HEADER APOPTOSIS, HYDROLASE/HYDROLASE INHIBITOR20-MAR-13 4JR2
TITLE HUMAN PROCASPASE-7/CASPASE-7 HETERODIMER BOUND TO AC-DEVD-CMK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROCASPASE-7;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PROTEASE DOMAIN (UNP RESIDUES 57-303);
COMPND 5 SYNONYM: CASP-7, APOPTOTIC PROTEASE MCH-3, CMH-1, ICE-LIKE APOPTOTIC
COMPND 6 PROTEASE 3, ICE-LAP3, CASPASE-7;
COMPND 7 EC: 3.4.22.60;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: AC-DEVD-CMK;
COMPND 12 CHAIN: C, D;
COMPND 13 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: CASP7, MCH3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: ADDGENE PLASMID 29653;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS PROTEASE, PROENZYME, PROTEIN-PEPTIDE COMPLEX, IRREVERSIBLE INHIBITOR,
KEYWDS 2 ACTIVITY BASED PROBE, CASPASE, APOPTOSIS, HYDROLASE-HYDROLASE
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.D.THOMSEN,J.A.WELLS
REVDAT 6 20-SEP-23 4JR2 1 REMARK SEQADV LINK
REVDAT 5 15-NOV-17 4JR2 1 REMARK
REVDAT 4 12-JUN-13 4JR2 1 REMARK
REVDAT 3 05-JUN-13 4JR2 1 JRNL
REVDAT 2 22-MAY-13 4JR2 1 JRNL
REVDAT 1 08-MAY-13 4JR2 0
JRNL AUTH N.D.THOMSEN,J.T.KOERBER,J.A.WELLS
JRNL TITL STRUCTURAL SNAPSHOTS REVEAL DISTINCT MECHANISMS OF
JRNL TITL 2 PROCASPASE-3 AND -7 ACTIVATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 8477 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23650375
JRNL DOI 10.1073/PNAS.1306759110
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 55899
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2819
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 32.8737 - 4.4754 0.99 2828 156 0.1654 0.1926
REMARK 3 2 4.4754 - 3.5536 0.99 2721 140 0.1307 0.1632
REMARK 3 3 3.5536 - 3.1048 0.99 2724 129 0.1484 0.1862
REMARK 3 4 3.1048 - 2.8211 0.99 2650 162 0.1673 0.1828
REMARK 3 5 2.8211 - 2.6190 0.99 2652 144 0.1719 0.1813
REMARK 3 6 2.6190 - 2.4646 1.00 2659 153 0.1581 0.2096
REMARK 3 7 2.4646 - 2.3412 1.00 2660 138 0.1520 0.1915
REMARK 3 8 2.3412 - 2.2393 1.00 2656 161 0.1549 0.1900
REMARK 3 9 2.2393 - 2.1531 1.00 2648 145 0.1508 0.2032
REMARK 3 10 2.1531 - 2.0789 1.00 2651 144 0.1543 0.2038
REMARK 3 11 2.0789 - 2.0139 1.00 2636 141 0.1579 0.2386
REMARK 3 12 2.0139 - 1.9563 1.00 2651 160 0.1652 0.1922
REMARK 3 13 1.9563 - 1.9048 0.99 2627 123 0.1749 0.2458
REMARK 3 14 1.9048 - 1.8583 0.99 2625 144 0.1787 0.1937
REMARK 3 15 1.8583 - 1.8161 0.99 2632 124 0.1851 0.2065
REMARK 3 16 1.8161 - 1.7775 0.99 2617 132 0.1923 0.2470
REMARK 3 17 1.7775 - 1.7419 0.99 2633 119 0.2029 0.2358
REMARK 3 18 1.7419 - 1.7090 0.99 2619 120 0.2097 0.2799
REMARK 3 19 1.7090 - 1.6785 0.99 2611 156 0.2245 0.2530
REMARK 3 20 1.6785 - 1.6500 0.98 2580 128 0.2381 0.2994
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.007 4027
REMARK 3 ANGLE : 1.104 5467
REMARK 3 CHIRALITY : 0.082 595
