SEQADV 3ALQ PRO E  128  UNP  P01375    LYS   204 ENGINEERED MUTATION
SEQADV 3ALQ MET F   11  UNP  P01375    LYS    87 ENGINEERED MUTATION
SEQADV 3ALQ SER F   65  UNP  P01375    LYS   141 ENGINEERED MUTATION
SEQADV 3ALQ PRO F   90  UNP  P01375    LYS   166 ENGINEERED MUTATION
SEQADV 3ALQ ARG F   98  UNP  P01375    LYS   174 ENGINEERED MUTATION
SEQADV 3ALQ ASN F  112  UNP  P01375    LYS   188 ENGINEERED MUTATION
SEQADV 3ALQ PRO F  128  UNP  P01375    LYS   204 ENGINEERED MUTATION
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL
SEQRES   2 A  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 A  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 A  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 A  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER
SEQRES   6 A  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 A  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP
SEQRES  11 A  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP
SEQRES  12 A  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 A  157  LEU
SEQRES   1 B  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL
SEQRES   2 B  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 B  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 B  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 B  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER
SEQRES   6 B  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 B  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL
SEQRES   8 B  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 B  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 B  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP
SEQRES  11 B  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP
SEQRES  12 B  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 B  157  LEU
SEQRES   1 C  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL
SEQRES   2 C  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 C  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 C  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 C  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER
SEQRES   6 C  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 C  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP
SEQRES  11 C  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 C  157  LEU
SEQRES   1 D  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL
SEQRES   2 D  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 D  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 D  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 D  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER
SEQRES   6 D  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 D  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL
SEQRES   8 D  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 D  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 D  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP
SEQRES  11 D  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP
SEQRES  12 D  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 D  157  LEU
SEQRES   1 E  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL
SEQRES   2 E  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 E  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 E  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 E  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER
SEQRES   6 E  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 E  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL
SEQRES   8 E  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 E  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 E  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP
SEQRES  11 E  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP
SEQRES  12 E  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 E  157  LEU
SEQRES   1 F  157  VAL ARG SER SER SER ARG THR PRO SER ASP MET PRO VAL
SEQRES   2 F  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU
SEQRES   3 F  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN
SEQRES   4 F  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER
SEQRES   5 F  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE SER
SEQRES   6 F  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS
SEQRES   7 F  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR PRO VAL
SEQRES   8 F  157  ASN LEU LEU SER ALA ILE ARG SER PRO CYS GLN ARG GLU
SEQRES   9 F  157  THR PRO GLU GLY ALA GLU ALA ASN PRO TRP TYR GLU PRO
SEQRES  10 F  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU PRO GLY ASP
SEQRES  11 F  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP
SEQRES  12 F  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA
SEQRES  13 F  157  LEU
SEQRES   1 R  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR
SEQRES   2 R  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER
SEQRES   3 R  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER
SEQRES   4 R  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR
SEQRES   5 R  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY
SEQRES   6 R  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS
SEQRES   7 R  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY
SEQRES   8 R  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU
SEQRES   9 R  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL
SEQRES  10 R  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS
SEQRES  11 R  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER
SEQRES  12 R  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL
SEQRES  13 R  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR
SEQRES  14 R  173  SER THR SER PRO
SEQRES   1 S  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR
SEQRES   2 S  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER
SEQRES   3 S  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER
SEQRES   4 S  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR
SEQRES   5 S  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY
SEQRES   6 S  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS
SEQRES   7 S  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY
SEQRES   8 S  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU
SEQRES   9 S  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL
SEQRES  10 S  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS
SEQRES  11 S  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER
SEQRES  12 S  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL
SEQRES  13 S  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR
SEQRES  14 S  173  SER THR SER PRO
SEQRES   1 T  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR
SEQRES   2 T  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER
SEQRES   3 T  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER
SEQRES   4 T  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR
SEQRES   5 T  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY
SEQRES   6 T  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS
SEQRES   7 T  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY
SEQRES   8 T  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU
SEQRES   9 T  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL
SEQRES  10 T  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS
SEQRES  11 T  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER
SEQRES  12 T  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL
SEQRES  13 T  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR
SEQRES  14 T  173  SER THR SER PRO
SEQRES   1 U  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR
SEQRES   2 U  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER
SEQRES   3 U  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER
SEQRES   4 U  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR
SEQRES   5 U  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY
SEQRES   6 U  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS
SEQRES   7 U  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY
SEQRES   8 U  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU
SEQRES   9 U  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL
SEQRES  10 U  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS
SEQRES  11 U  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER
SEQRES  12 U  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL
SEQRES  13 U  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR
SEQRES  14 U  173  SER THR SER PRO
SEQRES   1 V  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR
SEQRES   2 V  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER
SEQRES   3 V  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER
SEQRES   4 V  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR
SEQRES   5 V  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY
SEQRES   6 V  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS
SEQRES   7 V  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY
SEQRES   8 V  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU
SEQRES   9 V  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL
SEQRES  10 V  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS
SEQRES  11 V  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER
SEQRES  12 V  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL
SEQRES  13 V  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR
SEQRES  14 V  173  SER THR SER PRO
SEQRES   1 W  173  ALA PRO GLU PRO GLY SER THR CYS ARG LEU ARG GLU TYR
SEQRES   2 W  173  TYR ASP GLN THR ALA GLN MET CYS CYS SER LYS CYS SER
SEQRES   3 W  173  PRO GLY GLN HIS ALA LYS VAL PHE CYS THR LYS THR SER
SEQRES   4 W  173  ASP THR VAL CYS ASP SER CYS GLU ASP SER THR TYR THR
SEQRES   5 W  173  GLN LEU TRP ASN TRP VAL PRO GLU CYS LEU SER CYS GLY
SEQRES   6 W  173  SER ARG CYS SER SER ASP GLN VAL GLU THR GLN ALA CYS
SEQRES   7 W  173  THR ARG GLU GLN ASN ARG ILE CYS THR CYS ARG PRO GLY
SEQRES   8 W  173  TRP TYR CYS ALA LEU SER LYS GLN GLU GLY CYS ARG LEU
SEQRES   9 W  173  CYS ALA PRO LEU ARG LYS CYS ARG PRO GLY PHE GLY VAL
SEQRES  10 W  173  ALA ARG PRO GLY THR GLU THR SER ASP VAL VAL CYS LYS
SEQRES  11 W  173  PRO CYS ALA PRO GLY THR PHE SER ASN THR THR SER SER
SEQRES  12 W  173  THR ASP ILE CYS ARG PRO HIS GLN ILE CYS ASN VAL VAL
SEQRES  13 W  173  ALA ILE PRO GLY ASN ALA SER MET ASP ALA VAL CYS THR
SEQRES  14 W  173  SER THR SER PRO
HET     CO  R   2       1
HET     CO  S   1       1
HET     CO  T   3       1
HET     CO  U   4       1
HET     CO  V   5       1
HET     CO  W   6       1
HETNAM      CO COBALT (II) ION
FORMUL  13   CO    6(CO 2+)
FORMUL  19  HOH   *11(H2 O)
HELIX    1   1 ARG A  138  LEU A  142  5                                   5
HELIX    2   2 ARG B  138  LEU B  142  5                                   5
HELIX    3   3 ARG C  138  LEU C  142  5                                   5
HELIX    4   4 ARG D  138  LEU D  142  5                                   5
HELIX    5   5 ARG E  138  LEU E  142  5                                   5
SHEET    1   A 3 TRP A  28  LEU A  29  0
SHEET    2   A 3 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29
SHEET    3   A 3 LEU A  36  ALA A  38 -1  O  LEU A  36   N  HIS A  15
SHEET    1   B 5 TRP A  28  LEU A  29  0
SHEET    2   B 5 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29
SHEET    3   B 5 TYR A 151  ALA A 156 -1  O  ILE A 154   N  ALA A  14
SHEET    4   B 5 GLY A  54  GLY A  66 -1  N  TYR A  59   O  GLY A 153
SHEET    5   B 5 TRP A 114  LEU A 126 -1  O  PHE A 124   N  TYR A  56
SHEET    1   C 5 GLU A  42  ARG A  44  0
SHEET    2   C 5 GLN A  47  VAL A  49 -1  O  VAL A  49   N  GLU A  42
SHEET    3   C 5 ARG A 131  ILE A 136 -1  O  LEU A 132   N  LEU A  48
SHEET    4   C 5 LEU A  76  ALA A  84 -1  N  THR A  79   O  GLU A 135
SHEET    5   C 5 TYR A  87  ARG A  98 -1  O  ARG A  98   N  LEU A  76
SHEET    1   D 3 TRP B  28  LEU B  29  0
SHEET    2   D 3 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29
