HEADER APOPTOSIS INHIBITOR 26-MAR-12 4EC4
TITLE XIAP-BIR3 IN COMPLEX WITH A POTENT DIVALENT SMAC MIMETIC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B, C, D, E, J, F, G, K, L;
COMPND 4 FRAGMENT: BIR3 DOMAIN (UNP RESIDUES 241-356);
COMPND 5 SYNONYM: E3 UBIQUITIN-PROTEIN LIGASE XIAP, IAP-LIKE PROTEIN, ILP,
COMPND 6 HILP, INHIBITOR OF APOPTOSIS PROTEIN 3, IAP-3, HIAP-3, HIAP3, X-
COMPND 7 LINKED INHIBITOR OF APOPTOSIS PROTEIN, X-LINKED IAP;
COMPND 8 EC: 6.3.2.-;
COMPND 9 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: XIAP, API3, BIRC4, IAP3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZINC FINGER, APOPTOSIS INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR E.MASTRANGELO,F.COSSU,M.BOLOGNESI,M.MILANI
REVDAT 2 13-SEP-23 4EC4 1 REMARK SEQADV HETSYN LINK
REVDAT 1 05-DEC-12 4EC4 0
JRNL AUTH F.COSSU,M.MILANI,P.VACHETTE,F.MALVEZZI,S.GRASSI,D.LECIS,
JRNL AUTH 2 D.DELIA,C.DRAGO,P.SENECI,M.BOLOGNESI,E.MASTRANGELO
JRNL TITL STRUCTURAL INSIGHT INTO INHIBITOR OF APOPTOSIS PROTEINS
JRNL TITL 2 RECOGNITION BY A POTENT DIVALENT SMAC-MIMETIC.
JRNL REF PLOS ONE V. 7 49527 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 23166698
JRNL DOI 10.1371/JOURNAL.PONE.0049527
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 27126
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1440
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1975
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8691
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 562
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.54000
REMARK 3 B22 (A**2) : -1.63000
REMARK 3 B33 (A**2) : -0.91000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.545
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.429
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 56.742
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.877
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.795
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9611 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12975 ; 1.283 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1059 ; 5.676 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 474 ;36.246 ;24.304
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1426 ;21.737 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;13.364 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1246 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7458 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5328 ; 0.332 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8523 ; 0.651 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4283 ; 1.077 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4451 ; 1.817 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 246 A 354
REMARK 3 RESIDUE RANGE : A 401 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7842 4.9970 19.0912
REMARK 3 T TENSOR
REMARK 3 T11: 0.0208 T22: 0.1008
REMARK 3 T33: 0.0884 T12: -0.0253
REMARK 3 T13: -0.0376 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 3.8704 L22: 1.4999
REMARK 3 L33: 3.6275 L12: -0.4358
REMARK 3 L13: -1.6355 L23: 0.9798
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.0483 S13: -0.1230
REMARK 3 S21: 0.0384 S22: -0.0495 S23: -0.0431
REMARK 3 S31: -0.0144 S32: 0.0186 S33: 0.0643
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 248 B 353
REMARK 3 RESIDUE RANGE : B 401 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6939 9.2797 -38.0399
REMARK 3 T TENSOR
REMARK 3 T11: 0.2958 T22: 0.2673
REMARK 3 T33: 0.2495 T12: 0.0567
REMARK 3 T13: 0.1005 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 5.3436 L22: 2.8936
REMARK 3 L33: 3.7686 L12: 3.1359
REMARK 3 L13: -1.0218 L23: 1.2423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.0874 S13: 0.1228
REMARK 3 S21: -0.1680 S22: 0.2068 S23: -0.1830
REMARK 3 S31: -0.1701 S32: 0.3409 S33: -0.2033
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 249 C 353
REMARK 3 RESIDUE RANGE : C 401 C 401
REMARK 3 RESIDUE RANGE : J 401 J 401
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8589 -23.4291 39.8714
REMARK 3 T TENSOR
REMARK 3 T11: 0.4523 T22: 0.1796
REMARK 3 T33: 0.2376 T12: -0.0648
