HEADER HYDROLASE/LIGASE 18-JAN-12 4DDI
TITLE CRYSTAL STRUCTURE OF HUMAN OTUB1/UBCH5B~UB/UB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D2, UBIQUITIN THIOESTERASE
COMPND 3 OTUB1;
COMPND 4 CHAIN: A, B, C;
COMPND 5 SYNONYM: UBIQUITIN CARRIER PROTEIN D2, UBIQUITIN-CONJUGATING ENZYME
COMPND 6 E2(17)KB 2, UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2, UBIQUITIN-
COMPND 7 PROTEIN LIGASE D2, DEUBIQUITINATING ENZYME OTUB1, OTU DOMAIN-
COMPND 8 CONTAINING UBIQUITIN ALDEHYDE-BINDING PROTEIN 1, OTUBAIN-1, HOTU1,
COMPND 9 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE OTUB1;
COMPND 10 EC: 6.3.2.19, 3.4.19.12;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: POLYUBIQUITIN-C;
COMPND 14 CHAIN: D, E, F, G, H, I;
COMPND 15 SYNONYM: UBIQUITIN;
COMPND 16 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: UBE2D2, UBC4, UBC5B, UBCH4, UBCH5B, HSPC263, OTB1, OTU1,
SOURCE 6 OTUB1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: UBC;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE-LIGASE COMPLEX, INHIBITION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.C.JUANG,M.SANCHES,F.SICHERI
REVDAT 4 15-NOV-17 4DDI 1 REMARK
REVDAT 3 02-AUG-17 4DDI 1 SOURCE
REVDAT 2 23-MAY-12 4DDI 1 ATOM HELIX REMARK SHEET
REVDAT 1 22-FEB-12 4DDI 0
JRNL AUTH Y.C.JUANG,M.C.LANDRY,M.SANCHES,V.VITTAL,C.C.LEUNG,
JRNL AUTH 2 D.F.CECCARELLI,A.R.MATEO,J.N.PRUNEDA,D.Y.MAO,R.K.SZILARD,
JRNL AUTH 3 S.ORLICKY,M.MUNRO,P.S.BRZOVIC,R.E.KLEVIT,F.SICHERI,
JRNL AUTH 4 D.DUROCHER
JRNL TITL OTUB1 CO-OPTS LYS48-LINKED UBIQUITIN RECOGNITION TO SUPPRESS
JRNL TITL 2 E2 ENZYME FUNCTION.
JRNL REF MOL.CELL V. 45 384 2012
JRNL REFN ISSN 1097-2765
JRNL PMID 22325355
JRNL DOI 10.1016/J.MOLCEL.2012.01.011
REMARK 2
REMARK 2 RESOLUTION. 3.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 3.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 19712
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 986
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 49.4732 - 7.2665 0.99 2762 146 0.1678 0.1965
REMARK 3 2 7.2665 - 5.7704 1.00 2764 145 0.2089 0.2501
REMARK 3 3 5.7704 - 5.0418 1.00 2733 144 0.2158 0.2908
REMARK 3 4 5.0418 - 4.5812 1.00 2731 144 0.2250 0.3199
REMARK 3 5 4.5812 - 4.2531 1.00 2712 143 0.2588 0.3455
REMARK 3 6 4.2531 - 4.0024 1.00 2733 144 0.2960 0.3410
REMARK 3 7 4.0024 - 3.8020 0.85 2291 120 0.3402 0.3927
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 155.3
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.530
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.190
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) : 22.77060
REMARK 3 B22 (A**2) : 9.21980
REMARK 3 B33 (A**2) : -31.99040
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 13.58380
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 13563
REMARK 3 ANGLE : 1.028 18330
REMARK 3 CHIRALITY : 0.081 2016
REMARK 3 PLANARITY : 0.005 2391
REMARK 3 DIHEDRAL : 17.971 5163
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ -1:150)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0875 -11.0008 70.1738
REMARK 3 T TENSOR
REMARK 3 T11: 0.9285 T22: 0.5974
REMARK 3 T33: 0.5572 T12: 0.1602
REMARK 3 T13: 0.0490 T23: 0.3220
REMARK 3 L TENSOR
REMARK 3 L11: 3.9572 L22: 5.4613
REMARK 3 L33: 3.7443 L12: 0.0973
REMARK 3 L13: 1.0845 L23: 0.8558
REMARK 3 S TENSOR
REMARK 3 S11: 0.2830 S12: 0.2453 S13: 0.2765
REMARK 3 S21: -0.1891 S22: 0.0553 S23: -0.1587
REMARK 3 S31: -0.7772 S32: -0.0030 S33: -0.2652
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8745 4.0386 32.0870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2020 T22: 0.4166
REMARK 3 T33: 0.3850 T12: 0.1573
REMARK 3 T13: -0.2558 T23: 0.1697
REMARK 3 L TENSOR
REMARK 3 L11: 4.0722 L22: 2.6677
REMARK 3 L33: 3.9602 L12: 0.0137
