HEADER VIRUS LIKE PARTICLE 21-JUL-09 3IDE
TITLE STRUCTURE OF IPNV SUBVIRAL PARTICLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAPSID PROTEIN VP2;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 SYNONYM: PP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: INFECTIOUS PANCREATIC NECROSIS VIRUS -;
SOURCE 3 ORGANISM_COMMON: IPNV;
SOURCE 4 ORGANISM_TAXID: 11005;
SOURCE 5 STRAIN: SP;
SOURCE 6 GENE: VP2;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC1
KEYWDS JELLY ROLL, BETA SANDWICH, ICOSAHEDRAL PARTICLE, VIRION, VIRUS LIKE
KEYWDS 2 PARTICLE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.COULIBALY,C.CHEVALIER,B.DELMAS,F.A.REY
REVDAT 6 01-NOV-17 3IDE 1 REMARK
REVDAT 5 13-JUL-11 3IDE 1 VERSN
REVDAT 4 09-FEB-10 3IDE 1 MTRIX1 MTRIX2 MTRIX3
REVDAT 3 02-FEB-10 3IDE 1 JRNL
REVDAT 2 26-JAN-10 3IDE 1 MTRIX1 MTRIX2 MTRIX3
REVDAT 1 29-DEC-09 3IDE 0
JRNL AUTH F.COULIBALY,C.CHEVALIER,B.DELMAS,F.A.REY
JRNL TITL CRYSTAL STRUCTURE OF AN AQUABIRNAVIRUS PARTICLE: INSIGHTS
JRNL TITL 2 INTO ANTIGENIC DIVERSITY AND VIRULENCE DETERMINISM
JRNL REF J.VIROL. V. 84 1792 2010
JRNL REFN ISSN 0022-538X
JRNL PMID 20007275
JRNL DOI 10.1128/JVI.01536-09
REMARK 2
REMARK 2 RESOLUTION. 3.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 3.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 65456
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
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 29.7550 - 8.0260 1.00 4707 166 0.1770 0.1790
REMARK 3 2 8.0260 - 6.3910 1.00 4633 166 0.1690 0.1960
REMARK 3 3 6.3910 - 5.5890 0.99 4622 83 0.1790 0.2010
REMARK 3 4 5.5890 - 5.0810 0.99 4572 166 0.1750 0.2020
REMARK 3 5 5.0810 - 4.7180 0.98 4439 166 0.1680 0.1590
REMARK 3 6 4.7180 - 4.4410 0.98 4537 83 0.1800 0.2070
REMARK 3 7 4.4410 - 4.2190 0.98 4442 166 0.2090 0.2190
REMARK 3 8 4.2190 - 4.0360 0.98 4447 166 0.2350 0.2580
REMARK 3 9 4.0360 - 3.8810 0.98 4562 83 0.2740 0.3000
REMARK 3 10 3.8810 - 3.7470 0.99 4493 166 0.2820 0.3120
REMARK 3 11 3.7470 - 3.6300 0.99 4497 166 0.2840 0.3160
REMARK 3 12 3.6300 - 3.5270 0.99 4527 166 0.3090 0.2720
REMARK 3 13 3.5270 - 3.4340 0.98 4540 83 0.3100 0.3720
REMARK 3 14 3.4340 - 3.3500 0.98 4446 166 0.3340 0.3080
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 : 0.27
REMARK 3 B_SOL : 43.88
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 99.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 : 0.005 16356
REMARK 3 ANGLE : 0.918 22267
REMARK 3 CHIRALITY : 0.065 2599
REMARK 3 PLANARITY : 0.003 2897
REMARK 3 DIHEDRAL : 18.010 6011
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8874 135.3274 127.5307
REMARK 3 T TENSOR
REMARK 3 T11: 0.6869 T22: 0.5377
REMARK 3 T33: 0.6104 T12: -0.1461
REMARK 3 T13: 0.0610 T23: -0.0694
REMARK 3 L TENSOR
REMARK 3 L11: 0.3118 L22: 2.1103
REMARK 3 L33: 0.9636 L12: 0.0144
REMARK 3 L13: -0.4907 L23: 0.6123
REMARK 3 S TENSOR
REMARK 3 S11: -0.2414 S12: 0.1584 S13: -0.0790
REMARK 3 S21: 0.6444 S22: 0.0661 S23: 0.1214
REMARK 3 S31: 0.4726 S32: -0.3203 S33: 0.1728
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 65.9286 137.0218 173.3840
REMARK 3 T TENSOR
REMARK 3 T11: 0.6663 T22: 0.5540
REMARK 3 T33: 0.6837 T12: -0.1963
REMARK 3 T13: -0.0266 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.4821 L22: 1.8119
REMARK 3 L33: 1.4784 L12: 0.4549
REMARK 3 L13: 0.6654 L23: -0.1525
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: -0.2208 S13: -0.1524
REMARK 3 S21: -0.4370 S22: 0.1141 S23: 0.2819
REMARK 3 S31: 0.4655 S32: -0.3935 S33: -0.1451
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 88.7542 100.6508 189.2645
REMARK 3 T TENSOR
REMARK 3 T11: 0.6739 T22: 0.6117
REMARK 3 T33: 0.5753 T12: -0.1018
REMARK 3 T13: 0.0209 T23: 0.1330
REMARK 3 L TENSOR
REMARK 3 L11: 0.3772 L22: 0.7363
REMARK 3 L33: 0.1988 L12: -0.0147
REMARK 3 L13: 0.5454 L23: -0.1278
REMARK 3 S TENSOR
REMARK 3 S11: -0.0350 S12: 0.1474 S13: 0.0231
REMARK 3 S21: -0.3063 S22: -0.0284 S23: 0.1405
REMARK 3 S31: 0.1555 S32: 0.0570 S33: 0.0489
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 103.6172 75.9217 153.1406
REMARK 3 T TENSOR
REMARK 3 T11: 0.5734 T22: 0.7254
REMARK 3 T33: 0.7673 T12: -0.0687
REMARK 3 T13: 0.0073 T23: 0.0684
REMARK 3 L TENSOR
REMARK 3 L11: 1.0237 L22: 0.0364
REMARK 3 L33: 1.7925 L12: -0.5098
REMARK 3 L13: -0.1972 L23: -0.1886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: 0.1073 S13: -0.4298
REMARK 3 S21: 0.0061 S22: 0.0782 S23: 0.2259
REMARK 3 S31: -0.1868 S32: -0.5722 S33: -0.0852
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): 90.3896 97.7562 115.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.5384 T22: 0.5468
REMARK 3 T33: 0.4828 T12: -0.0614
REMARK 3 T13: -0.0155 T23: -0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 0.6045 L22: 0.7601