SHEET    3   D 3 LEU B  36  ALA B  38 -1  O  LEU B  36   N  HIS B  15
SHEET    1   E 5 TRP B  28  LEU B  29  0
SHEET    2   E 5 VAL B  13  ALA B  18 -1  N  VAL B  17   O  LEU B  29
SHEET    3   E 5 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16
SHEET    4   E 5 GLY B  54  GLY B  66 -1  N  TYR B  59   O  GLY B 153
SHEET    5   E 5 TRP B 114  LEU B 126 -1  O  PHE B 124   N  TYR B  56
SHEET    1   F 5 GLU B  42  ARG B  44  0
SHEET    2   F 5 GLN B  47  VAL B  49 -1  O  VAL B  49   N  GLU B  42
SHEET    3   F 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48
SHEET    4   F 5 LEU B  76  ALA B  84 -1  N  SER B  81   O  SER B 133
SHEET    5   F 5 TYR B  87  ARG B  98 -1  O  ARG B  98   N  LEU B  76
SHEET    1   G 3 TRP C  28  LEU C  29  0
SHEET    2   G 3 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29
SHEET    3   G 3 LEU C  36  ALA C  38 -1  O  LEU C  36   N  HIS C  15
SHEET    1   H 5 TRP C  28  LEU C  29  0
SHEET    2   H 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29
SHEET    3   H 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16
SHEET    4   H 5 GLY C  54  GLY C  66 -1  N  TYR C  59   O  GLY C 153
SHEET    5   H 5 TRP C 114  LEU C 126 -1  O  GLY C 122   N  ILE C  58
SHEET    1   I 5 GLU C  42  ARG C  44  0
SHEET    2   I 5 GLN C  47  VAL C  49 -1  O  VAL C  49   N  GLU C  42
SHEET    3   I 5 ARG C 131  ILE C 136 -1  O  LEU C 132   N  LEU C  48
SHEET    4   I 5 LEU C  76  ALA C  84 -1  N  ILE C  83   O  ARG C 131
SHEET    5   I 5 TYR C  87  ARG C  98 -1  O  VAL C  91   N  ARG C  82
SHEET    1   J 3 TRP D  28  LEU D  29  0
SHEET    2   J 3 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29
SHEET    3   J 3 LEU D  36  ALA D  38 -1  O  LEU D  36   N  HIS D  15
SHEET    1   K 5 TRP D  28  LEU D  29  0
SHEET    2   K 5 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29
SHEET    3   K 5 TYR D 151  ALA D 156 -1  O  PHE D 152   N  VAL D  16
SHEET    4   K 5 GLY D  54  GLY D  66 -1  N  LEU D  57   O  ILE D 155
SHEET    5   K 5 TRP D 114  LEU D 126 -1  O  GLU D 116   N  PHE D  64
SHEET    1   L 5 GLU D  42  ARG D  44  0
SHEET    2   L 5 GLN D  47  VAL D  49 -1  O  GLN D  47   N  ARG D  44
SHEET    3   L 5 ARG D 131  ILE D 136 -1  O  LEU D 132   N  LEU D  48
SHEET    4   L 5 LEU D  76  ILE D  83 -1  N  THR D  79   O  GLU D 135
SHEET    5   L 5 VAL D  91  ARG D  98 -1  O  ARG D  98   N  LEU D  76
SHEET    1   M 3 TRP E  28  LEU E  29  0
SHEET    2   M 3 VAL E  13  ALA E  18 -1  N  VAL E  17   O  LEU E  29
SHEET    3   M 3 LEU E  36  ALA E  38 -1  O  LEU E  36   N  HIS E  15
SHEET    1   N 5 TRP E  28  LEU E  29  0
SHEET    2   N 5 VAL E  13  ALA E  18 -1  N  VAL E  17   O  LEU E  29
SHEET    3   N 5 TYR E 151  ALA E 156 -1  O  ILE E 154   N  ALA E  14
SHEET    4   N 5 GLY E  54  GLY E  66 -1  N  TYR E  59   O  GLY E 153
SHEET    5   N 5 TRP E 114  LEU E 126 -1  O  GLU E 116   N  PHE E  64
SHEET    1   O 5 GLU E  42  ARG E  44  0
SHEET    2   O 5 GLN E  47  VAL E  49 -1  O  GLN E  47   N  ARG E  44
SHEET    3   O 5 ARG E 131  ILE E 136 -1  O  LEU E 132   N  LEU E  48
SHEET    4   O 5 LEU E  76  ILE E  83 -1  N  ILE E  83   O  ARG E 131
SHEET    5   O 5 VAL E  91  ARG E  98 -1  O  LEU E  93   N  ILE E  80
SHEET    1   P 3 TRP F  28  LEU F  29  0
SHEET    2   P 3 VAL F  13  ALA F  18 -1  N  VAL F  17   O  LEU F  29
SHEET    3   P 3 LEU F  36  ALA F  38 -1  O  LEU F  36   N  HIS F  15
SHEET    1   Q 5 TRP F  28  LEU F  29  0
SHEET    2   Q 5 VAL F  13  ALA F  18 -1  N  VAL F  17   O  LEU F  29
SHEET    3   Q 5 TYR F 151  ALA F 156 -1  O  PHE F 152   N  VAL F  16
SHEET    4   Q 5 GLY F  54  GLY F  66 -1  N  LEU F  57   O  ILE F 155
SHEET    5   Q 5 TRP F 114  LEU F 126 -1  O  GLY F 122   N  ILE F  58
SHEET    1   R 5 GLU F  42  ARG F  44  0
SHEET    2   R 5 GLN F  47  VAL F  49 -1  O  VAL F  49   N  GLU F  42
SHEET    3   R 5 ARG F 131  ILE F 136 -1  O  LEU F 132   N  LEU F  48
SHEET    4   R 5 LEU F  76  ILE F  83 -1  N  ILE F  83   O  ARG F 131