REMARK 3 T13: -0.1480 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 2.7125 L22: 2.2973
REMARK 3 L33: 6.4006 L12: -0.6075
REMARK 3 L13: 1.0316 L23: -1.7386
REMARK 3 S TENSOR
REMARK 3 S11: 0.2601 S12: -0.1984 S13: -0.2516
REMARK 3 S21: 0.3795 S22: -0.2209 S23: -0.3039
REMARK 3 S31: 1.0465 S32: -0.0536 S33: -0.0392
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 249 D 353
REMARK 3 RESIDUE RANGE : D 401 D 402
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8511 18.7257 -7.3808
REMARK 3 T TENSOR
REMARK 3 T11: 0.0686 T22: 0.1014
REMARK 3 T33: 0.1084 T12: -0.0373
REMARK 3 T13: 0.0356 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 2.3703 L22: 2.7584
REMARK 3 L33: 6.0537 L12: -0.8039
REMARK 3 L13: 0.6599 L23: -0.7388
REMARK 3 S TENSOR
REMARK 3 S11: 0.1124 S12: -0.0430 S13: -0.0620
REMARK 3 S21: 0.1542 S22: 0.0639 S23: -0.1003
REMARK 3 S31: 0.0013 S32: 0.1228 S33: -0.1763
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 246 E 353
REMARK 3 RESIDUE RANGE : E 401 E 402
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7882 -17.0373 -7.6731
REMARK 3 T TENSOR
REMARK 3 T11: 0.0739 T22: 0.1371
REMARK 3 T33: 0.1628 T12: -0.0646
REMARK 3 T13: -0.0472 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 3.9433 L22: 2.8395
REMARK 3 L33: 4.7545 L12: -1.5737
REMARK 3 L13: 0.3482 L23: 0.4738
REMARK 3 S TENSOR
REMARK 3 S11: -0.1336 S12: -0.2937 S13: 0.0281
REMARK 3 S21: 0.1629 S22: -0.0098 S23: -0.0109
REMARK 3 S31: 0.0703 S32: -0.1381 S33: 0.1434
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 246 J 353
REMARK 3 RESIDUE RANGE : J 402 J 402
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8124 -9.1416 24.1433
REMARK 3 T TENSOR
REMARK 3 T11: 0.0863 T22: 0.1054
REMARK 3 T33: 0.0858 T12: 0.0111
REMARK 3 T13: 0.0098 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 4.9356 L22: 1.6292
REMARK 3 L33: 4.6506 L12: -0.1713
REMARK 3 L13: 1.9686 L23: -0.2121
REMARK 3 S TENSOR
REMARK 3 S11: 0.1520 S12: -0.2356 S13: -0.0864
REMARK 3 S21: 0.1128 S22: -0.1129 S23: 0.2268
REMARK 3 S31: 0.0495 S32: -0.2791 S33: -0.0391
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 248 F 352
REMARK 3 RESIDUE RANGE : F 401 F 401
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9535 20.6228 37.5882
REMARK 3 T TENSOR
REMARK 3 T11: 0.2864 T22: 0.0630
REMARK 3 T33: 0.1659 T12: -0.0010
REMARK 3 T13: 0.0435 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 3.6723 L22: 3.4833
REMARK 3 L33: 7.3571 L12: -0.1425
REMARK 3 L13: 2.1035 L23: 0.2459
REMARK 3 S TENSOR
REMARK 3 S11: 0.0792 S12: -0.1835 S13: 0.1298
REMARK 3 S21: 0.5043 S22: -0.1201 S23: -0.0647
REMARK 3 S31: -0.7634 S32: 0.1259 S33: 0.0409
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 247 G 353
REMARK 3 RESIDUE RANGE : G 401 G 401
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0865 -6.6467 -40.7444
REMARK 3 T TENSOR
REMARK 3 T11: 0.1521 T22: 0.1806
REMARK 3 T33: 0.2053 T12: -0.0145
REMARK 3 T13: 0.0384 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 4.0965 L22: 2.8476
REMARK 3 L33: 8.3545 L12: 0.9098
REMARK 3 L13: 2.0964 L23: 0.8280
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: 0.3071 S13: -0.3139
REMARK 3 S21: -0.2654 S22: -0.0107 S23: 0.0985
REMARK 3 S31: 0.0842 S32: -0.3328 S33: 0.0579
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 246 K 352
REMARK 3 RESIDUE RANGE : K 401 K 401
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1226 33.2310 -19.5710
REMARK 3 T TENSOR
REMARK 3 T11: 0.2602 T22: 0.2734
REMARK 3 T33: 0.2715 T12: 0.1004
REMARK 3 T13: -0.0425 T23: -0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 8.3102 L22: 1.6634
REMARK 3 L33: 2.8538 L12: 1.1871
REMARK 3 L13: -0.0968 L23: -1.0598
REMARK 3 S TENSOR
REMARK 3 S11: 0.0496 S12: -0.0919 S13: 0.1666
REMARK 3 S21: -0.0790 S22: -0.0595 S23: 0.5228
REMARK 3 S31: -0.3956 S32: -0.4264 S33: 0.0099
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 247 L 353
REMARK 3 RESIDUE RANGE : L 401 L 401
REMARK 3 ORIGIN FOR THE GROUP (A): 45.0482 -31.8420 -16.3392
REMARK 3 T TENSOR
REMARK 3 T11: 0.3172 T22: 0.2489
REMARK 3 T33: 0.2564 T12: 0.0851
REMARK 3 T13: 0.0974 T23: 0.1131
REMARK 3 L TENSOR
REMARK 3 L11: 8.4772 L22: 4.1591
REMARK 3 L33: 2.7822 L12: 0.9624