REMARK 3 L33: 0.5274 L12: 0.1384
REMARK 3 L13: -0.0412 L23: -0.2390
REMARK 3 S TENSOR
REMARK 3 S11: -0.0157 S12: -0.2083 S13: -0.0054
REMARK 3 S21: 0.2214 S22: 0.0638 S23: 0.1306
REMARK 3 S31: -0.0970 S32: -0.0609 S33: -0.0422
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 ATOM PAIRS NUMBER : 3208
REMARK 3 RMSD : 0.014
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 ATOM PAIRS NUMBER : 3208
REMARK 3 RMSD : 0.016
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 ATOM PAIRS NUMBER : 3208
REMARK 3 RMSD : 0.013
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 6:109 OR RESSEQ
REMARK 3 118:428 )
REMARK 3 ATOM PAIRS NUMBER : 3208
REMARK 3 RMSD : 0.021
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054271.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9500
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66153
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.37900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M 1,6-HEXANEDIOL, 10MM COCL2, 100MM
REMARK 280 SODIUM ACETATE PH 4.6, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 151.71550
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 151.71550
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 151.71550
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 151.71550
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 151.71550
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 151.71550
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 151.71550
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 151.71550
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 151.71550
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 151.71550
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 151.71550
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 151.71550
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 151.71550
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 151.71550
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 151.71550
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 151.71550
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 151.71550
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 151.71550
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 151.71550
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 151.71550
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 151.71550
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 151.71550
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 151.71550
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 151.71550
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 151.71550
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 151.71550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE ENTRY CONTAINS THE ASYMMETRIC UNIT OF THE T=1
REMARK 300 ICOSAHEDRAL PARTICLE.
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: 60-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 303.43100
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 303.43100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 303.43100
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 303.43100
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 303.43100
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 303.43100
REMARK 350 BIOMT1 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 303.43100
REMARK 350 BIOMT3 6 0.000000 -1.000000 0.000000 303.43100
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 303.43100
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 303.43100
REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 0.000000 -1.000000 303.43100
REMARK 350 BIOMT2 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 -1.000000 0.000000 303.43100
REMARK 350 BIOMT1 9 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 9 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 9 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 303.43100
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 10 -1.000000 0.000000 0.000000 303.43100
REMARK 350 BIOMT1 11 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 0.000000 -1.000000 303.43100
REMARK 350 BIOMT3 11 -1.000000 0.000000 0.000000 303.43100
REMARK 350 BIOMT1 12 0.000000 -1.000000 0.000000 303.43100
REMARK 350 BIOMT2 12 0.000000 0.000000 -1.000000 303.43100
REMARK 350 BIOMT3 12 1.000000 0.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CO CO C 443 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL C 444 LIES ON A SPECIAL POSITION.
REMARK 375 CO CO E 443 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL E 444 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 THR A 3
REMARK 465 ASN A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 110
REMARK 465 PRO A 111
REMARK 465 ALA A 112