SHEET    5   R 5 VAL F  91  ARG F  98 -1  O  ARG F  98   N  LEU F  76
SHEET    1   S 2 GLU R  22  ASP R  25  0
SHEET    2   S 2 MET R  30  SER R  33 -1  O  CYS R  32   N  TYR R  23
SHEET    1   T 2 GLN R  39  VAL R  43  0
SHEET    2   T 2 VAL R  52  SER R  55 -1  O  VAL R  52   N  VAL R  43
SHEET    1   U 2 THR R  60  TYR R  61  0
SHEET    2   U 2 LEU R  72  SER R  73 -1  O  LEU R  72   N  TYR R  61
SHEET    1   V 2 GLN R  82  GLN R  86  0
SHEET    2   V 2 ILE R  95  CYS R  98 -1  O  THR R  97   N  VAL R  83
SHEET    1   W 2 TRP R 102  SER R 107  0
SHEET    2   W 2 CYS R 112  PRO R 117 -1  O  ARG R 113   N  LEU R 106
SHEET    1   X 2 PHE R 125  ARG R 129  0
SHEET    2   X 2 VAL R 138  PRO R 141 -1  O  LYS R 140   N  GLY R 126
SHEET    1   Y 2 THR R 146  PHE R 147  0
SHEET    2   Y 2 ARG R 158  PRO R 159 -1  O  ARG R 158   N  PHE R 147
SHEET    1   Z 2 GLU S  22  ASP S  25  0
SHEET    2   Z 2 MET S  30  SER S  33 -1  O  CYS S  32   N  TYR S  23
SHEET    1  AA 2 GLN S  39  VAL S  43  0
SHEET    2  AA 2 VAL S  52  SER S  55 -1  O  VAL S  52   N  LYS S  42
SHEET    1  AB 2 THR S  60  TYR S  61  0
SHEET    2  AB 2 LEU S  72  SER S  73 -1  O  LEU S  72   N  TYR S  61
SHEET    1  AC 2 GLN S  82  GLN S  86  0
SHEET    2  AC 2 ILE S  95  CYS S  98 -1  O  THR S  97   N  VAL S  83
SHEET    1  AD 2 TRP S 102  SER S 107  0
SHEET    2  AD 2 CYS S 112  PRO S 117 -1  O  ALA S 116   N  TYR S 103
SHEET    1  AE 2 PHE S 125  ARG S 129  0
SHEET    2  AE 2 VAL S 138  PRO S 141 -1  O  VAL S 138   N  ALA S 128
SHEET    1  AF 2 THR S 146  PHE S 147  0
SHEET    2  AF 2 ARG S 158  PRO S 159 -1  O  ARG S 158   N  PHE S 147
SHEET    1  AG 2 GLU T  22  ASP T  25  0
SHEET    2  AG 2 MET T  30  SER T  33 -1  O  CYS T  32   N  TYR T  23
SHEET    1  AH 2 GLN T  39  VAL T  43  0
SHEET    2  AH 2 VAL T  52  SER T  55 -1  O  VAL T  52   N  VAL T  43
SHEET    1  AI 2 THR T  60  TYR T  61  0
SHEET    2  AI 2 LEU T  72  SER T  73 -1  O  LEU T  72   N  TYR T  61
SHEET    1  AJ 2 GLN T  82  GLN T  86  0
SHEET    2  AJ 2 ILE T  95  CYS T  98 -1  O  THR T  97   N  VAL T  83
SHEET    1  AK 2 TRP T 102  LYS T 108  0
SHEET    2  AK 2 GLY T 111  PRO T 117 -1  O  ALA T 116   N  TYR T 103
SHEET    1  AL 2 PHE T 125  ARG T 129  0
SHEET    2  AL 2 VAL T 138  PRO T 141 -1  O  LYS T 140   N  GLY T 126
SHEET    1  AM 2 THR T 146  PHE T 147  0
SHEET    2  AM 2 ARG T 158  PRO T 159 -1  O  ARG T 158   N  PHE T 147
SHEET    1  AN 2 GLU U  22  ASP U  25  0
SHEET    2  AN 2 MET U  30  SER U  33 -1  O  CYS U  32   N  TYR U  23
SHEET    1  AO 2 GLN U  39  VAL U  43  0
SHEET    2  AO 2 VAL U  52  SER U  55 -1  O  VAL U  52   N  VAL U  43
SHEET    1  AP 2 THR U  60  TYR U  61  0
SHEET    2  AP 2 LEU U  72  SER U  73 -1  O  LEU U  72   N  TYR U  61
SHEET    1  AQ 2 GLN U  82  GLN U  86  0
SHEET    2  AQ 2 ILE U  95  CYS U  98 -1  O  THR U  97   N  VAL U  83
SHEET    1  AR 2 TRP U 102  SER U 107  0
SHEET    2  AR 2 CYS U 112  PRO U 117 -1  O  ARG U 113   N  LEU U 106
SHEET    1  AS 2 PHE U 125  ARG U 129  0
SHEET    2  AS 2 VAL U 138  PRO U 141 -1  O  VAL U 138   N  ALA U 128
SHEET    1  AT 2 THR U 146  PHE U 147  0
SHEET    2  AT 2 ARG U 158  PRO U 159 -1  O  ARG U 158   N  PHE U 147
SHEET    1  AU 2 GLU V  22  ASP V  25  0
SHEET    2  AU 2 MET V  30  SER V  33 -1  O  CYS V  32   N  TYR V  23
SHEET    1  AV 2 GLN V  39  VAL V  43  0
SHEET    2  AV 2 VAL V  52  SER V  55 -1  O  VAL V  52   N  VAL V  43
SHEET    1  AW 2 THR V  60  TYR V  61  0
SHEET    2  AW 2 LEU V  72  SER V  73 -1  O  LEU V  72   N  TYR V  61
SHEET    1  AX 2 GLN V  82  GLN V  86  0
SHEET    2  AX 2 ILE V  95  CYS V  98 -1  O  THR V  97   N  VAL V  83
SHEET    1  AY 2 TRP V 102  SER V 107  0
SHEET    2  AY 2 CYS V 112  PRO V 117 -1  O  ARG V 113   N  LEU V 106
SHEET    1  AZ 2 PHE V 125  ARG V 129  0
SHEET    2  AZ 2 VAL V 138  PRO V 141 -1  O  LYS V 140   N  GLY V 126
SHEET    1  BA 2 THR V 146  PHE V 147  0
SHEET    2  BA 2 ARG V 158  PRO V 159 -1  O  ARG V 158   N  PHE V 147
SHEET    1  BB 2 GLU W  22  ASP W  25  0