REMARK 3 L13: 0.5247 L23: 0.0200
REMARK 3 S TENSOR
REMARK 3 S11: -0.1777 S12: -0.2347 S13: -0.6358
REMARK 3 S21: 0.1006 S22: -0.1751 S23: -0.6100
REMARK 3 S31: 0.4006 S32: 0.5978 S33: 0.3528
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4EC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071431.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93340
REMARK 200 MONOCHROMATOR : 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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28624
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 51.412
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.25800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.50800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3CLX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.2 M SODIUM CITRATE, 0.1
REMARK 280 M TRIS, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 32.71000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 107.86500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 107.86500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.71000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.24500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 241
REMARK 465 ASP A 242
REMARK 465 ALA A 243
REMARK 465 VAL A 244
REMARK 465 SER A 245
REMARK 465 THR A 355
REMARK 465 THR A 356
REMARK 465 HIS A 357
REMARK 465 HIS A 358
REMARK 465 HIS A 359
REMARK 465 HIS A 360
REMARK 465 HIS A 361
REMARK 465 HIS A 362
REMARK 465 SER B 241
REMARK 465 ASP B 242
REMARK 465 ALA B 243
REMARK 465 VAL B 244
REMARK 465 SER B 245
REMARK 465 SER B 246
REMARK 465 ASP B 247
REMARK 465 ARG B 354
REMARK 465 THR B 355
REMARK 465 THR B 356
REMARK 465 HIS B 357
REMARK 465 HIS B 358
REMARK 465 HIS B 359
REMARK 465 HIS B 360
REMARK 465 HIS B 361
REMARK 465 HIS B 362
REMARK 465 SER C 241
REMARK 465 ASP C 242
REMARK 465 ALA C 243
REMARK 465 VAL C 244
REMARK 465 SER C 245
REMARK 465 SER C 246
REMARK 465 ASP C 247
REMARK 465 ARG C 248
REMARK 465 ARG C 354
REMARK 465 THR C 355
REMARK 465 THR C 356
REMARK 465 HIS C 357
REMARK 465 HIS C 358
REMARK 465 HIS C 359
REMARK 465 HIS C 360
REMARK 465 HIS C 361
REMARK 465 HIS C 362
REMARK 465 SER D 241
REMARK 465 ASP D 242
REMARK 465 ALA D 243
REMARK 465 VAL D 244
REMARK 465 SER D 245
REMARK 465 SER D 246
REMARK 465 ASP D 247
REMARK 465 ARG D 248
REMARK 465 ARG D 354
REMARK 465 THR D 355
REMARK 465 THR D 356
REMARK 465 HIS D 357
REMARK 465 HIS D 358
REMARK 465 HIS D 359
REMARK 465 HIS D 360
REMARK 465 HIS D 361
REMARK 465 HIS D 362
REMARK 465 SER E 241
REMARK 465 ASP E 242
REMARK 465 ALA E 243
REMARK 465 VAL E 244
REMARK 465 SER E 245
REMARK 465 ARG E 354
REMARK 465 THR E 355
REMARK 465 THR E 356
REMARK 465 HIS E 357
REMARK 465 HIS E 358
REMARK 465 HIS E 359
REMARK 465 HIS E 360
REMARK 465 HIS E 361
REMARK 465 HIS E 362
REMARK 465 SER J 241
REMARK 465 ASP J 242
REMARK 465 ALA J 243
REMARK 465 VAL J 244
REMARK 465 SER J 245
REMARK 465 ARG J 354
REMARK 465 THR J 355
REMARK 465 THR J 356
REMARK 465 HIS J 357
REMARK 465 HIS J 358
REMARK 465 HIS J 359
REMARK 465 HIS J 360
REMARK 465 HIS J 361
REMARK 465 HIS J 362
REMARK 465 SER F 241
REMARK 465 ASP F 242
REMARK 465 ALA F 243
REMARK 465 VAL F 244
REMARK 465 SER F 245
REMARK 465 SER F 246
REMARK 465 ASP F 247
REMARK 465 VAL F 353
REMARK 465 ARG F 354
REMARK 465 THR F 355
REMARK 465 THR F 356
REMARK 465 HIS F 357
REMARK 465 HIS F 358
REMARK 465 HIS F 359
REMARK 465 HIS F 360
REMARK 465 HIS F 361
REMARK 465 HIS F 362
REMARK 465 SER G 241
REMARK 465 ASP G 242
REMARK 465 ALA G 243
REMARK 465 VAL G 244
REMARK 465 SER G 245
REMARK 465 SER G 246
REMARK 465 ARG G 354
REMARK 465 THR G 355
REMARK 465 THR G 356
REMARK 465 HIS G 357
REMARK 465 HIS G 358
REMARK 465 HIS G 359
REMARK 465 HIS G 360
REMARK 465 HIS G 361
REMARK 465 HIS G 362
REMARK 465 SER K 241
REMARK 465 ASP K 242
REMARK 465 ALA K 243
REMARK 465 VAL K 244
REMARK 465 SER K 245
REMARK 465 VAL K 353
REMARK 465 ARG K 354
REMARK 465 THR K 355
REMARK 465 THR K 356
REMARK 465 HIS K 357
REMARK 465 HIS K 358
REMARK 465 HIS K 359
REMARK 465 HIS K 360
REMARK 465 HIS K 361
REMARK 465 HIS K 362
REMARK 465 SER L 241
REMARK 465 ASP L 242
REMARK 465 ALA L 243
REMARK 465 VAL L 244