REMARK 465 GLY A 113
REMARK 465 LEU A 114
REMARK 465 TYR A 115
REMARK 465 ALA A 116
REMARK 465 LEU A 117
REMARK 465 GLU A 429
REMARK 465 ILE A 430
REMARK 465 THR A 431
REMARK 465 ASP A 432
REMARK 465 PHE A 433
REMARK 465 SER A 434
REMARK 465 SER A 435
REMARK 465 ASP A 436
REMARK 465 LEU A 437
REMARK 465 PRO A 438
REMARK 465 THR A 439
REMARK 465 SER A 440
REMARK 465 LYS A 441
REMARK 465 ALA A 442
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 ASN B 4
REMARK 465 LYS B 5
REMARK 465 PRO B 111
REMARK 465 ALA B 112
REMARK 465 GLY B 113
REMARK 465 LEU B 114
REMARK 465 TYR B 115
REMARK 465 ALA B 116
REMARK 465 LEU B 117
REMARK 465 GLU B 429
REMARK 465 ILE B 430
REMARK 465 THR B 431
REMARK 465 ASP B 432
REMARK 465 PHE B 433
REMARK 465 SER B 434
REMARK 465 SER B 435
REMARK 465 ASP B 436
REMARK 465 LEU B 437
REMARK 465 PRO B 438
REMARK 465 THR B 439
REMARK 465 SER B 440
REMARK 465 LYS B 441
REMARK 465 ALA B 442
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 THR C 3
REMARK 465 ASN C 4
REMARK 465 LYS C 5
REMARK 465 LEU C 110
REMARK 465 PRO C 111
REMARK 465 ALA C 112
REMARK 465 GLY C 113
REMARK 465 LEU C 114
REMARK 465 TYR C 115
REMARK 465 ALA C 116
REMARK 465 LEU C 117
REMARK 465 GLU C 429
REMARK 465 ILE C 430
REMARK 465 THR C 431
REMARK 465 ASP C 432
REMARK 465 PHE C 433
REMARK 465 SER C 434
REMARK 465 SER C 435
REMARK 465 ASP C 436
REMARK 465 LEU C 437
REMARK 465 PRO C 438
REMARK 465 THR C 439
REMARK 465 SER C 440
REMARK 465 LYS C 441
REMARK 465 ALA C 442
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 THR D 3
REMARK 465 ASN D 4
REMARK 465 LYS D 5
REMARK 465 PRO D 111
REMARK 465 ALA D 112
REMARK 465 GLY D 113
REMARK 465 LEU D 114
REMARK 465 TYR D 115
REMARK 465 ALA D 116
REMARK 465 LEU D 117
REMARK 465 GLU D 429
REMARK 465 ILE D 430
REMARK 465 THR D 431
REMARK 465 ASP D 432
REMARK 465 PHE D 433
REMARK 465 SER D 434
REMARK 465 SER D 435
REMARK 465 ASP D 436
REMARK 465 LEU D 437
REMARK 465 PRO D 438
REMARK 465 THR D 439
REMARK 465 SER D 440
REMARK 465 LYS D 441
REMARK 465 ALA D 442
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 THR E 3
REMARK 465 ASN E 4
REMARK 465 LYS E 5
REMARK 465 LEU E 110
REMARK 465 PRO E 111
REMARK 465 ALA E 112
REMARK 465 GLY E 113
REMARK 465 LEU E 114
REMARK 465 TYR E 115
REMARK 465 ALA E 116
REMARK 465 LEU E 117
REMARK 465 GLU E 429
REMARK 465 ILE E 430
REMARK 465 THR E 431
REMARK 465 ASP E 432
REMARK 465 PHE E 433
REMARK 465 SER E 434
REMARK 465 SER E 435
REMARK 465 ASP E 436
REMARK 465 LEU E 437
REMARK 465 PRO E 438
REMARK 465 THR E 439
REMARK 465 SER E 440
REMARK 465 LYS E 441
REMARK 465 ALA E 442
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 ALA A 8 3.39 -65.20
REMARK 500 PRO A 25 41.96 -78.80
REMARK 500 ASP A 26 -158.61 -109.51
REMARK 500 ILE A 28 59.72 -97.70
REMARK 500 PHE A 56 67.27 -116.63
REMARK 500 ASP A 80 -66.29 -98.73
REMARK 500 GLU A 127 42.01 -93.65
REMARK 500 THR A 168 63.07 -101.04
REMARK 500 MET A 188 153.67 -47.77
REMARK 500 ALA A 198 -39.91 -130.62
REMARK 500 ALA A 200 70.73 41.03
REMARK 500 ASN A 267 11.05 53.63
REMARK 500 ASP A 268 5.96 52.56
REMARK 500 THR A 293 8.75 -150.69
REMARK 500 ILE A 314 -159.72 -112.24
REMARK 500 THR A 318 23.24 -75.03
REMARK 500 ASN A 340 -2.94 63.03
REMARK 500 HIS A 405 37.10 -91.23
REMARK 500 LEU A 409 -172.58 -64.29
REMARK 500 ARG A 423 6.68 -68.13
REMARK 500 ARG A 425 4.70 -65.97
REMARK 500 ALA B 8 3.28 -65.07
REMARK 500 PRO B 25 42.20 -78.83
REMARK 500 ASP B 26 -159.38 -110.39
REMARK 500 PHE B 56 67.38 -116.16
REMARK 500 ASP B 80 -66.18 -99.02
REMARK 500 GLU B 127 41.85 -93.77
REMARK 500 THR B 168 63.10 -100.42
REMARK 500 MET B 188 153.96 -47.98
REMARK 500 ALA B 198 -39.38 -130.48
REMARK 500 ALA B 200 71.30 41.53
REMARK 500 ASN B 267 10.87 53.83
REMARK 500 ASP B 268 6.06 52.78
REMARK 500 THR B 293 9.17 -150.10
REMARK 500 ILE B 314 -159.29 -112.66
REMARK 500 THR B 318 23.61 -75.23
REMARK 500 ASN B 340 -3.70 63.48
REMARK 500 HIS B 405 38.40 -92.05
REMARK 500 LEU B 409 -172.41 -63.63
REMARK 500 ARG B 423 6.68 -68.12
REMARK 500 ARG B 425 4.69 -66.19
REMARK 500 ALA C 8 3.72 -65.39
REMARK 500 PRO C 25 42.77 -79.29
REMARK 500 ASP C 26 -158.96 -111.00
REMARK 500 PHE C 56 66.84 -116.76
REMARK 500 ASP C 80 -66.43 -98.57
REMARK 500 GLU C 127 41.40 -93.54
REMARK 500 THR C 168 62.73 -100.49
REMARK 500 MET C 188 153.50 -48.53
REMARK 500 ALA C 198 -38.11 -131.06
REMARK 500
REMARK 500 THIS ENTRY HAS 101 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 A 443 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 27 OD2
REMARK 620 2 ASP B 27 OD2 74.1
REMARK 620 3 ASP D 27 OD2 129.0 73.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 443
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 444
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO C 443