REMARK 3 PLANARITY : 0.005 712
REMARK 3 DIHEDRAL : 13.345 1562
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESSEQ 56:63
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9903 -8.3419 -34.3665
REMARK 3 T TENSOR
REMARK 3 T11: 0.3741 T22: 0.3177
REMARK 3 T33: 0.1926 T12: 0.1559
REMARK 3 T13: 0.0308 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.5529 L22: 0.6864
REMARK 3 L33: 0.2326 L12: 0.9568
REMARK 3 L13: 0.4023 L23: 0.1531
REMARK 3 S TENSOR
REMARK 3 S11: 0.1680 S12: 0.6854 S13: -0.3481
REMARK 3 S21: -0.7690 S22: -0.2194 S23: -0.5058
REMARK 3 S31: 0.8591 S32: 0.8335 S33: -0.1527
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 64:78
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2350 7.1033 -27.4639
REMARK 3 T TENSOR
REMARK 3 T11: 0.1162 T22: 0.1550
REMARK 3 T33: 0.1079 T12: 0.0242
REMARK 3 T13: 0.0028 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.0837 L22: 2.6854
REMARK 3 L33: 2.0113 L12: -1.0296
REMARK 3 L13: -0.8082 L23: 1.1502
REMARK 3 S TENSOR
REMARK 3 S11: 0.1287 S12: 0.2071 S13: -0.1213
REMARK 3 S21: -0.3188 S22: -0.3174 S23: 0.4845
REMARK 3 S31: -0.0907 S32: -0.3048 S33: -0.0984
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESSEQ 79:84
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9322 17.9256 -8.1363
REMARK 3 T TENSOR
REMARK 3 T11: 0.4114 T22: 0.3660
REMARK 3 T33: 0.3267 T12: 0.0308
REMARK 3 T13: 0.1810 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 0.1171 L22: 0.0248
REMARK 3 L33: 0.0237 L12: 0.0234
REMARK 3 L13: 0.0520 L23: 0.0157
REMARK 3 S TENSOR
REMARK 3 S11: 0.2688 S12: -0.1786 S13: 0.1968
REMARK 3 S21: 0.4807 S22: -0.0745 S23: 0.3750
REMARK 3 S31: -0.6905 S32: -0.3776 S33: 0.0047
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESSEQ 85:152
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5279 7.8403 -24.3378
REMARK 3 T TENSOR
REMARK 3 T11: 0.0750 T22: 0.1164
REMARK 3 T33: 0.1023 T12: -0.0012
REMARK 3 T13: 0.0020 T23: 0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 1.4381 L22: 1.8115
REMARK 3 L33: 1.4368 L12: -0.3462
REMARK 3 L13: -0.3285 L23: -0.3321
REMARK 3 S TENSOR
REMARK 3 S11: 0.0809 S12: 0.0101 S13: 0.0357
REMARK 3 S21: -0.0232 S22: -0.0347 S23: 0.2321
REMARK 3 S31: -0.0161 S32: -0.1304 S33: -0.0102
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESSEQ 153:184
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2983 -2.7559 -20.2486
REMARK 3 T TENSOR
REMARK 3 T11: 0.1607 T22: 0.1400
REMARK 3 T33: 0.1721 T12: -0.0274
REMARK 3 T13: 0.0210 T23: 0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 1.1325 L22: 0.7773
REMARK 3 L33: 0.5868 L12: -0.2301
REMARK 3 L13: 0.0242 L23: -0.0449
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: -0.1074 S13: -0.2630
REMARK 3 S21: 0.0709 S22: -0.0314 S23: 0.4417
REMARK 3 S31: 0.2439 S32: -0.2517 S33: 0.0177
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESSEQ 185:243