REMARK 465 SER L 245
REMARK 465 SER L 246
REMARK 465 ARG L 354
REMARK 465 THR L 355
REMARK 465 THR L 356
REMARK 465 HIS L 357
REMARK 465 HIS L 358
REMARK 465 HIS L 359
REMARK 465 HIS L 360
REMARK 465 HIS L 361
REMARK 465 HIS L 362
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP G 247 CG OD1 OD2
REMARK 470 ASP L 247 CG OD1 OD2
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 ASP A 247 59.08 38.57
REMARK 500 PRO A 251 -175.31 -67.96
REMARK 500 SER A 261 -7.84 -58.71
REMARK 500 SER A 278 58.36 -99.39
REMARK 500 GLU A 349 6.52 -67.59
REMARK 500 GLU A 350 -85.33 -78.48
REMARK 500 HIS B 302 -64.22 -104.50
REMARK 500 SER B 313 0.19 87.41
REMARK 500 TRP C 275 79.73 -154.71
REMARK 500 HIS C 302 -68.63 -106.66
REMARK 500 PRO C 312 107.31 -25.53
REMARK 500 CYS C 351 48.59 -85.79
REMARK 500 SER D 253 31.20 -142.88
REMARK 500 ASN D 259 78.38 -170.01
REMARK 500 PHE D 272 40.07 -108.36
REMARK 500 ASP D 296 34.87 -76.95
REMARK 500 ASP D 309 75.30 61.13
REMARK 500 GLU D 314 153.50 -49.64
REMARK 500 TYR D 324 68.51 -117.90
REMARK 500 ASP E 247 -6.40 -146.04
REMARK 500 ASN E 259 88.06 -169.45
REMARK 500 PRO E 312 120.90 -36.49
REMARK 500 SER E 313 35.61 72.48
REMARK 500 LEU E 352 51.97 39.20
REMARK 500 TRP F 275 131.57 -36.17
REMARK 500 GLU F 350 -14.21 -49.15
REMARK 500 PRO G 251 -176.87 -69.79
REMARK 500 PRO G 260 0.91 -69.67
REMARK 500 PHE G 272 37.32 -93.32
REMARK 500 SER G 278 53.98 -99.49
REMARK 500 ASN G 280 105.26 -52.39
REMARK 500 SER G 313 19.26 -68.53
REMARK 500 THR K 254 -153.96 -113.15
REMARK 500 MET K 262 19.22 -142.09
REMARK 500 PHE K 272 36.70 -88.57
REMARK 500 SER K 278 43.73 -75.74
REMARK 500 ASP K 296 33.05 -76.90
REMARK 500 HIS K 302 -65.77 -100.73
REMARK 500 LYS K 322 -80.99 -58.83
REMARK 500 ASN L 259 89.84 -159.02
REMARK 500 TRP L 275 103.17 -43.79
REMARK 500 TYR L 277 -166.17 -76.26
REMARK 500 HIS L 302 -64.48 -91.98
REMARK 500 THR L 308 -58.50 -137.15
REMARK 500 PRO L 312 12.20 -52.55
REMARK 500 SER L 313 -0.18 -147.47
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 300 SG
REMARK 620 2 CYS A 303 SG 102.3
REMARK 620 3 HIS A 320 NE2 99.6 111.5
REMARK 620 4 CYS A 327 SG 126.1 105.6 111.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 300 SG
REMARK 620 2 CYS B 303 SG 90.9
REMARK 620 3 HIS B 320 NE2 110.6 85.6
REMARK 620 4 CYS B 327 SG 132.3 96.6 116.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 300 SG
REMARK 620 2 CYS C 303 SG 105.8
REMARK 620 3 HIS C 320 NE2 112.9 105.1
REMARK 620 4 CYS C 327 SG 128.5 104.4 98.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 300 SG
REMARK 620 2 CYS D 303 SG 91.6
REMARK 620 3 HIS D 320 NE2 105.4 115.4
REMARK 620 4 CYS D 327 SG 113.2 99.2 126.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 300 SG
REMARK 620 2 CYS E 303 SG 104.6
REMARK 620 3 HIS E 320 NE2 97.9 111.9
REMARK 620 4 CYS E 327 SG 131.5 104.2 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 300 SG
REMARK 620 2 CYS J 303 SG 109.0
REMARK 620 3 HIS J 320 NE2 96.8 119.6
REMARK 620 4 CYS J 327 SG 121.7 104.2 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 300 SG
REMARK 620 2 CYS F 303 SG 97.3
REMARK 620 3 HIS F 320 NE2 92.6 123.7
REMARK 620 4 CYS F 327 SG 121.2 110.1 111.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 300 SG
REMARK 620 2 CYS G 303 SG 110.6
REMARK 620 3 HIS G 320 NE2 101.1 109.0
REMARK 620 4 CYS G 327 SG 134.8 104.3 93.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 300 SG
REMARK 620 2 CYS K 303 SG 111.8
REMARK 620 3 HIS K 320 NE2 112.7 116.3
REMARK 620 4 CYS K 327 SG 128.3 100.4 85.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 300 SG
REMARK 620 2 CYS L 303 SG 100.2
REMARK 620 3 HIS L 320 NE2 116.9 90.5
REMARK 620 4 CYS L 327 SG 129.8 106.7 104.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O6 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P33 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O6 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O6 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P33 D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O6 E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O6 J 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P33 J 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EB9 RELATED DB: PDB