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 444
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO E 443
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 444
DBREF 3IDE A 1 442 UNP Q703G9 POLS_IPNVS 1 442
DBREF 3IDE B 1 442 UNP Q703G9 POLS_IPNVS 1 442
DBREF 3IDE C 1 442 UNP Q703G9 POLS_IPNVS 1 442
DBREF 3IDE D 1 442 UNP Q703G9 POLS_IPNVS 1 442
DBREF 3IDE E 1 442 UNP Q703G9 POLS_IPNVS 1 442
SEQRES 1 A 442 MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER
SEQRES 2 A 442 ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP
SEQRES 3 A 442 ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER
SEQRES 4 A 442 SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL
SEQRES 5 A 442 LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY
SEQRES 6 A 442 ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU
SEQRES 7 A 442 PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS
SEQRES 8 A 442 ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP
SEQRES 9 A 442 ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU
SEQRES 10 A 442 ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU
SEQRES 11 A 442 SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER
SEQRES 12 A 442 LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU
SEQRES 13 A 442 VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY
SEQRES 14 A 442 PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO
SEQRES 15 A 442 GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS
SEQRES 16 A 442 THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU
SEQRES 17 A 442 PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR
SEQRES 18 A 442 LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN
SEQRES 19 A 442 SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA
SEQRES 20 A 442 GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU
SEQRES 21 A 442 ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR
SEQRES 22 A 442 VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG
SEQRES 23 A 442 GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU
SEQRES 24 A 442 ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR
SEQRES 25 A 442 LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR
SEQRES 26 A 442 LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER
SEQRES 27 A 442 GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR
SEQRES 28 A 442 LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU
SEQRES 29 A 442 THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN
SEQRES 30 A 442 PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS
SEQRES 31 A 442 TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU
SEQRES 32 A 442 SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG
SEQRES 33 A 442 THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU
SEQRES 34 A 442 ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA
SEQRES 1 B 442 MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER
SEQRES 2 B 442 ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP
SEQRES 3 B 442 ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER
SEQRES 4 B 442 SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL
SEQRES 5 B 442 LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY
SEQRES 6 B 442 ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU
SEQRES 7 B 442 PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS
SEQRES 8 B 442 ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP
SEQRES 9 B 442 ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU
SEQRES 10 B 442 ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU
SEQRES 11 B 442 SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER
SEQRES 12 B 442 LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU
SEQRES 13 B 442 VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY
SEQRES 14 B 442 PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO
SEQRES 15 B 442 GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS
SEQRES 16 B 442 THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU
SEQRES 17 B 442 PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR
SEQRES 18 B 442 LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN
SEQRES 19 B 442 SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA
SEQRES 20 B 442 GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU
SEQRES 21 B 442 ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR
SEQRES 22 B 442 VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG
SEQRES 23 B 442 GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU
SEQRES 24 B 442 ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR
SEQRES 25 B 442 LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR
SEQRES 26 B 442 LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER
SEQRES 27 B 442 GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR
SEQRES 28 B 442 LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU
SEQRES 29 B 442 THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN
SEQRES 30 B 442 PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS
SEQRES 31 B 442 TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU
SEQRES 32 B 442 SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG
SEQRES 33 B 442 THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU
SEQRES 34 B 442 ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA
SEQRES 1 C 442 MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER
SEQRES 2 C 442 ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP
SEQRES 3 C 442 ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER
SEQRES 4 C 442 SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL
SEQRES 5 C 442 LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY
SEQRES 6 C 442 ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU
SEQRES 7 C 442 PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS
SEQRES 8 C 442 ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP
SEQRES 9 C 442 ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU
SEQRES 10 C 442 ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU
SEQRES 11 C 442 SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER
SEQRES 12 C 442 LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU
SEQRES 13 C 442 VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY
SEQRES 14 C 442 PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO
SEQRES 15 C 442 GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS
SEQRES 16 C 442 THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU
SEQRES 17 C 442 PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR
SEQRES 18 C 442 LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN
SEQRES 19 C 442 SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA
SEQRES 20 C 442 GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU
SEQRES 21 C 442 ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR
SEQRES 22 C 442 VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG
SEQRES 23 C 442 GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU
SEQRES 24 C 442 ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR
SEQRES 25 C 442 LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR
SEQRES 26 C 442 LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER
SEQRES 27 C 442 GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR
SEQRES 28 C 442 LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU
SEQRES 29 C 442 THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN
SEQRES 30 C 442 PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS
SEQRES 31 C 442 TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU
SEQRES 32 C 442 SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG
SEQRES 33 C 442 THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU
SEQRES 34 C 442 ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA
SEQRES 1 D 442 MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER
SEQRES 2 D 442 ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP
SEQRES 3 D 442 ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER
SEQRES 4 D 442 SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL
SEQRES 5 D 442 LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY
SEQRES 6 D 442 ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU
SEQRES 7 D 442 PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS
SEQRES 8 D 442 ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP
SEQRES 9 D 442 ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU
SEQRES 10 D 442 ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU
SEQRES 11 D 442 SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER
SEQRES 12 D 442 LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU
SEQRES 13 D 442 VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY
SEQRES 14 D 442 PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO
SEQRES 15 D 442 GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS
SEQRES 16 D 442 THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU
SEQRES 17 D 442 PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR
SEQRES 18 D 442 LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN
SEQRES 19 D 442 SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA
SEQRES 20 D 442 GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU
SEQRES 21 D 442 ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR
SEQRES 22 D 442 VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG
SEQRES 23 D 442 GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU
SEQRES 24 D 442 ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR
SEQRES 25 D 442 LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR
SEQRES 26 D 442 LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER
SEQRES 27 D 442 GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR
SEQRES 28 D 442 LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU
SEQRES 29 D 442 THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN
SEQRES 30 D 442 PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS
SEQRES 31 D 442 TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU
SEQRES 32 D 442 SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG
SEQRES 33 D 442 THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU
SEQRES 34 D 442 ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA
SEQRES 1 E 442 MET ASN THR ASN LYS ALA THR ALA THR TYR LEU LYS SER
SEQRES 2 E 442 ILE MET LEU PRO GLU THR GLY PRO ALA SER ILE PRO ASP
SEQRES 3 E 442 ASP ILE THR GLU ARG HIS ILE LEU LYS GLN GLU THR SER
SEQRES 4 E 442 SER TYR ASN LEU GLU VAL SER GLU SER GLY SER GLY VAL
SEQRES 5 E 442 LEU VAL CYS PHE PRO GLY ALA PRO GLY SER ARG ILE GLY
SEQRES 6 E 442 ALA HIS TYR ARG TRP ASN ALA ASN GLN THR GLY LEU GLU
SEQRES 7 E 442 PHE ASP GLN TRP LEU GLU THR SER GLN ASP LEU LYS LYS
SEQRES 8 E 442 ALA PHE ASN TYR GLY ARG LEU ILE SER ARG LYS TYR ASP
SEQRES 9 E 442 ILE GLN SER SER THR LEU PRO ALA GLY LEU TYR ALA LEU
SEQRES 10 E 442 ASN GLY THR LEU ASN ALA ALA THR PHE GLU GLY SER LEU
SEQRES 11 E 442 SER GLU VAL GLU SER LEU THR TYR ASN SER LEU MET SER
SEQRES 12 E 442 LEU THR THR ASN PRO GLN ASP LYS VAL ASN ASN GLN LEU
SEQRES 13 E 442 VAL THR LYS GLY VAL THR VAL LEU ASN LEU PRO THR GLY
SEQRES 14 E 442 PHE ASP LYS PRO TYR VAL ARG LEU GLU ASP GLU THR PRO
SEQRES 15 E 442 GLN GLY LEU GLN SER MET ASN GLY ALA LYS MET ARG CYS
SEQRES 16 E 442 THR ALA ALA ILE ALA PRO ARG ARG TYR GLU ILE ASP LEU
SEQRES 17 E 442 PRO SER GLN ARG LEU PRO PRO VAL PRO ALA THR GLY THR
SEQRES 18 E 442 LEU THR THR LEU TYR GLU GLY ASN ALA ASP ILE VAL ASN
SEQRES 19 E 442 SER THR THR VAL THR GLY ASP ILE ASN PHE SER LEU ALA
SEQRES 20 E 442 GLU GLN PRO ALA ASP GLU THR LYS PHE ASP PHE GLN LEU
SEQRES 21 E 442 ASP PHE MET GLY LEU ASP ASN ASP VAL PRO VAL VAL THR
SEQRES 22 E 442 VAL VAL SER SER VAL LEU ALA THR ASN ASP ASN TYR ARG
SEQRES 23 E 442 GLY VAL SER ALA LYS MET THR GLN SER ILE PRO THR GLU
SEQRES 24 E 442 ASN ILE THR LYS PRO ILE THR ARG VAL LYS LEU SER TYR
SEQRES 25 E 442 LYS ILE ASN GLN GLN THR ALA ILE GLY ASN VAL ALA THR
SEQRES 26 E 442 LEU GLY THR MET GLY PRO ALA SER VAL SER PHE SER SER
SEQRES 27 E 442 GLY ASN GLY ASN VAL PRO GLY VAL LEU ARG PRO ILE THR
SEQRES 28 E 442 LEU VAL ALA TYR GLU LYS MET THR PRO LEU SER ILE LEU
SEQRES 29 E 442 THR VAL ALA GLY VAL SER ASN TYR GLU LEU ILE PRO ASN
SEQRES 30 E 442 PRO GLU LEU LEU LYS ASN MET VAL THR ARG TYR GLY LYS
SEQRES 31 E 442 TYR ASP PRO GLU GLY LEU ASN TYR ALA LYS MET ILE LEU
SEQRES 32 E 442 SER HIS ARG GLU GLU LEU ASP ILE ARG THR VAL TRP ARG
SEQRES 33 E 442 THR GLU GLU TYR LYS GLU ARG THR ARG VAL PHE ASN GLU
SEQRES 34 E 442 ILE THR ASP PHE SER SER ASP LEU PRO THR SER LYS ALA
HET CO A 443 1
HET CL A 444 1
HET CO C 443 1
HET CL C 444 1
HET CO E 443 1
HET CL E 444 1
HETNAM CO COBALT (II) ION
HETNAM CL CHLORIDE ION
FORMUL 6 CO 3(CO 2+)
FORMUL 7 CL 3(CL 1-)
FORMUL 12 HOH *10(H2 O)
HELIX 1 1 ALA A 8 LEU A 16 1 9
HELIX 2 2 PRO A 17 GLY A 20 5 4
HELIX 3 3 ASP A 88 LYS A 91 5 4
HELIX 4 4 SER A 129 VAL A 133 5 5
HELIX 5 5 ASN A 139 LEU A 144 5 6
HELIX 6 6 ASN A 147 GLN A 149 5 3
HELIX 7 7 PRO A 297 ILE A 301 5 5
HELIX 8 8 GLN A 316 ILE A 320 5 5
HELIX 9 9 LEU A 326 GLY A 330 5 5
HELIX 10 10 ASN A 377 LYS A 382 1 6
HELIX 11 11 GLU A 394 HIS A 405 1 12
HELIX 12 12 THR A 417 ARG A 423 1 7
HELIX 13 13 THR A 424 ASN A 428 5 5
HELIX 14 14 ALA B 8 LEU B 16 1 9
HELIX 15 15 PRO B 17 GLY B 20 5 4
HELIX 16 16 ASP B 88 LYS B 91 5 4
HELIX 17 17 SER B 129 VAL B 133 5 5
HELIX 18 18 ASN B 139 LEU B 144 5 6
HELIX 19 19 ASN B 147 GLN B 149 5 3
HELIX 20 20 PRO B 297 ILE B 301 5 5
HELIX 21 21 GLN B 316 ILE B 320 5 5
HELIX 22 22 LEU B 326 GLY B 330 5 5
HELIX 23 23 ASN B 377 LYS B 382 1 6
HELIX 24 24 GLU B 394 HIS B 405 1 12
HELIX 25 25 THR B 417 ARG B 423 1 7
HELIX 26 26 THR B 424 ASN B 428 5 5
HELIX 27 27 ALA C 8 LEU C 16 1 9
HELIX 28 28 PRO C 17 GLY C 20 5 4
HELIX 29 29 ASP C 88 LYS C 91 5 4
HELIX 30 30 SER C 129 VAL C 133 5 5
HELIX 31 31 ASN C 139 LEU C 144 5 6
HELIX 32 32 ASN C 147 GLN C 149 5 3
HELIX 33 33 PRO C 297 ILE C 301 5 5
HELIX 34 34 GLN C 316 ILE C 320 5 5
HELIX 35 35 LEU C 326 GLY C 330 5 5
HELIX 36 36 ASN C 377 LYS C 382 1 6
HELIX 37 37 GLU C 394 HIS C 405 1 12
HELIX 38 38 THR C 417 ARG C 423 1 7
HELIX 39 39 THR C 424 ASN C 428 5 5
HELIX 40 40 ALA D 8 LEU D 16 1 9
HELIX 41 41 PRO D 17 GLY D 20 5 4
HELIX 42 42 ASP D 88 LYS D 91 5 4
HELIX 43 43 SER D 129 VAL D 133 5 5
HELIX 44 44 ASN D 139 LEU D 144 5 6