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2815 7.4723 -15.9955
REMARK 3 T TENSOR
REMARK 3 T11: 0.1176 T22: 0.1461
REMARK 3 T33: 0.0804 T12: -0.0232
REMARK 3 T13: 0.0088 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.5539 L22: 0.9424
REMARK 3 L33: 1.3812 L12: -0.3708
REMARK 3 L13: -0.2967 L23: -0.2924
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.1938 S13: 0.1506
REMARK 3 S21: 0.3116 S22: -0.0175 S23: -0.0610
REMARK 3 S31: -0.0585 S32: 0.0003 S33: -0.0010
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND RESSEQ 244:280
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7386 13.4594 -22.5954
REMARK 3 T TENSOR
REMARK 3 T11: 0.1485 T22: 0.1216
REMARK 3 T33: 0.2162 T12: -0.0109
REMARK 3 T13: 0.0480 T23: 0.0881
REMARK 3 L TENSOR
REMARK 3 L11: 2.6086 L22: 1.0808
REMARK 3 L33: 1.1138 L12: -0.4261
REMARK 3 L13: 0.0527 L23: -1.0188
REMARK 3 S TENSOR
REMARK 3 S11: 0.1242 S12: -0.1834 S13: 0.5082
REMARK 3 S21: -0.1129 S22: -0.1547 S23: -0.3054
REMARK 3 S31: -0.2655 S32: 0.1175 S33: 0.2117
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND RESSEQ 281:302
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1374 6.5503 -18.1911
REMARK 3 T TENSOR
REMARK 3 T11: 0.1143 T22: 0.1216
REMARK 3 T33: 0.1612 T12: 0.0039
REMARK 3 T13: 0.0090 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 1.6277 L22: 1.7869
REMARK 3 L33: 1.2184 L12: 0.4661
REMARK 3 L13: 0.2346 L23: -0.3772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0790 S12: -0.2238 S13: 0.3493
REMARK 3 S21: 0.2140 S22: -0.2610 S23: -0.0115
REMARK 3 S31: -0.0406 S32: 0.0077 S33: -0.1778
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND RESSEQ 56:63
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6305 6.0116 -21.3089
REMARK 3 T TENSOR
REMARK 3 T11: -0.1441 T22: 0.4474
REMARK 3 T33: 0.4249 T12: -0.3167
REMARK 3 T13: 0.1717 T23: 0.4308
REMARK 3 L TENSOR
REMARK 3 L11: 0.6884 L22: 0.1691
REMARK 3 L33: 1.1121 L12: 0.1048
REMARK 3 L13: -0.8724 L23: -0.1240
REMARK 3 S TENSOR
REMARK 3 S11: 0.0990 S12: 0.5361 S13: 0.9176
REMARK 3 S21: -0.3223 S22: -0.0155 S23: -0.4495
REMARK 3 S31: -0.3839 S32: 0.5240 S33: 0.9628
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND RESSEQ 64:78
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8679 -9.1863 -3.6608
REMARK 3 T TENSOR
REMARK 3 T11: 0.0629 T22: 0.1547
REMARK 3 T33: 0.1395 T12: 0.0258
REMARK 3 T13: -0.0156 T23: 0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 0.9698 L22: 1.4399
REMARK 3 L33: 1.0143 L12: -0.0898
REMARK 3 L13: 0.1356 L23: 0.2163
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: 0.0322 S13: -0.0317
REMARK 3 S21: 0.1223 S22: -0.1988 S23: -0.4566
REMARK 3 S31: -0.0412 S32: 0.4105 S33: 0.1221
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B AND RESSEQ 79:121
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8051 -14.8699 -1.0635