REMARK 3 L13: -0.6153 L23: -1.2380
REMARK 3 S TENSOR
REMARK 3 S11: -0.4629 S12: 0.1334 S13: 0.3119
REMARK 3 S21: -0.3465 S22: 0.0789 S23: -0.0587
REMARK 3 S31: 0.9169 S32: 0.2166 S33: 0.0148
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ -1:150)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1634 -13.6567 58.2366
REMARK 3 T TENSOR
REMARK 3 T11: 1.2561 T22: 1.6372
REMARK 3 T33: 0.8437 T12: 0.2137
REMARK 3 T13: -0.1458 T23: 0.2607
REMARK 3 L TENSOR
REMARK 3 L11: 4.2007 L22: 5.2664
REMARK 3 L33: 2.4180 L12: -0.5320
REMARK 3 L13: -1.1323 L23: -1.8716
REMARK 3 S TENSOR
REMARK 3 S11: 0.0883 S12: -0.2668 S13: -0.3572
REMARK 3 S21: 0.3455 S22: 0.1199 S23: 0.4611
REMARK 3 S31: 0.5766 S32: -0.8756 S33: -0.1697
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1025:1271)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.2267 10.6620 84.1217
REMARK 3 T TENSOR
REMARK 3 T11: 0.6554 T22: 1.0014
REMARK 3 T33: 2.3935 T12: 0.3693
REMARK 3 T13: 0.1353 T23: 0.7015
REMARK 3 L TENSOR
REMARK 3 L11: 2.3296 L22: 2.0836
REMARK 3 L33: 3.2235 L12: 0.1323
REMARK 3 L13: 1.2493 L23: 0.3710
REMARK 3 S TENSOR
REMARK 3 S11: -0.1715 S12: 0.7135 S13: 1.5038
REMARK 3 S21: -0.2393 S22: -0.3083 S23: 1.0247
REMARK 3 S31: 0.0542 S32: -0.2737 S33: -0.0430
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ -1:150)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0083 44.1816 24.5630
REMARK 3 T TENSOR
REMARK 3 T11: 0.5834 T22: 0.4150
REMARK 3 T33: 0.8782 T12: -0.0789
REMARK 3 T13: 0.0152 T23: -0.1599
REMARK 3 L TENSOR
REMARK 3 L11: 4.1275 L22: 4.9311
REMARK 3 L33: 3.3807 L12: 1.4326
REMARK 3 L13: -0.1678 L23: -0.7807
REMARK 3 S TENSOR
REMARK 3 S11: 0.0481 S12: -0.8178 S13: 0.3728
REMARK 3 S21: -0.1515 S22: -0.2423 S23: 0.0526
REMARK 3 S31: -0.0764 S32: 0.0578 S33: 0.1738
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 1025:1271)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2740 66.7527 20.5718
REMARK 3 T TENSOR
REMARK 3 T11: 1.8587 T22: 1.1026
REMARK 3 T33: 1.2795 T12: 0.7274
REMARK 3 T13: 0.6853 T23: 0.3597
REMARK 3 L TENSOR
REMARK 3 L11: 2.2127 L22: 0.5687
REMARK 3 L33: 1.9965 L12: 0.1715
REMARK 3 L13: 0.5261 L23: -0.9751
REMARK 3 S TENSOR
REMARK 3 S11: 0.5256 S12: 0.1257 S13: 1.1553
REMARK 3 S21: 0.6381 S22: 0.1534 S23: 0.3063
REMARK 3 S31: -1.8781 S32: -0.8409 S33: -0.3552
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 1:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0514 -16.8521 14.8154
REMARK 3 T TENSOR
REMARK 3 T11: 2.2664 T22: 1.9648
REMARK 3 T33: 1.1977 T12: -0.3024
REMARK 3 T13: -0.1299 T23: -0.3748
REMARK 3 L TENSOR
REMARK 3 L11: 3.3904 L22: 3.2725
REMARK 3 L33: 2.1750 L12: 0.5012
REMARK 3 L13: -0.4062 L23: 1.7634
REMARK 3 S TENSOR
REMARK 3 S11: -0.3418 S12: 2.0230 S13: -1.8667
REMARK 3 S21: -1.0753 S22: 0.2045 S23: 0.0375
REMARK 3 S31: 1.2997 S32: -0.8008 S33: -0.2015
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 1:76)
REMARK 3 ORIGIN FOR THE GROUP (A): -47.3351 -6.9174 98.5143
REMARK 3 T TENSOR
REMARK 3 T11: 1.4062 T22: 1.5643
REMARK 3 T33: 1.4817 T12: -0.3453
REMARK 3 T13: 0.4951 T23: -0.1360
REMARK 3 L TENSOR
REMARK 3 L11: 2.6707 L22: 3.1051
REMARK 3 L33: 2.8074 L12: 0.5235
REMARK 3 L13: 0.3676 L23: -1.6511
REMARK 3 S TENSOR
REMARK 3 S11: 1.2881 S12: -0.7525 S13: 1.1601
REMARK 3 S21: 1.1340 S22: -0.9034 S23: 1.6223
REMARK 3 S31: -0.2140 S32: -0.5710 S33: -0.4722
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 1:76)
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4196 48.9156 10.7962
REMARK 3 T TENSOR
REMARK 3 T11: 0.8954 T22: 1.7274
REMARK 3 T33: 0.8722 T12: 0.6206
REMARK 3 T13: 0.3242 T23: 0.4183
REMARK 3 L TENSOR
REMARK 3 L11: 3.4361 L22: 3.4857
REMARK 3 L33: 1.9305 L12: 1.3753