HELIX 45 45 ASN D 147 GLN D 149 5 3
HELIX 46 46 PRO D 297 ILE D 301 5 5
HELIX 47 47 GLN D 316 ILE D 320 5 5
HELIX 48 48 LEU D 326 GLY D 330 5 5
HELIX 49 49 ASN D 377 LYS D 382 1 6
HELIX 50 50 GLU D 394 HIS D 405 1 12
HELIX 51 51 THR D 417 ARG D 423 1 7
HELIX 52 52 THR D 424 ASN D 428 5 5
HELIX 53 53 ALA E 8 LEU E 16 1 9
HELIX 54 54 PRO E 17 GLY E 20 5 4
HELIX 55 55 ASP E 88 LYS E 91 5 4
HELIX 56 56 SER E 129 VAL E 133 5 5
HELIX 57 57 ASN E 139 LEU E 144 5 6
HELIX 58 58 ASN E 147 GLN E 149 5 3
HELIX 59 59 PRO E 297 ILE E 301 5 5
HELIX 60 60 GLN E 316 ILE E 320 5 5
HELIX 61 61 LEU E 326 GLY E 330 5 5
HELIX 62 62 ASN E 377 LYS E 382 1 6
HELIX 63 63 GLU E 394 HIS E 405 1 12
HELIX 64 64 THR E 417 ARG E 423 1 7
HELIX 65 65 THR E 424 ASN E 428 5 5
SHEET 1 A 4 ILE A 33 GLU A 44 0
SHEET 2 A 4 ILE A 363 PRO A 376 -1 O GLY A 368 N SER A 39
SHEET 3 A 4 PHE A 93 SER A 107 -1 N ILE A 99 O ASN A 371
SHEET 4 A 4 VAL A 175 ARG A 176 -1 O VAL A 175 N GLY A 96
SHEET 1 B 5 ILE A 33 GLU A 44 0
SHEET 2 B 5 ILE A 363 PRO A 376 -1 O GLY A 368 N SER A 39
SHEET 3 B 5 PHE A 93 SER A 107 -1 N ILE A 99 O ASN A 371
SHEET 4 B 5 VAL A 161 LEU A 164 -1 O VAL A 163 N TYR A 103
SHEET 5 B 5 VAL A 414 ARG A 416 -1 O TRP A 415 N THR A 162
SHEET 1 C 6 LEU A 77 GLU A 84 0
SHEET 2 C 6 ARG A 63 TRP A 70 -1 N ARG A 69 O GLU A 78
SHEET 3 C 6 GLY A 51 CYS A 55 -1 N VAL A 54 O ALA A 66
SHEET 4 C 6 ILE A 350 GLU A 356 -1 O VAL A 353 N LEU A 53
SHEET 5 C 6 THR A 120 PHE A 126 -1 N ASN A 122 O ALA A 354
SHEET 6 C 6 LYS A 151 LEU A 156 -1 O VAL A 152 N ALA A 123
SHEET 1 D 2 ASP A 179 GLU A 180 0
SHEET 2 D 2 ARG A 194 CYS A 195 -1 O CYS A 195 N ASP A 179
SHEET 1 E 4 ARG A 202 LEU A 208 0
SHEET 2 E 4 ALA A 332 SER A 338 -1 O VAL A 334 N ILE A 206
SHEET 3 E 4 THR A 236 LEU A 246 -1 N THR A 239 O SER A 335
SHEET 4 E 4 SER A 295 ILE A 296 -1 O ILE A 296 N THR A 236
SHEET 1 F 3 VAL A 288 MET A 292 0
SHEET 2 F 3 THR A 236 LEU A 246 -1 N PHE A 244 O VAL A 288
SHEET 3 F 3 ALA A 324 THR A 325 -1 O THR A 325 N SER A 245
SHEET 1 G 4 THR A 223 ILE A 232 0
SHEET 2 G 4 ILE A 305 LYS A 313 -1 O LEU A 310 N LEU A 225
SHEET 3 G 4 THR A 254 MET A 263 -1 N ASP A 261 O LYS A 309
SHEET 4 G 4 VAL A 272 ALA A 280 -1 O VAL A 274 N LEU A 260
SHEET 1 H 4 ILE B 33 GLU B 44 0
SHEET 2 H 4 ILE B 363 PRO B 376 -1 O GLY B 368 N SER B 39
SHEET 3 H 4 PHE B 93 SER B 107 -1 N ILE B 99 O ASN B 371
SHEET 4 H 4 VAL B 175 ARG B 176 -1 O VAL B 175 N GLY B 96
SHEET 1 I 5 ILE B 33 GLU B 44 0
SHEET 2 I 5 ILE B 363 PRO B 376 -1 O GLY B 368 N SER B 39
SHEET 3 I 5 PHE B 93 SER B 107 -1 N ILE B 99 O ASN B 371
SHEET 4 I 5 VAL B 161 LEU B 164 -1 O VAL B 163 N TYR B 103
SHEET 5 I 5 VAL B 414 ARG B 416 -1 O TRP B 415 N THR B 162
SHEET 1 J 6 LEU B 77 GLU B 84 0
SHEET 2 J 6 ARG B 63 TRP B 70 -1 N ARG B 69 O GLU B 78
SHEET 3 J 6 GLY B 51 CYS B 55 -1 N VAL B 54 O ALA B 66
SHEET 4 J 6 ILE B 350 GLU B 356 -1 O VAL B 353 N LEU B 53
SHEET 5 J 6 THR B 120 PHE B 126 -1 N ASN B 122 O ALA B 354
SHEET 6 J 6 LYS B 151 LEU B 156 -1 O VAL B 152 N ALA B 123
SHEET 1 K 2 ASP B 179 GLU B 180 0
SHEET 2 K 2 ARG B 194 CYS B 195 -1 O CYS B 195 N ASP B 179
SHEET 1 L 4 ARG B 202 LEU B 208 0
SHEET 2 L 4 ALA B 332 SER B 338 -1 O VAL B 334 N ILE B 206
SHEET 3 L 4 THR B 236 LEU B 246 -1 N THR B 239 O SER B 335
SHEET 4 L 4 SER B 295 ILE B 296 -1 O ILE B 296 N THR B 236
SHEET 1 M 3 VAL B 288 MET B 292 0
SHEET 2 M 3 THR B 236 LEU B 246 -1 N PHE B 244 O VAL B 288
SHEET 3 M 3 ALA B 324 THR B 325 -1 O THR B 325 N SER B 245
SHEET 1 N 4 THR B 223 ILE B 232 0
SHEET 2 N 4 ILE B 305 LYS B 313 -1 O LEU B 310 N LEU B 225
SHEET 3 N 4 THR B 254 MET B 263 -1 N ASP B 261 O LYS B 309
SHEET 4 N 4 VAL B 272 ALA B 280 -1 O VAL B 274 N LEU B 260
SHEET 1 O 4 ILE C 33 GLU C 44 0
SHEET 2 O 4 ILE C 363 PRO C 376 -1 O GLY C 368 N SER C 39
SHEET 3 O 4 PHE C 93 SER C 107 -1 N ILE C 99 O ASN C 371
SHEET 4 O 4 VAL C 175 ARG C 176 -1 O VAL C 175 N GLY C 96
SHEET 1 P 5 ILE C 33 GLU C 44 0
SHEET 2 P 5 ILE C 363 PRO C 376 -1 O GLY C 368 N SER C 39
SHEET 3 P 5 PHE C 93 SER C 107 -1 N ILE C 99 O ASN C 371
SHEET 4 P 5 VAL C 161 LEU C 164 -1 O VAL C 163 N TYR C 103
SHEET 5 P 5 VAL C 414 ARG C 416 -1 O TRP C 415 N THR C 162
SHEET 1 Q 6 LEU C 77 GLU C 84 0
SHEET 2 Q 6 ARG C 63 TRP C 70 -1 N ARG C 69 O GLU C 78
SHEET 3 Q 6 GLY C 51 CYS C 55 -1 N VAL C 54 O ALA C 66
SHEET 4 Q 6 ILE C 350 GLU C 356 -1 O THR C 351 N CYS C 55
SHEET 5 Q 6 THR C 120 PHE C 126 -1 N ASN C 122 O ALA C 354
SHEET 6 Q 6 LYS C 151 LEU C 156 -1 O VAL C 152 N ALA C 123
SHEET 1 R 2 ASP C 179 GLU C 180 0
SHEET 2 R 2 ARG C 194 CYS C 195 -1 O CYS C 195 N ASP C 179
SHEET 1 S 4 ARG C 202 LEU C 208 0
SHEET 2 S 4 ALA C 332 SER C 338 -1 O VAL C 334 N ILE C 206
SHEET 3 S 4 THR C 236 LEU C 246 -1 N THR C 239 O SER C 335