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.1028
REMARK 3 T33: 0.1050 T12: 0.0457
REMARK 3 T13: 0.0096 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.0904 L22: 1.5945
REMARK 3 L33: 1.4137 L12: -0.4594
REMARK 3 L13: 0.8725 L23: -0.0277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0409 S12: 0.0339 S13: 0.0834
REMARK 3 S21: 0.0690 S22: -0.0314 S23: -0.1057
REMARK 3 S31: 0.1720 S32: 0.2866 S33: 0.0030
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND RESSEQ 122:191
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1783 -2.6718 -2.2165
REMARK 3 T TENSOR
REMARK 3 T11: 0.0969 T22: 0.1005
REMARK 3 T33: 0.1311 T12: 0.0018
REMARK 3 T13: 0.0026 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 1.1992 L22: 1.4042
REMARK 3 L33: 2.1636 L12: -0.2029
REMARK 3 L13: -0.1694 L23: -0.3997
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: -0.0834 S13: 0.3533
REMARK 3 S21: 0.1653 S22: -0.0530 S23: -0.0147
REMARK 3 S31: -0.1959 S32: 0.1886 S33: -0.0309
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND RESSEQ 192:215
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1252 -5.2542 -15.7859
REMARK 3 T TENSOR
REMARK 3 T11: 0.4371 T22: 0.3828
REMARK 3 T33: 0.3587 T12: -0.1294
REMARK 3 T13: 0.0625 T23: 0.0965
REMARK 3 L TENSOR
REMARK 3 L11: 0.6435 L22: 0.4571
REMARK 3 L33: 0.4582 L12: -0.4032
REMARK 3 L13: 0.0434 L23: -0.3657
REMARK 3 S TENSOR
REMARK 3 S11: -0.3106 S12: 0.1834 S13: 0.0722
REMARK 3 S21: -0.8212 S22: 0.2127 S23: -0.1852
REMARK 3 S31: -0.1165 S32: -0.0760 S33: -0.0142
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND RESSEQ 216:243
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8390 -13.2172 -10.1181
REMARK 3 T TENSOR
REMARK 3 T11: 0.0964 T22: 0.0845
REMARK 3 T33: 0.0874 T12: 0.0136
REMARK 3 T13: 0.0189 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.7952 L22: 0.6499
REMARK 3 L33: 1.3568 L12: 0.4235
REMARK 3 L13: 0.2224 L23: -0.4696
REMARK 3 S TENSOR
REMARK 3 S11: 0.0286 S12: 0.0181 S13: 0.0778
REMARK 3 S21: -0.0018 S22: -0.0160 S23: 0.1018
REMARK 3 S31: 0.1478 S32: 0.0127 S33: -0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND RESSEQ 244:280
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2506 -15.8816 -19.2895
REMARK 3 T TENSOR
REMARK 3 T11: 0.1413 T22: 0.1242
REMARK 3 T33: 0.0560 T12: 0.0650
REMARK 3 T13: 0.0767 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.1814 L22: 1.1789
REMARK 3 L33: 0.8894 L12: -0.4441
REMARK 3 L13: 0.3372 L23: -0.2051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0881 S12: 0.2275 S13: -0.0688
REMARK 3 S21: -0.4058 S22: -0.0815 S23: -0.2102
REMARK 3 S31: 0.2613 S32: 0.0775 S33: -0.0359
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND RESSEQ 281:302
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9271 -8.8224 -15.8289
REMARK 3 T TENSOR
REMARK 3 T11: 0.0693 T22: 0.1094