SHEET    2  BB 2 MET W  30  SER W  33 -1  O  MET W  30   N  ASP W  25
SHEET    1  BC 2 GLN W  39  VAL W  43  0
SHEET    2  BC 2 VAL W  52  SER W  55 -1  O  ASP W  54   N  HIS W  40
SHEET    1  BD 2 THR W  60  TYR W  61  0
SHEET    2  BD 2 LEU W  72  SER W  73 -1  O  LEU W  72   N  TYR W  61
SHEET    1  BE 2 GLN W  82  GLN W  86  0
SHEET    2  BE 2 ILE W  95  CYS W  98 -1  O  THR W  97   N  VAL W  83
SHEET    1  BF 2 TRP W 102  SER W 107  0
SHEET    2  BF 2 CYS W 112  PRO W 117 -1  O  ALA W 116   N  TYR W 103
SHEET    1  BG 2 PHE W 125  ARG W 129  0
SHEET    2  BG 2 VAL W 138  PRO W 141 -1  O  VAL W 138   N  ARG W 129
SHEET    1  BH 2 THR W 146  PHE W 147  0
SHEET    2  BH 2 ARG W 158  PRO W 159 -1  O  ARG W 158   N  PHE W 147
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.03
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  2.04
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.03
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.03
SSBOND   5 CYS E   69    CYS E  101                          1555   1555  2.03
SSBOND   6 CYS F   69    CYS F  101                          1555   1555  2.03
SSBOND   7 CYS R   18    CYS R   31                          1555   1555  2.04
SSBOND   8 CYS R   32    CYS R   45                          1555   1555  2.03
SSBOND   9 CYS R   35    CYS R   53                          1555   1555  2.05
SSBOND  10 CYS R   56    CYS R   71                          1555   1555  2.04
SSBOND  11 CYS R   74    CYS R   88                          1555   1555  2.03
SSBOND  12 CYS R   78    CYS R   96                          1555   1555  2.04
SSBOND  13 CYS R   98    CYS R  115                          1555   1555  2.03
SSBOND  14 CYS R  104    CYS R  112                          1555   1555  2.04
SSBOND  15 CYS R  121    CYS R  139                          1555   1555  2.03
SSBOND  16 CYS R  142    CYS R  157                          1555   1555  2.03
SSBOND  17 CYS R  163    CYS R  178                          1555   1555  2.04
SSBOND  18 CYS S   18    CYS S   31                          1555   1555  2.03
SSBOND  19 CYS S   32    CYS S   45                          1555   1555  2.03
SSBOND  20 CYS S   35    CYS S   53                          1555   1555  2.03
SSBOND  21 CYS S   56    CYS S   71                          1555   1555  2.04
SSBOND  22 CYS S   74    CYS S   88                          1555   1555  2.04
SSBOND  23 CYS S   78    CYS S   96                          1555   1555  2.03
SSBOND  24 CYS S   98    CYS S  115                          1555   1555  2.04
SSBOND  25 CYS S  104    CYS S  112                          1555   1555  2.03
SSBOND  26 CYS S  121    CYS S  139                          1555   1555  2.04
SSBOND  27 CYS S  142    CYS S  157                          1555   1555  2.03
SSBOND  28 CYS S  163    CYS S  178                          1555   1555  2.02
SSBOND  29 CYS T   18    CYS T   31                          1555   1555  2.04
SSBOND  30 CYS T   32    CYS T   45                          1555   1555  2.03
SSBOND  31 CYS T   35    CYS T   53                          1555   1555  2.04
SSBOND  32 CYS T   56    CYS T   71                          1555   1555  2.03
SSBOND  33 CYS T   74    CYS T   88                          1555   1555  2.04
SSBOND  34 CYS T   78    CYS T   96                          1555   1555  2.04
SSBOND  35 CYS T   98    CYS T  115                          1555   1555  2.03
SSBOND  36 CYS T  104    CYS T  112                          1555   1555  2.03
SSBOND  37 CYS T  121    CYS T  139                          1555   1555  2.03
SSBOND  38 CYS T  142    CYS T  157                          1555   1555  2.03
SSBOND  39 CYS T  163    CYS T  178                          1555   1555  2.02
SSBOND  40 CYS U   18    CYS U   31                          1555   1555  2.03
SSBOND  41 CYS U   32    CYS U   45                          1555   1555  2.03
SSBOND  42 CYS U   35    CYS U   53                          1555   1555  2.05