DBREF 4EC4 A 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 B 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 C 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 D 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 E 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 J 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 F 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 G 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 K 241 356 UNP P98170 XIAP_HUMAN 241 356
DBREF 4EC4 L 241 356 UNP P98170 XIAP_HUMAN 241 356
SEQADV 4EC4 HIS A 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS A 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS A 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS A 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS A 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS A 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS B 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS B 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS B 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS B 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS B 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS B 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS C 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS C 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS C 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS C 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS C 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS C 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS D 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS D 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS D 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS D 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS D 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS D 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS E 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS E 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS E 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS E 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS E 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS E 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS J 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS J 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS J 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS J 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS J 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS J 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS F 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS F 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS F 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS F 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS F 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS F 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS G 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS G 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS G 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS G 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS G 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS G 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS K 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS K 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS K 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS K 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS K 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS K 362 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS L 357 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS L 358 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS L 359 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS L 360 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS L 361 UNP P98170 EXPRESSION TAG
SEQADV 4EC4 HIS L 362 UNP P98170 EXPRESSION TAG
SEQRES 1 A 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 A 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 A 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 A 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 A 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 A 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 A 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 A 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 A 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 A 122 HIS HIS HIS HIS HIS
SEQRES 1 B 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 B 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 B 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 B 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 B 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 B 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 B 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 B 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 B 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 B 122 HIS HIS HIS HIS HIS
SEQRES 1 C 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 C 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 C 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 C 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 C 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 C 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 C 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 C 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 C 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 C 122 HIS HIS HIS HIS HIS
SEQRES 1 D 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 D 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 D 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 D 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 D 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 D 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 D 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 D 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 D 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 D 122 HIS HIS HIS HIS HIS
SEQRES 1 E 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 E 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 E 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 E 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 E 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 E 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 E 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 E 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 E 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 E 122 HIS HIS HIS HIS HIS
SEQRES 1 J 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 J 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 J 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 J 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 J 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 J 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 J 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 J 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 J 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 J 122 HIS HIS HIS HIS HIS
SEQRES 1 F 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 F 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 F 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 F 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 F 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 F 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 F 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 F 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 F 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 F 122 HIS HIS HIS HIS HIS
SEQRES 1 G 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 G 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 G 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 G 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 G 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 G 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 G 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 G 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 G 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 G 122 HIS HIS HIS HIS HIS