REMARK 3 T33: 0.0744 T12: 0.0106
REMARK 3 T13: 0.0241 T23: 0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 0.6918 L22: 1.0234
REMARK 3 L33: 1.0710 L12: -0.4619
REMARK 3 L13: 0.4562 L23: 0.4966
REMARK 3 S TENSOR
REMARK 3 S11: 0.1181 S12: 0.0424 S13: 0.1297
REMARK 3 S21: 0.0416 S22: -0.2249 S23: -0.0345
REMARK 3 S31: 0.0550 S32: 0.1042 S33: -0.0174
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN C AND RESSEQ 1:6
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5835 21.5676 -11.6728
REMARK 3 T TENSOR
REMARK 3 T11: 0.2576 T22: 0.1813
REMARK 3 T33: 0.2110 T12: -0.0477
REMARK 3 T13: 0.0813 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 0.6620 L22: 0.1671
REMARK 3 L33: 0.1401 L12: 0.0406
REMARK 3 L13: 0.2504 L23: -0.0699
REMARK 3 S TENSOR
REMARK 3 S11: 0.2697 S12: 0.0864 S13: 0.4597
REMARK 3 S21: -0.0567 S22: -0.0767 S23: -0.0244
REMARK 3 S31: -0.3179 S32: 0.1066 S33: -0.0234
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN D AND RESSEQ 1:6
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5004 -23.1989 -5.2262
REMARK 3 T TENSOR
REMARK 3 T11: 0.1615 T22: 0.0623
REMARK 3 T33: 0.1164 T12: 0.0175
REMARK 3 T13: -0.0132 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.2736 L22: 0.2466
REMARK 3 L33: 0.4750 L12: 0.2608
REMARK 3 L13: 0.3626 L23: 0.3434
REMARK 3 S TENSOR
REMARK 3 S11: 0.1873 S12: -0.0951 S13: -0.2203
REMARK 3 S21: 0.0692 S22: 0.0964 S23: -0.0660
REMARK 3 S31: 0.4793 S32: 0.0116 S33: 0.0444
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: ( CHAIN A AND RESSEQ 501:665 ) OR ( CHAIN B AND
REMARK 3 RESSEQ 501:704 ) OR ( CHAIN C AND RESSEQ 201:205 )
REMARK 3 OR ( CHAIN D AND RESSEQ 201:208 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2351 -3.3877 -14.5473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1533 T22: 0.1967
REMARK 3 T33: 0.1782 T12: -0.0047
REMARK 3 T13: 0.0498 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.5360 L22: 0.9886
REMARK 3 L33: 1.0144 L12: -0.3535
REMARK 3 L13: 0.3836 L23: -0.4842
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.0297 S13: 0.0614
REMARK 3 S21: -0.0691 S22: -0.0206 S23: -0.0311
REMARK 3 S31: 0.0380 S32: 0.0605 S33: -0.0013
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 4JR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.116
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55958
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.59400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: PDB ENTRY 1F1J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM TRIS, PH 8.0, 2 MM DTT, 50 MM
REMARK 280 SODIUM CHLORIDE, 200 MM SODIUM/POTASSIUM PHOSPHATE, 100 MM BIS-
REMARK 280 TRIS PROPANE, PH 6.5, 20% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 29.24650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.44550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.33150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.44550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.24650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.33150