SSBOND  43 CYS U   56    CYS U   71                          1555   1555  2.04
SSBOND  44 CYS U   74    CYS U   88                          1555   1555  2.02
SSBOND  45 CYS U   78    CYS U   96                          1555   1555  2.03
SSBOND  46 CYS U   98    CYS U  115                          1555   1555  2.03
SSBOND  47 CYS U  104    CYS U  112                          1555   1555  2.04
SSBOND  48 CYS U  121    CYS U  139                          1555   1555  2.04
SSBOND  49 CYS U  142    CYS U  157                          1555   1555  2.05
SSBOND  50 CYS U  163    CYS U  178                          1555   1555  2.04
SSBOND  51 CYS V   18    CYS V   31                          1555   1555  2.03
SSBOND  52 CYS V   32    CYS V   45                          1555   1555  2.03
SSBOND  53 CYS V   35    CYS V   53                          1555   1555  2.04
SSBOND  54 CYS V   56    CYS V   71                          1555   1555  2.04
SSBOND  55 CYS V   74    CYS V   88                          1555   1555  2.04
SSBOND  56 CYS V   78    CYS V   96                          1555   1555  2.04
SSBOND  57 CYS V   98    CYS V  115                          1555   1555  2.04
SSBOND  58 CYS V  104    CYS V  112                          1555   1555  2.03
SSBOND  59 CYS V  121    CYS V  139                          1555   1555  2.03
SSBOND  60 CYS V  142    CYS V  157                          1555   1555  2.04
SSBOND  61 CYS V  163    CYS V  178                          1555   1555  2.04
SSBOND  62 CYS W   18    CYS W   31                          1555   1555  2.04
SSBOND  63 CYS W   32    CYS W   45                          1555   1555  2.04
SSBOND  64 CYS W   35    CYS W   53                          1555   1555  2.04
SSBOND  65 CYS W   56    CYS W   71                          1555   1555  2.04
SSBOND  66 CYS W   74    CYS W   88                          1555   1555  2.02
SSBOND  67 CYS W   78    CYS W   96                          1555   1555  2.04
SSBOND  68 CYS W   98    CYS W  115                          1555   1555  2.03
SSBOND  69 CYS W  104    CYS W  112                          1555   1555  2.04
SSBOND  70 CYS W  121    CYS W  139                          1555   1555  2.03
SSBOND  71 CYS W  142    CYS W  157                          1555   1555  2.04
SSBOND  72 CYS W  163    CYS W  178                          1555   1555  2.02
LINK         OD1 ASP R  54                CO    CO R   2     1555   1555  2.14
LINK         NE2 HIS S  40                CO    CO S   1     1555   1555  2.17
LINK         NE2 HIS U  40                CO    CO U   4     1555   1555  2.19
LINK         OD1 ASP S  54                CO    CO S   1     1555   1555  2.25
LINK         OD1 ASP T  54                CO    CO T   3     1555   1555  2.28
LINK         NE2 HIS R  40                CO    CO R   2     1555   1555  2.31
LINK         NE2 HIS V  40                CO    CO V   5     1555   1555  2.31
LINK         OD1 ASP W  54                CO    CO W   6     1555   1555  2.36
LINK         NE2 HIS T  40                CO    CO T   3     1555   1555  2.37
LINK         NE2 HIS W  40                CO    CO W   6     1555   1555  2.44
LINK         OD1 ASP U  54                CO    CO U   4     1555   1555  2.47
LINK         OE2 GLU T  57                CO    CO T   3     1555   1555  2.75
LINK         OD1 ASP V  54                CO    CO V   5     1555   1555  2.77
SITE     1 AC1  3 HIS R  40  ASP R  54  GLU R  57
SITE     1 AC2  3 HIS S  40  ASP S  54  GLU S  57
SITE     1 AC3  3 HIS T  40  ASP T  54  GLU T  57
SITE     1 AC4  2 HIS U  40  ASP U  54
SITE     1 AC5  2 HIS V  40  ASP V  54
SITE     1 AC6  3 HIS W  40  ASP W  54  GLU W  57
CRYST1   74.470  117.356  246.835  90.00  90.00  90.00 P 21 21 21   24
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013428  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008521  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004051        0.00000
      
PROCHECK
Go to PROCHECK summary
 References