REMARK 3 L13: 0.2893 L23: 0.1051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 1.0061 S13: -0.2894
REMARK 3 S21: 0.0262 S22: 0.3413 S23: 0.2199
REMARK 3 S31: 0.0390 S32: -0.7573 S33: -0.2360
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'G' AND (RESSEQ 1:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6837 -15.0042 39.6103
REMARK 3 T TENSOR
REMARK 3 T11: 1.0899 T22: 0.7694
REMARK 3 T33: 0.6204 T12: 0.3222
REMARK 3 T13: 0.0823 T23: 0.2218
REMARK 3 L TENSOR
REMARK 3 L11: 3.0570 L22: 2.9482
REMARK 3 L33: 5.1388 L12: 0.1536
REMARK 3 L13: 0.5061 L23: -1.5820
REMARK 3 S TENSOR
REMARK 3 S11: -0.5859 S12: -0.4676 S13: -0.5233
REMARK 3 S21: -0.9925 S22: -0.1986 S23: -0.4842
REMARK 3 S31: 1.9611 S32: 0.8702 S33: 0.6232
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 1:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8192 41.5794 40.6735
REMARK 3 T TENSOR
REMARK 3 T11: 1.4300 T22: 1.9700
REMARK 3 T33: 1.6947 T12: -0.2118
REMARK 3 T13: 0.0506 T23: -0.4703
REMARK 3 L TENSOR
REMARK 3 L11: 3.9179 L22: 4.4405
REMARK 3 L33: 2.6192 L12: 1.1877
REMARK 3 L13: -1.8116 L23: -0.6283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: -1.4583 S13: 0.0257
REMARK 3 S21: 0.2598 S22: -0.7359 S23: -0.0326
REMARK 3 S31: 0.1164 S32: -0.7434 S33: 0.7094
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'I' AND (RESSEQ 1:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6009 -5.2315 105.5792
REMARK 3 T TENSOR
REMARK 3 T11: 0.4002 T22: 1.0255
REMARK 3 T33: 0.7192 T12: 0.0437
REMARK 3 T13: 0.1040 T23: -0.2995
REMARK 3 L TENSOR
REMARK 3 L11: 5.0990 L22: 4.2773
REMARK 3 L33: 4.4269 L12: 0.9481
REMARK 3 L13: 1.2624 L23: -0.7665
REMARK 3 S TENSOR
REMARK 3 S11: 0.6993 S12: -0.9880 S13: 0.4392
REMARK 3 S21: 0.4052 S22: 0.2720 S23: 0.1898
REMARK 3 S31: -0.7049 S32: 0.4136 S33: -0.6671
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 4
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'D'
REMARK 3 SELECTION : CHAIN 'E'
REMARK 3 ATOM PAIRS NUMBER : 601
REMARK 3 RMSD : 0.002
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'D'
REMARK 3 SELECTION : CHAIN 'F'
REMARK 3 ATOM PAIRS NUMBER : 601
REMARK 3 RMSD : 0.002
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 1:150 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1191
REMARK 3 RMSD : 0.002
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'C' AND (RESSEQ 1:150 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1191
REMARK 3 RMSD : 0.002
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND
REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 1025:1271 ) AND
REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 2026
REMARK 3 RMSD : 0.001
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND
REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN 'C' AND (RESSEQ 1025:1271 ) AND
REMARK 3 (NOT ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 2026
REMARK 3 RMSD : 0.002
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'G'
REMARK 3 SELECTION : CHAIN 'H'
REMARK 3 ATOM PAIRS NUMBER : 601
REMARK 3 RMSD : 0.001
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'G'
REMARK 3 SELECTION : CHAIN 'I'
REMARK 3 ATOM PAIRS NUMBER : 601
REMARK 3 RMSD : 0.001
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4DDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070192.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97922
REMARK 200 MONOCHROMATOR : SI (220), SI (311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19737
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.796