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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE AC-ASP-GLU-VAL-ASP-CMK IS PEPTIDE-LIKE, A MEMBER OF INHIBITOR
REMARK 400 CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: AC-ASP-GLU-VAL-ASP-CMK
REMARK 400 CHAIN: C, D
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 SER A 54
REMARK 465 ASN A 55
REMARK 465 THR A 189
REMARK 465 GLU A 190
REMARK 465 LEU A 191
REMARK 465 ASP A 192
REMARK 465 ASP A 193
REMARK 465 GLY A 194
REMARK 465 ILE A 195
REMARK 465 GLN A 196
REMARK 465 ALA A 197
REMARK 465 ALA A 198
REMARK 465 SER A 199
REMARK 465 GLY A 200
REMARK 465 PRO A 201
REMARK 465 ILE A 202
REMARK 465 ASN A 203
REMARK 465 ASP A 204
REMARK 465 THR A 205
REMARK 465 ASP A 206
REMARK 465 ALA A 207
REMARK 465 ASN A 208
REMARK 465 PRO A 209
REMARK 465 ARG A 210
REMARK 465 TYR A 211
REMARK 465 GLN A 303
REMARK 465 SER B 54
REMARK 465 ASN B 55
REMARK 465 ALA B 198
REMARK 465 SER B 199
REMARK 465 GLY B 200
REMARK 465 PRO B 201
REMARK 465 ILE B 202
REMARK 465 ASN B 203
REMARK 465 ASP B 204
REMARK 465 THR B 205
REMARK 465 ASP B 206
REMARK 465 ALA B 207
REMARK 465 ASN B 208
REMARK 465 PRO B 209
REMARK 465 ARG B 210
REMARK 465 TYR B 211
REMARK 465 GLN B 303
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 GLU A 147 -126.73 53.58
REMARK 500 ASN B 148 -5.64 75.06
REMARK 500 PHE B 301 57.08 -91.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF AC-DEVD-CMK
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF AC-DEVD-CMK
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JQY RELATED DB: PDB
REMARK 900 RELATED ID: 4JQZ RELATED DB: PDB
REMARK 900 RELATED ID: 4JR0 RELATED DB: PDB
REMARK 900 RELATED ID: 4JR1 RELATED DB: PDB
DBREF 4JR2 A 57 303 UNP P55210 CASP7_HUMAN 57 303
DBREF 4JR2 B 57 303 UNP P55210 CASP7_HUMAN 57 303
DBREF 4JR2 C 1 6 PDB 4JR2 4JR2 1 6
DBREF 4JR2 D 1 6 PDB 4JR2 4JR2 1 6
SEQADV 4JR2 SER A 54 UNP P55210 EXPRESSION TAG
SEQADV 4JR2 ASN A 55 UNP P55210 EXPRESSION TAG
SEQADV 4JR2 ALA A 56 UNP P55210 EXPRESSION TAG
SEQADV 4JR2 ALA A 198 UNP P55210 ASP 198 ENGINEERED MUTATION
SEQADV 4JR2 SER B 54 UNP P55210 EXPRESSION TAG
SEQADV 4JR2 ASN B 55 UNP P55210 EXPRESSION TAG
SEQADV 4JR2 ALA B 56 UNP P55210 EXPRESSION TAG
SEQADV 4JR2 ALA B 198 UNP P55210 ASP 198 ENGINEERED MUTATION
SEQRES 1 A 250 SER ASN ALA THR TYR GLN TYR ASN MET ASN PHE GLU LYS
SEQRES 2 A 250 LEU GLY LYS CYS ILE ILE ILE ASN ASN LYS ASN PHE ASP
SEQRES 3 A 250 LYS VAL THR GLY MET GLY VAL ARG ASN GLY THR ASP LYS
SEQRES 4 A 250 ASP ALA GLU ALA LEU PHE LYS CYS PHE ARG SER LEU GLY
SEQRES 5 A 250 PHE ASP VAL ILE VAL TYR ASN ASP CYS SER CYS ALA LYS
SEQRES 6 A 250 MET GLN ASP LEU LEU LYS LYS ALA SER GLU GLU ASP HIS
