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 3 01-NOV-23 3ALQ 1 REMARK SEQADV LINK
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 1.5_2
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER 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 : 0.282
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. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000029405.
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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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, R, S, T
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, E, F, U, V, W
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 HIS R 40 NE2
REMARK 620 2 ASP R 54 OD1 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 T 3 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS T 40 NE2
REMARK 620 2 ASP T 54 OD1 92.3
REMARK 620 3 GLU T 57 OE2 131.2 61.6
REMARK 620 N 1 2
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 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 HIS W 40 NE2
REMARK 620 2 ASP W 54 OD1 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 CO CO R 2 NE2 HIS R 40 1555 1555 2.31
LINK CO CO R 2 OD1 ASP R 54 1555 1555 2.14
LINK CO CO S 1 NE2 HIS S 40 1555 1555 2.17
LINK CO CO S 1 OD1 ASP S 54 1555 1555 2.25
LINK CO CO T 3 NE2 HIS T 40 1555 1555 2.37
LINK CO CO T 3 OD1 ASP T 54 1555 1555 2.28
LINK CO CO T 3 OE2 GLU T 57 1555 1555 2.75
LINK CO CO U 4 NE2 HIS U 40 1555 1555 2.19
LINK CO CO U 4 OD1 ASP U 54 1555 1555 2.47
LINK CO CO V 5 NE2 HIS V 40 1555 1555 2.31
LINK CO CO V 5 OD1 ASP V 54 1555 1555 2.77
LINK CO CO W 6 NE2 HIS W 40 1555 1555 2.44
LINK CO CO W 6 OD1 ASP W 54 1555 1555 2.36
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
(ATOM LINES ARE NOT SHOWN.)
END