REMARK 200 RESOLUTION RANGE LOW (A) : 49.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG1500, 0.1 M SPG, PH 8.0, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 86.86950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.11250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 86.86950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 53.11250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: THERE ARE THREE BIOLOGICAL COMPLEXES PER
REMARK 300 ASYMMETRIC UNIT. THE BIOLOGICAL COMPLEX DEFINED BY THE
REMARK 300 AUTHOR CONSISTS OF
REMARK 300 COMPLEX 1: CHAIN H, CHAIN E, RESIDUES 1 TO 147 OF CHAIN C,
REMARK 300 AND RESIDUES 1025-1071 OF CHAIN B;
REMARK 300 COMPLEX 2: CHAIN G, CHAIN D, RESIDUES 1 TO 147 OF CHAIN B,
REMARK 300 AND RESIDUES 1025-1271 OF CHAIN A;
REMARK 300 COMPLEX 3: CHAIN I, CHAIN F, RESIDUES 1 TO 147 OF CHAIN A,
REMARK 300 AND RESIDUES 1025-1271 OF CHAIN C;
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER C 150 N TYR C 1026 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 61 52.79 -98.01
REMARK 500 ARG A 90 -79.34 -124.85
REMARK 500 PRO A 113 -178.58 -68.42
REMARK 500 ASP A 117 67.02 -119.96
REMARK 500 THR A 129 -74.99 -109.78
REMARK 500 SER A 150 -75.00 -16.19
REMARK 500 ALA A1025 -53.28 -15.81
REMARK 500 SER A1187 -36.84 -39.19
REMARK 500 GLU A1191 -37.91 -38.70
REMARK 500 VAL A1208 -58.13 -127.58
REMARK 500 ASP A1237 -92.45 -125.69
REMARK 500 PRO B 61 52.71 -97.91
REMARK 500 ARG B 90 -79.30 -124.83
REMARK 500 PRO B 113 -178.58 -68.44
REMARK 500 ASP B 117 66.94 -119.90
REMARK 500 THR B 129 -74.97 -109.79
REMARK 500 SER B 150 -89.46 4.63
REMARK 500 ALA B1025 -48.39 -19.01
REMARK 500 SER B1187 -36.85 -39.16
REMARK 500 GLU B1191 -37.64 -38.85
REMARK 500 VAL B1208 -58.25 -127.61
REMARK 500 ASP B1237 -92.48 -125.66
REMARK 500 PRO C 61 52.82 -97.93
REMARK 500 ARG C 90 -79.29 -124.93
REMARK 500 PRO C 113 -178.60 -68.47
REMARK 500 ASP C 117 66.96 -119.91
REMARK 500 THR C 129 -74.94 -109.72
REMARK 500 SER C 150 -95.68 -13.29
REMARK 500 ALA C1025 -65.01 1.99
REMARK 500 SER C1187 -36.82 -39.21
REMARK 500 GLU C1191 -37.67 -38.92
REMARK 500 VAL C1208 -58.24 -127.55
REMARK 500 ASP C1237 -92.43 -125.73
REMARK 500 ALA D 46 64.09 39.64
REMARK 500 ASN D 60 -3.17 65.36
REMARK 500 ILE D 61 70.95 32.36
REMARK 500 GLU D 64 -55.75 -147.96
REMARK 500 SER D 65 -179.10 -68.29
REMARK 500 ALA E 46 64.07 39.62
REMARK 500 ASN E 60 -7.24 67.93
REMARK 500 ILE E 61 55.00 31.31
REMARK 500 GLU E 64 -55.77 -148.02
REMARK 500 SER E 65 -179.12 -68.33
REMARK 500 ALA F 46 64.03 39.64
REMARK 500 ASN F 60 -7.24 67.92
REMARK 500 ILE F 61 55.19 30.88
REMARK 500 GLU F 64 -55.73 -147.99
REMARK 500 SER F 65 -179.13 -68.32
REMARK 500 LYS G 33 -67.17 -98.94
REMARK 500 LYS H 33 -66.94 -99.00
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN D 60 ILE D 61 106.31
REMARK 500 ASN E 60 ILE E 61 111.78
REMARK 500 ASN F 60 ILE F 61 112.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DDG RELATED DB: PDB
DBREF 4DDI A 1 147 UNP P62837 UB2D2_HUMAN 1 147
DBREF 4DDI A 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271
DBREF 4DDI B 1 147 UNP P62837 UB2D2_HUMAN 1 147
DBREF 4DDI B 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271
DBREF 4DDI C 1 147 UNP P62837 UB2D2_HUMAN 1 147
DBREF 4DDI C 1025 1271 UNP Q96FW1 OTUB1_HUMAN 25 271
DBREF 4DDI D 1 76 UNP P0CG48 UBC_HUMAN 1 76
DBREF 4DDI E 1 76 UNP P0CG48 UBC_HUMAN 1 76
DBREF 4DDI F 1 76 UNP P0CG48 UBC_HUMAN 1 76
DBREF 4DDI G 1 76 UNP P0CG48 UBC_HUMAN 1 76
DBREF 4DDI H 1 76 UNP P0CG48 UBC_HUMAN 1 76
DBREF 4DDI I 1 76 UNP P0CG48 UBC_HUMAN 1 76
SEQADV 4DDI GLY A -1 UNP P62837 EXPRESSION TAG
SEQADV 4DDI ALA A 0 UNP P62837 EXPRESSION TAG
SEQADV 4DDI SER A 85 UNP P62837 CYS 85 CONFLICT
SEQADV 4DDI GLY A 148 UNP Q96FW1 LINKER
SEQADV 4DDI GLY A 149 UNP Q96FW1 LINKER
SEQADV 4DDI SER A 150 UNP Q96FW1 LINKER
SEQADV 4DDI SER A 1091 UNP Q96FW1 CYS 91 CONFLICT