SEQRES 7 A 250 THR ASN ALA ALA CYS PHE ALA CYS ILE LEU LEU SER HIS
SEQRES 8 A 250 GLY GLU GLU ASN VAL ILE TYR GLY LYS ASP GLY VAL THR
SEQRES 9 A 250 PRO ILE LYS ASP LEU THR ALA HIS PHE ARG GLY ASP ARG
SEQRES 10 A 250 CYS LYS THR LEU LEU GLU LYS PRO LYS LEU PHE PHE ILE
SEQRES 11 A 250 GLN ALA CYS ARG GLY THR GLU LEU ASP ASP GLY ILE GLN
SEQRES 12 A 250 ALA ALA SER GLY PRO ILE ASN ASP THR ASP ALA ASN PRO
SEQRES 13 A 250 ARG TYR LYS ILE PRO VAL GLU ALA ASP PHE LEU PHE ALA
SEQRES 14 A 250 TYR SER THR VAL PRO GLY TYR TYR SER TRP ARG SER PRO
SEQRES 15 A 250 GLY ARG GLY SER TRP PHE VAL GLN ALA LEU CYS SER ILE
SEQRES 16 A 250 LEU GLU GLU HIS GLY LYS ASP LEU GLU ILE MET GLN ILE
SEQRES 17 A 250 LEU THR ARG VAL ASN ASP ARG VAL ALA ARG HIS PHE GLU
SEQRES 18 A 250 SER GLN SER ASP ASP PRO HIS PHE HIS GLU LYS LYS GLN
SEQRES 19 A 250 ILE PRO CYS VAL VAL SER MET LEU THR LYS GLU LEU TYR
SEQRES 20 A 250 PHE SER GLN
SEQRES 1 B 250 SER ASN ALA THR TYR GLN TYR ASN MET ASN PHE GLU LYS
SEQRES 2 B 250 LEU GLY LYS CYS ILE ILE ILE ASN ASN LYS ASN PHE ASP
SEQRES 3 B 250 LYS VAL THR GLY MET GLY VAL ARG ASN GLY THR ASP LYS
SEQRES 4 B 250 ASP ALA GLU ALA LEU PHE LYS CYS PHE ARG SER LEU GLY
SEQRES 5 B 250 PHE ASP VAL ILE VAL TYR ASN ASP CYS SER CYS ALA LYS
SEQRES 6 B 250 MET GLN ASP LEU LEU LYS LYS ALA SER GLU GLU ASP HIS
SEQRES 7 B 250 THR ASN ALA ALA CYS PHE ALA CYS ILE LEU LEU SER HIS
SEQRES 8 B 250 GLY GLU GLU ASN VAL ILE TYR GLY LYS ASP GLY VAL THR
SEQRES 9 B 250 PRO ILE LYS ASP LEU THR ALA HIS PHE ARG GLY ASP ARG
SEQRES 10 B 250 CYS LYS THR LEU LEU GLU LYS PRO LYS LEU PHE PHE ILE
SEQRES 11 B 250 GLN ALA CYS ARG GLY THR GLU LEU ASP ASP GLY ILE GLN
SEQRES 12 B 250 ALA ALA SER GLY PRO ILE ASN ASP THR ASP ALA ASN PRO
SEQRES 13 B 250 ARG TYR LYS ILE PRO VAL GLU ALA ASP PHE LEU PHE ALA
SEQRES 14 B 250 TYR SER THR VAL PRO GLY TYR TYR SER TRP ARG SER PRO
SEQRES 15 B 250 GLY ARG GLY SER TRP PHE VAL GLN ALA LEU CYS SER ILE
SEQRES 16 B 250 LEU GLU GLU HIS GLY LYS ASP LEU GLU ILE MET GLN ILE
SEQRES 17 B 250 LEU THR ARG VAL ASN ASP ARG VAL ALA ARG HIS PHE GLU
SEQRES 18 B 250 SER GLN SER ASP ASP PRO HIS PHE HIS GLU LYS LYS GLN
SEQRES 19 B 250 ILE PRO CYS VAL VAL SER MET LEU THR LYS GLU LEU TYR
SEQRES 20 B 250 PHE SER GLN
SEQRES 1 C 6 ACE ASP GLU VAL ASP 0QE
SEQRES 1 D 6 ACE ASP GLU VAL ASP 0QE
HET ACE C 1 3
HET 0QE C 6 1
HET ACE D 1 3
HET 0QE D 6 1
HET CL A 401 1
HET CL B 401 1
HETNAM ACE ACETYL GROUP
HETNAM 0QE CHLOROMETHANE
HETNAM CL CHLORIDE ION
HETSYN 0QE CHLORO METHYL GROUP
FORMUL 3 ACE 2(C2 H4 O)
FORMUL 3 0QE 2(C H3 CL)
FORMUL 5 CL 2(CL 1-)
FORMUL 7 HOH *382(H2 O)
HELIX 1 1 ASP A 79 GLY A 83 5 5
HELIX 2 2 GLY A 89 GLY A 105 1 17
HELIX 3 3 SER A 115 GLU A 128 1 14
HELIX 4 4 ILE A 159 ALA A 164 1 6
HELIX 5 5 HIS A 165 ARG A 167 5 3
HELIX 6 6 CYS A 171 LEU A 175 5 5
HELIX 7 7 TRP A 240 GLY A 253 1 14
HELIX 8 8 GLU A 257 PHE A 273 1 17