SHEET 4 S 4 SER C 295 ILE C 296 -1 O ILE C 296 N THR C 236
SHEET 1 T 3 VAL C 288 MET C 292 0
SHEET 2 T 3 THR C 236 LEU C 246 -1 N PHE C 244 O VAL C 288
SHEET 3 T 3 ALA C 324 THR C 325 -1 O THR C 325 N SER C 245
SHEET 1 U 4 THR C 223 ILE C 232 0
SHEET 2 U 4 ILE C 305 LYS C 313 -1 O LEU C 310 N LEU C 225
SHEET 3 U 4 THR C 254 MET C 263 -1 N ASP C 261 O LYS C 309
SHEET 4 U 4 VAL C 272 ALA C 280 -1 O VAL C 274 N LEU C 260
SHEET 1 V 4 ILE D 33 GLU D 44 0
SHEET 2 V 4 ILE D 363 PRO D 376 -1 O GLY D 368 N SER D 39
SHEET 3 V 4 PHE D 93 SER D 107 -1 N ILE D 99 O ASN D 371
SHEET 4 V 4 VAL D 175 ARG D 176 -1 O VAL D 175 N GLY D 96
SHEET 1 W 5 ILE D 33 GLU D 44 0
SHEET 2 W 5 ILE D 363 PRO D 376 -1 O GLY D 368 N SER D 39
SHEET 3 W 5 PHE D 93 SER D 107 -1 N ILE D 99 O ASN D 371
SHEET 4 W 5 VAL D 161 LEU D 164 -1 O VAL D 163 N TYR D 103
SHEET 5 W 5 VAL D 414 ARG D 416 -1 O TRP D 415 N THR D 162
SHEET 1 X 6 LEU D 77 GLU D 84 0
SHEET 2 X 6 ARG D 63 TRP D 70 -1 N ARG D 69 O GLU D 78
SHEET 3 X 6 GLY D 51 CYS D 55 -1 N VAL D 54 O ALA D 66
SHEET 4 X 6 ILE D 350 GLU D 356 -1 O VAL D 353 N LEU D 53
SHEET 5 X 6 THR D 120 PHE D 126 -1 N ASN D 122 O ALA D 354
SHEET 6 X 6 LYS D 151 LEU D 156 -1 O VAL D 152 N ALA D 123
SHEET 1 Y 2 ASP D 179 GLU D 180 0
SHEET 2 Y 2 ARG D 194 CYS D 195 -1 O CYS D 195 N ASP D 179
SHEET 1 Z 4 ARG D 202 LEU D 208 0
SHEET 2 Z 4 ALA D 332 SER D 338 -1 O VAL D 334 N ILE D 206
SHEET 3 Z 4 THR D 236 LEU D 246 -1 N THR D 239 O SER D 335
SHEET 4 Z 4 SER D 295 ILE D 296 -1 O ILE D 296 N THR D 236
SHEET 1 AA 3 VAL D 288 MET D 292 0
SHEET 2 AA 3 THR D 236 LEU D 246 -1 N PHE D 244 O VAL D 288
SHEET 3 AA 3 ALA D 324 THR D 325 -1 O THR D 325 N SER D 245
SHEET 1 AB 4 THR D 223 ILE D 232 0
SHEET 2 AB 4 ILE D 305 LYS D 313 -1 O LEU D 310 N LEU D 225
SHEET 3 AB 4 THR D 254 MET D 263 -1 N ASP D 261 O LYS D 309
SHEET 4 AB 4 VAL D 272 ALA D 280 -1 O VAL D 274 N LEU D 260
SHEET 1 AC 4 ILE E 33 GLU E 44 0
SHEET 2 AC 4 ILE E 363 PRO E 376 -1 O GLY E 368 N SER E 39
SHEET 3 AC 4 PHE E 93 SER E 107 -1 N ILE E 99 O ASN E 371
SHEET 4 AC 4 VAL E 175 ARG E 176 -1 O VAL E 175 N GLY E 96
SHEET 1 AD 5 ILE E 33 GLU E 44 0
SHEET 2 AD 5 ILE E 363 PRO E 376 -1 O GLY E 368 N SER E 39
SHEET 3 AD 5 PHE E 93 SER E 107 -1 N ILE E 99 O ASN E 371
SHEET 4 AD 5 VAL E 161 LEU E 164 -1 O VAL E 163 N TYR E 103
SHEET 5 AD 5 VAL E 414 ARG E 416 -1 O TRP E 415 N THR E 162
SHEET 1 AE 6 LEU E 77 GLU E 84 0
SHEET 2 AE 6 ARG E 63 TRP E 70 -1 N ARG E 69 O GLU E 78
SHEET 3 AE 6 GLY E 51 CYS E 55 -1 N VAL E 54 O ALA E 66
SHEET 4 AE 6 ILE E 350 GLU E 356 -1 O VAL E 353 N LEU E 53
SHEET 5 AE 6 THR E 120 PHE E 126 -1 N ASN E 122 O ALA E 354
SHEET 6 AE 6 LYS E 151 LEU E 156 -1 O VAL E 152 N ALA E 123
SHEET 1 AF 2 ASP E 179 GLU E 180 0
SHEET 2 AF 2 ARG E 194 CYS E 195 -1 O CYS E 195 N ASP E 179
SHEET 1 AG 4 ARG E 202 LEU E 208 0
SHEET 2 AG 4 ALA E 332 SER E 338 -1 O VAL E 334 N ILE E 206
SHEET 3 AG 4 THR E 236 LEU E 246 -1 N THR E 239 O SER E 335
SHEET 4 AG 4 SER E 295 ILE E 296 -1 O ILE E 296 N THR E 236
SHEET 1 AH 3 VAL E 288 MET E 292 0
SHEET 2 AH 3 THR E 236 LEU E 246 -1 N PHE E 244 O VAL E 288
SHEET 3 AH 3 ALA E 324 THR E 325 -1 O THR E 325 N SER E 245
SHEET 1 AI 4 THR E 223 ILE E 232 0
SHEET 2 AI 4 ILE E 305 LYS E 313 -1 O LEU E 310 N LEU E 225
SHEET 3 AI 4 THR E 254 MET E 263 -1 N ASP E 261 O LYS E 309
SHEET 4 AI 4 VAL E 272 ALA E 280 -1 O VAL E 274 N LEU E 260
LINK OD2 ASP A 27 CO CO A 443 1555 1555 2.15
LINK OD2 ASP B 27 CO CO A 443 1555 4566 2.11
LINK OD2 ASP C 27 CO CO C 443 1555 1555 2.12
LINK OD2 ASP D 27 CO CO A 443 1555 5555 2.11
LINK OD2 ASP E 27 CO CO E 443 1555 1555 2.16
CISPEP 1 ARG A 348 PRO A 349 0 -1.52
CISPEP 2 ARG B 348 PRO B 349 0 -1.67
CISPEP 3 ARG C 348 PRO C 349 0 -0.46
CISPEP 4 ARG D 348 PRO D 349 0 -0.96
CISPEP 5 ARG E 348 PRO E 349 0 -0.87
SITE 1 AC1 3 ASP A 27 ASP B 27 ASP D 27
SITE 1 AC2 3 ALA A 200 ALA B 200 ALA D 200
SITE 1 AC3 1 ASP C 27
SITE 1 AC4 1 ALA C 200
SITE 1 AC5 1 ASP E 27
SITE 1 AC6 1 ALA E 200
CRYST1 303.431 303.431 303.431 90.00 90.00 90.00 I 2 3 120
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 0.003296 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003296 0.00000
MTRIX1 1 0.810781 0.303649 -0.500432 58.60710 1
MTRIX2 1 0.308983 0.504104 0.806479 -94.00760 1
MTRIX3 1 0.497156 -0.808503 0.314896 150.99100 1
MTRIX1 2 0.501223 0.806866 -0.312639 0.36153 1
MTRIX2 2 0.812262 -0.314144 0.491471 1.83655 1
MTRIX3 2 0.298337 -0.500282 -0.812843 305.24799 1
MTRIX1 3 0.491694 0.814407 0.308185 -93.07320 1
MTRIX2 3 0.813667 -0.303659 -0.495719 149.92799 1
MTRIX3 3 -0.310134 0.494502 -0.811963 246.52100 1
MTRIX1 4 0.805853 0.312112 0.503177 -94.39900 1
MTRIX2 4 0.307898 0.504986 -0.806342 150.97200 1
MTRIX3 4 -0.505767 0.804720 0.310846 58.79010 1
(ATOM LINES ARE NOT SHOWN.)
END