SEQADV 4DDI GLY B -1 UNP P62837 EXPRESSION TAG
SEQADV 4DDI ALA B 0 UNP P62837 EXPRESSION TAG
SEQADV 4DDI SER B 85 UNP P62837 CYS 85 CONFLICT
SEQADV 4DDI GLY B 148 UNP Q96FW1 LINKER
SEQADV 4DDI GLY B 149 UNP Q96FW1 LINKER
SEQADV 4DDI SER B 150 UNP Q96FW1 LINKER
SEQADV 4DDI SER B 1091 UNP Q96FW1 CYS 91 CONFLICT
SEQADV 4DDI GLY C -1 UNP P62837 EXPRESSION TAG
SEQADV 4DDI ALA C 0 UNP P62837 EXPRESSION TAG
SEQADV 4DDI SER C 85 UNP P62837 CYS 85 CONFLICT
SEQADV 4DDI GLY C 148 UNP Q96FW1 LINKER
SEQADV 4DDI GLY C 149 UNP Q96FW1 LINKER
SEQADV 4DDI SER C 150 UNP Q96FW1 LINKER
SEQADV 4DDI SER C 1091 UNP Q96FW1 CYS 91 CONFLICT
SEQRES 1 A 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN
SEQRES 2 A 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY
SEQRES 3 A 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE
SEQRES 4 A 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE
SEQRES 5 A 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS
SEQRES 6 A 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO
SEQRES 7 A 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU
SEQRES 8 A 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL
SEQRES 9 A 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO
SEQRES 10 A 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS
SEQRES 11 A 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP
SEQRES 12 A 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU
SEQRES 13 A 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE
SEQRES 14 A 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU
SEQRES 15 A 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE
SEQRES 16 A 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER
SEQRES 17 A 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR
SEQRES 18 A 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP
SEQRES 19 A 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA
SEQRES 20 A 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU
SEQRES 21 A 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU
SEQRES 22 A 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU
SEQRES 23 A 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU
SEQRES 24 A 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN
SEQRES 25 A 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY
SEQRES 26 A 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO
SEQRES 27 A 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU
SEQRES 28 A 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET
SEQRES 29 A 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE
SEQRES 30 A 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG
SEQRES 31 A 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS
SEQRES 1 B 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN
SEQRES 2 B 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY
SEQRES 3 B 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE
SEQRES 4 B 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE
SEQRES 5 B 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS
SEQRES 6 B 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO
SEQRES 7 B 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU
SEQRES 8 B 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL
SEQRES 9 B 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO
SEQRES 10 B 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS
SEQRES 11 B 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP
SEQRES 12 B 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU
SEQRES 13 B 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE
SEQRES 14 B 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU
SEQRES 15 B 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE
SEQRES 16 B 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER
SEQRES 17 B 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR
SEQRES 18 B 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP
SEQRES 19 B 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA
SEQRES 20 B 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU
SEQRES 21 B 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU
SEQRES 22 B 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU
SEQRES 23 B 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU
SEQRES 24 B 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN
SEQRES 25 B 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY
SEQRES 26 B 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO
SEQRES 27 B 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU
SEQRES 28 B 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET
SEQRES 29 B 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE
SEQRES 30 B 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG
SEQRES 31 B 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS
SEQRES 1 C 399 GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN
SEQRES 2 C 399 ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY
SEQRES 3 C 399 PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE
SEQRES 4 C 399 MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE
SEQRES 5 C 399 PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS
SEQRES 6 C 399 PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO
SEQRES 7 C 399 ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU
SEQRES 8 C 399 ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL
SEQRES 9 C 399 LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO
SEQRES 10 C 399 ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS
SEQRES 11 C 399 THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP
SEQRES 12 C 399 THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU
SEQRES 13 C 399 ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE
SEQRES 14 C 399 ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU
SEQRES 15 C 399 SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE
SEQRES 16 C 399 TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER
SEQRES 17 C 399 TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR
SEQRES 18 C 399 ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP
SEQRES 19 C 399 ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA
SEQRES 20 C 399 LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU
SEQRES 21 C 399 PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU
SEQRES 22 C 399 ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU
SEQRES 23 C 399 LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU
SEQRES 24 C 399 VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN
SEQRES 25 C 399 ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY
SEQRES 26 C 399 ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO
SEQRES 27 C 399 MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU
SEQRES 28 C 399 ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET
SEQRES 29 C 399 ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE
SEQRES 30 C 399 PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG
SEQRES 31 C 399 PRO GLY HIS TYR ASP ILE LEU TYR LYS