HELIX 9 9 ASP A 279 HIS A 283 5 5
HELIX 10 10 ASP B 79 GLY B 83 5 5
HELIX 11 11 GLY B 89 GLY B 105 1 17
HELIX 12 12 SER B 115 GLU B 129 1 15
HELIX 13 13 ILE B 159 ALA B 164 1 6
HELIX 14 14 HIS B 165 ARG B 167 5 3
HELIX 15 15 CYS B 171 LEU B 175 5 5
HELIX 16 16 TRP B 240 GLY B 253 1 14
HELIX 17 17 GLU B 257 PHE B 273 1 17
HELIX 18 18 ASP B 279 HIS B 283 5 5
SHEET 1 A12 PHE A 106 ASN A 112 0
SHEET 2 A12 GLY A 68 ASN A 74 1 N ASN A 74 O TYR A 111
SHEET 3 A12 PHE A 137 LEU A 142 1 O ILE A 140 N ILE A 71
SHEET 4 A12 LYS A 179 GLN A 184 1 O PHE A 182 N LEU A 141
SHEET 5 A12 PHE A 219 TYR A 223 1 O ALA A 222 N PHE A 181
SHEET 6 A12 CYS A 290 SER A 293 -1 O VAL A 292 N PHE A 221
SHEET 7 A12 CYS B 290 SER B 293 -1 O SER B 293 N VAL A 291
SHEET 8 A12 PHE B 219 TYR B 223 -1 N PHE B 221 O VAL B 292
SHEET 9 A12 LYS B 179 GLN B 184 1 N PHE B 181 O ALA B 222
SHEET 10 A12 ALA B 134 LEU B 142 1 N LEU B 141 O GLN B 184
SHEET 11 A12 LYS B 66 ASN B 74 1 N ILE B 71 O ILE B 140
SHEET 12 A12 PHE B 106 ASN B 112 1 O TYR B 111 N ASN B 74
SHEET 1 B 3 GLY A 145 GLU A 146 0
SHEET 2 B 3 VAL A 149 GLY A 152 -1 O VAL A 149 N GLU A 146
SHEET 3 B 3 GLY A 155 PRO A 158 -1 O GLY A 155 N GLY A 152
SHEET 1 C 3 GLY A 238 SER A 239 0
SHEET 2 C 3 TRP A 232 SER A 234 -1 N SER A 234 O GLY A 238
SHEET 3 C 3 GLU C 3 VAL C 4 -1 O GLU C 3 N ARG A 233
SHEET 1 D 3 GLY B 145 GLU B 146 0
SHEET 2 D 3 VAL B 149 GLY B 152 -1 O VAL B 149 N GLU B 146
SHEET 3 D 3 GLY B 155 PRO B 158 -1 O GLY B 155 N GLY B 152
SHEET 1 E 3 GLY B 238 SER B 239 0
SHEET 2 E 3 TRP B 232 SER B 234 -1 N SER B 234 O GLY B 238
SHEET 3 E 3 GLU D 3 VAL D 4 -1 O GLU D 3 N ARG B 233
SSBOND 1 CYS A 100 CYS A 246 1555 1555 2.05
SSBOND 2 CYS B 100 CYS B 246 1555 1555 2.05
LINK SG CYS A 186 C1 0QE C 6 1555 1555 2.17
LINK SG CYS B 186 C1 0QE D 6 1555 1555 2.15
LINK C ACE C 1 N ASP C 2 1555 1555 1.33
LINK C ASP C 5 C1 0QE C 6 1555 1555 1.47
LINK C ACE D 1 N ASP D 2 1555 1555 1.34
LINK C ASP D 5 C1 0QE D 6 1555 1555 1.44
SITE 1 AC1 6 LYS A 76 GLY A 89 THR A 90 ASP A 91
SITE 2 AC1 6 HOH A 546 HOH A 566
SITE 1 AC2 5 LYS B 76 GLY B 89 THR B 90 ASP B 91
SITE 2 AC2 5 HOH B 662
SITE 1 AC3 17 ARG A 87 SER A 143 HIS A 144 GLY A 145
SITE 2 AC3 17 GLN A 184 CYS A 186 SER A 231 TRP A 232
SITE 3 AC3 17 ARG A 233 PRO A 235 SER A 275 GLN A 276
SITE 4 AC3 17 HOH A 630 HOH C 202 HOH C 203 HOH C 204
SITE 5 AC3 17 HOH C 205
SITE 1 AC4 20 ARG B 87 SER B 143 HIS B 144 GLY B 145
SITE 2 AC4 20 GLN B 184 CYS B 186 SER B 231 TRP B 232
SITE 3 AC4 20 ARG B 233 SER B 234 PRO B 235 SER B 275
SITE 4 AC4 20 GLN B 276 HOH B 556 HOH D 201 HOH D 202
SITE 5 AC4 20 HOH D 203 HOH D 204 HOH D 205 HOH D 207
CRYST1 58.493 88.663 88.891 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017096 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011250 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