SEQRES 1 D 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 E 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 E 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 E 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 E 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 E 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 E 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 F 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 F 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 F 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 F 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 F 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 F 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 G 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 G 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 G 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 G 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 G 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 G 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 H 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 H 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 H 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 H 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 H 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 H 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 I 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 I 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 I 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 I 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 I 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 I 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HELIX 1 1 GLY A -1 ASP A 16 1 18
HELIX 2 2 THR A 98 ASP A 112 1 15
HELIX 3 3 VAL A 120 THR A 129 1 10
HELIX 4 4 ASP A 130 ALA A 146 1 17
HELIX 5 5 ALA A 1025 ASN A 1045 1 21
HELIX 6 6 VAL A 1056 TYR A 1061 1 6
HELIX 7 7 ASP A 1065 TYR A 1079 1 15
HELIX 8 8 ASN A 1090 LEU A 1104 1 15
HELIX 9 9 ASP A 1107 SER A 1127 1 21
HELIX 10 10 THR A 1131 LYS A 1151 1 21
HELIX 11 11 SER A 1154 ASN A 1163 1 10
HELIX 12 12 ASP A 1164 GLU A 1186 1 23
HELIX 13 13 GLU A 1186 GLU A 1191 1 6
HELIX 14 14 HIS A 1192 ILE A 1194 5 3
HELIX 15 15 THR A 1199 VAL A 1208 1 10
HELIX 16 16 ASP A 1216 SER A 1228 1 13
HELIX 17 17 ALA B 0 ASP B 16 1 17
HELIX 18 18 THR B 98 ASP B 112 1 15
HELIX 19 19 VAL B 120 THR B 129 1 10
HELIX 20 20 ASP B 130 ALA B 146 1 17
HELIX 21 21 GLY B 148 SER B 150 5 3
HELIX 22 22 ALA B 1025 ASN B 1045 1 21
HELIX 23 23 VAL B 1056 TYR B 1061 1 6
HELIX 24 24 ASP B 1065 TYR B 1079 1 15
HELIX 25 25 ASN B 1090 LEU B 1104 1 15
HELIX 26 26 ASP B 1107 SER B 1127 1 21
HELIX 27 27 THR B 1131 LYS B 1151 1 21
HELIX 28 28 SER B 1154 ASN B 1163 1 10
HELIX 29 29 ASP B 1164 GLU B 1186 1 23
HELIX 30 30 GLU B 1186 GLU B 1191 1 6
HELIX 31 31 HIS B 1192 ILE B 1194 5 3
HELIX 32 32 THR B 1199 VAL B 1208 1 10
HELIX 33 33 ASP B 1216 SER B 1228 1 13
HELIX 34 34 ALA C 0 ASP C 16 1 17
HELIX 35 35 THR C 98 ASP C 112 1 15
HELIX 36 36 VAL C 120 THR C 129 1 10
HELIX 37 37 ASP C 130 ALA C 146 1 17
HELIX 38 38 ALA C 1025 ASN C 1045 1 21
HELIX 39 39 VAL C 1056 TYR C 1061 1 6
HELIX 40 40 ASP C 1065 TYR C 1079 1 15
HELIX 41 41 ASN C 1090 LEU C 1104 1 15
HELIX 42 42 ASP C 1107 SER C 1127 1 21
HELIX 43 43 THR C 1131 LYS C 1151 1 21
HELIX 44 44 SER C 1154 ASN C 1163 1 10
HELIX 45 45 ASP C 1164 GLU C 1186 1 23
HELIX 46 46 GLU C 1186 GLU C 1191 1 6
HELIX 47 47 HIS C 1192 ILE C 1194 5 3
HELIX 48 48 THR C 1199 VAL C 1208 1 10
HELIX 49 49 ASP C 1216 SER C 1228 1 13
HELIX 50 50 ILE D 23 GLU D 34 1 12
HELIX 51 51 PRO D 37 ASP D 39 5 3
HELIX 52 52 THR D 55 ASN D 60 1 6
HELIX 53 53 ILE E 23 GLU E 34 1 12
HELIX 54 54 PRO E 37 ASP E 39 5 3
HELIX 55 55 THR E 55 ASN E 60 1 6
HELIX 56 56 ILE F 23 GLU F 34 1 12
HELIX 57 57 PRO F 37 ASP F 39 5 3
HELIX 58 58 THR F 55 ASN F 60 1 6
HELIX 59 59 THR G 22 ASP G 32 1 11
HELIX 60 60 THR G 55 ASN G 60 1 6
HELIX 61 61 THR H 22 ASP H 32 1 11
HELIX 62 62 THR H 55 ASN H 60 1 6
HELIX 63 63 THR I 22 ASP I 32 1 11
HELIX 64 64 THR I 55 ASN I 60 1 6
SHEET 1 A 4 CYS A 21 VAL A 26 0
SHEET 2 A 4 ASP A 29 MET A 38 -1 O GLN A 34 N GLY A 24
SHEET 3 A 4 VAL A 49 HIS A 55 -1 O LEU A 52 N ALA A 35
SHEET 4 A 4 LYS A 66 PHE A 69 -1 O LYS A 66 N HIS A 55
SHEET 1 B 6 LEU A1052 GLU A1053 0
SHEET 2 B 6 TYR A1081 ARG A1083 -1 O ILE A1082 N LEU A1052
SHEET 3 B 6 HIS A1265 TYR A1270 -1 O ILE A1268 N ARG A1083
SHEET 4 B 6 TYR A1258 ARG A1262 -1 N LEU A1260 O ASP A1267
SHEET 5 B 6 ILE A1231 TYR A1235 1 N GLU A1234 O TYR A1261
SHEET 6 B 6 ASN A1245 PHE A1249 -1 O ASN A1245 N TYR A1235
SHEET 1 C 4 CYS B 21 VAL B 26 0
SHEET 2 C 4 ASP B 29 MET B 38 -1 O GLN B 34 N GLY B 24
SHEET 3 C 4 VAL B 49 HIS B 55 -1 O LEU B 52 N ALA B 35
SHEET 4 C 4 LYS B 66 PHE B 69 -1 O LYS B 66 N HIS B 55
SHEET 1 D 6 LEU B1052 GLU B1053 0
SHEET 2 D 6 TYR B1081 ARG B1083 -1 O ILE B1082 N LEU B1052
SHEET 3 D 6 HIS B1265 TYR B1270 -1 O ILE B1268 N ARG B1083
SHEET 4 D 6 TYR B1258 ARG B1262 -1 N LEU B1260 O ASP B1267
SHEET 5 D 6 ILE B1231 TYR B1235 1 N GLU B1234 O TYR B1261
SHEET 6 D 6 ASN B1245 PHE B1249 -1 O ASN B1245 N TYR B1235
SHEET 1 E 4 CYS C 21 VAL C 26 0
SHEET 2 E 4 ASP C 29 MET C 38 -1 O GLN C 34 N GLY C 24
SHEET 3 E 4 VAL C 49 HIS C 55 -1 O LEU C 52 N ALA C 35
SHEET 4 E 4 LYS C 66 PHE C 69 -1 O LYS C 66 N HIS C 55
SHEET 1 F 6 LEU C1052 GLU C1053 0
SHEET 2 F 6 TYR C1081 ARG C1083 -1 O ILE C1082 N LEU C1052
SHEET 3 F 6 HIS C1265 TYR C1270 -1 O ILE C1268 N ARG C1083
SHEET 4 F 6 TYR C1258 ARG C1262 -1 N LEU C1260 O ASP C1267
SHEET 5 F 6 ILE C1231 TYR C1235 1 N GLU C1234 O TYR C1261
SHEET 6 F 6 ASN C1245 PHE C1249 -1 O ASN C1245 N TYR C1235
SHEET 1 G 5 LYS D 11 LEU D 15 0
SHEET 2 G 5 ILE D 3 THR D 7 -1 N VAL D 5 O ILE D 13
SHEET 3 G 5 THR D 66 LEU D 71 1 O LEU D 69 N LYS D 6
SHEET 4 G 5 GLN D 41 PHE D 45 -1 N ARG D 42 O VAL D 70
SHEET 5 G 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
SHEET 1 H 5 LYS E 11 LEU E 15 0
SHEET 2 H 5 ILE E 3 THR E 7 -1 N VAL E 5 O ILE E 13
SHEET 3 H 5 THR E 66 LEU E 71 1 O LEU E 69 N LYS E 6
SHEET 4 H 5 GLN E 41 PHE E 45 -1 N ARG E 42 O VAL E 70
SHEET 5 H 5 LYS E 48 GLN E 49 -1 O LYS E 48 N PHE E 45
SHEET 1 I 5 LYS F 11 LEU F 15 0
SHEET 2 I 5 ILE F 3 THR F 7 -1 N VAL F 5 O ILE F 13
SHEET 3 I 5 THR F 66 LEU F 71 1 O LEU F 69 N LYS F 6
SHEET 4 I 5 GLN F 41 PHE F 45 -1 N ARG F 42 O VAL F 70
SHEET 5 I 5 LYS F 48 GLN F 49 -1 O LYS F 48 N PHE F 45
SHEET 1 J 5 THR G 12 GLU G 16 0
SHEET 2 J 5 GLN G 2 LYS G 6 -1 N VAL G 5 O ILE G 13
SHEET 3 J 5 THR G 66 LEU G 71 1 O LEU G 67 N LYS G 6
SHEET 4 J 5 GLN G 41 PHE G 45 -1 N ILE G 44 O HIS G 68
SHEET 5 J 5 LYS G 48 GLN G 49 -1 O LYS G 48 N PHE G 45
SHEET 1 K 5 THR H 12 GLU H 16 0
SHEET 2 K 5 GLN H 2 LYS H 6 -1 N VAL H 5 O ILE H 13
SHEET 3 K 5 THR H 66 LEU H 71 1 O LEU H 67 N LYS H 6
SHEET 4 K 5 GLN H 41 PHE H 45 -1 N ILE H 44 O HIS H 68
SHEET 5 K 5 LYS H 48 GLN H 49 -1 O LYS H 48 N PHE H 45
SHEET 1 L 5 THR I 12 GLU I 16 0
SHEET 2 L 5 GLN I 2 LYS I 6 -1 N VAL I 5 O ILE I 13
SHEET 3 L 5 THR I 66 LEU I 71 1 O LEU I 67 N LYS I 6
SHEET 4 L 5 GLN I 41 PHE I 45 -1 N ILE I 44 O HIS I 68
SHEET 5 L 5 LYS I 48 GLN I 49 -1 O LYS I 48 N PHE I 45
SSBOND 1 CYS A 21 CYS A 107 1555 1555 2.03
SSBOND 2 CYS B 21 CYS B 107 1555 1555 2.03
SSBOND 3 CYS C 21 CYS C 107 1555 1555 2.03
CISPEP 1 TYR A 60 PRO A 61 0 -18.78
CISPEP 2 PHE A 1249 PRO A 1250 0 -17.22
CISPEP 3 TYR B 60 PRO B 61 0 -18.83
CISPEP 4 PHE B 1249 PRO B 1250 0 -17.23
CISPEP 5 TYR C 60 PRO C 61 0 -18.82
CISPEP 6 PHE C 1249 PRO C 1250 0 -17.09
CRYST1 173.739 106.225 134.689 90.00 123.74 90.00 C 1 2 1 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 0.005756 0.000000 0.003844 0.00000
SCALE2 0.000000 0.009414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008928 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