SEQRES 1 K 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 K 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 K 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 K 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 K 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 K 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 K 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 K 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 K 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 K 122 HIS HIS HIS HIS HIS
SEQRES 1 L 122 SER ASP ALA VAL SER SER ASP ARG ASN PHE PRO ASN SER
SEQRES 2 L 122 THR ASN LEU PRO ARG ASN PRO SER MET ALA ASP TYR GLU
SEQRES 3 L 122 ALA ARG ILE PHE THR PHE GLY THR TRP ILE TYR SER VAL
SEQRES 4 L 122 ASN LYS GLU GLN LEU ALA ARG ALA GLY PHE TYR ALA LEU
SEQRES 5 L 122 GLY GLU GLY ASP LYS VAL LYS CYS PHE HIS CYS GLY GLY
SEQRES 6 L 122 GLY LEU THR ASP TRP LYS PRO SER GLU ASP PRO TRP GLU
SEQRES 7 L 122 GLN HIS ALA LYS TRP TYR PRO GLY CYS LYS TYR LEU LEU
SEQRES 8 L 122 GLU GLN LYS GLY GLN GLU TYR ILE ASN ASN ILE HIS LEU
SEQRES 9 L 122 THR HIS SER LEU GLU GLU CYS LEU VAL ARG THR THR HIS
SEQRES 10 L 122 HIS HIS HIS HIS HIS
HET ZN A 401 1
HET 0O6 A 402 86
HET P33 A 403 22
HET ZN B 401 1
HET 0O6 B 402 86
HET ZN C 401 1
HET ZN D 401 1
HET 0O6 D 402 86
HET P33 D 403 22
HET ZN E 401 1
HET 0O6 E 402 86
HET 2PE E 403 28
HET 0O6 J 401 86
HET ZN J 402 1
HET P33 J 403 22
HET ZN F 401 1
HET ZN G 401 1
HET 2PE G 402 28
HET ZN K 401 1
HET ZN L 401 1
HETNAM ZN ZINC ION
HETNAM 0O6 (3S,6S,7S,9AS,3'S,6'S,7'S,9A'S)-N,N'-(BENZENE-1,4-
HETNAM 2 0O6 DIYLBIS{BUTANE-4,1-DIYL-1H-1,2,3-TRIAZOLE-1,4-
HETNAM 3 0O6 DIYL[(S)-PHENYLMETHANEDIYL]})BIS[7-(HYDROXYMETHYL)-6-
HETNAM 4 0O6 {[(2S)-2-(METHYLAMINO)BUTANOYL]AMINO}-5-OXOOCTAHYDRO-
HETNAM 5 0O6 1H-PYRROLO[1,2-A]AZEPINE-3-CARBOXAMIDE]
HETNAM P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL
HETNAM 2PE NONAETHYLENE GLYCOL
HETSYN P33 HEPTAETHYLENE GLYCOL; PEG330
FORMUL 11 ZN 10(ZN 2+)
FORMUL 12 0O6 5(C64 H88 N14 O8)
FORMUL 13 P33 3(C14 H30 O8)
FORMUL 22 2PE 2(C18 H38 O10)
FORMUL 31 HOH *96(H2 O)
HELIX 1 1 ASN A 259 ALA A 263 5 5
HELIX 2 2 ASP A 264 PHE A 270 1 7
HELIX 3 3 THR A 271 GLY A 273 5 3
HELIX 4 4 ASN A 280 ALA A 287 1 8
HELIX 5 5 ASP A 315 TYR A 324 1 10
HELIX 6 6 CYS A 327 GLY A 335 1 9
HELIX 7 7 GLY A 335 SER A 347 1 13
HELIX 8 8 SER A 347 LEU A 352 1 6
HELIX 9 9 ASN B 259 ALA B 263 5 5
HELIX 10 10 ASP B 264 THR B 271 1 8
HELIX 11 11 PHE B 272 TRP B 275 5 4
HELIX 12 12 ASN B 280 ALA B 287 1 8
HELIX 13 13 ASP B 315 TYR B 324 1 10
HELIX 14 14 CYS B 327 VAL B 353 1 27
HELIX 15 15 ASN C 259 ALA C 263 5 5
HELIX 16 16 ASP C 264 ILE C 269 1 6
HELIX 17 17 ASN C 280 ALA C 285 1 6
HELIX 18 18 ASP C 315 TYR C 324 1 10
HELIX 19 19 CYS C 327 CYS C 351 1 25
HELIX 20 20 ASN D 259 ALA D 263 5 5
HELIX 21 21 ASP D 264 THR D 271 1 8
HELIX 22 22 ASN D 280 ALA D 287 1 8
HELIX 23 23 ASP D 315 TYR D 324 1 10
HELIX 24 24 CYS D 327 LEU D 352 1 26
HELIX 25 25 ASN E 259 ALA E 263 5 5
HELIX 26 26 ASP E 264 PHE E 270 1 7
HELIX 27 27 THR E 271 GLY E 273 5 3
HELIX 28 28 ASN E 280 ALA E 287 1 8
HELIX 29 29 ASP E 315 TYR E 324 1 10
HELIX 30 30 CYS E 327 LEU E 352 1 26
HELIX 31 31 ASN J 259 ALA J 263 5 5
HELIX 32 32 ASP J 264 ILE J 269 1 6
HELIX 33 33 PHE J 270 GLY J 273 5 4
HELIX 34 34 ASN J 280 ALA J 287 1 8
HELIX 35 35 ASP J 315 TYR J 324 1 10
HELIX 36 36 CYS J 327 CYS J 351 1 25
HELIX 37 37 ASN F 259 ALA F 263 5 5
HELIX 38 38 ASP F 264 PHE F 270 1 7
HELIX 39 39 THR F 271 THR F 274 5 4
HELIX 40 40 ASN F 280 ALA F 287 1 8
HELIX 41 41 ASP F 315 TYR F 324 1 10
HELIX 42 42 CYS F 327 GLU F 350 1 24
HELIX 43 43 ASP G 264 ARG G 268 5 5
HELIX 44 44 ASN G 280 GLY G 288 1 9
HELIX 45 45 ASP G 315 TYR G 324 1 10
HELIX 46 46 CYS G 327 GLU G 350 1 24
HELIX 47 47 ASN K 259 ALA K 263 5 5
HELIX 48 48 ASP K 264 PHE K 270 1 7
HELIX 49 49 ASN K 280 ARG K 286 1 7
HELIX 50 50 ASP K 315 TYR K 324 1 10
HELIX 51 51 CYS K 327 GLY K 335 1 9
HELIX 52 52 GLY K 335 CYS K 351 1 17
HELIX 53 53 ASN L 259 ALA L 263 5 5
HELIX 54 54 ASP L 264 PHE L 270 1 7
HELIX 55 55 ASN L 280 ALA L 285 1 6
HELIX 56 56 ASP L 315 TYR L 324 1 10
HELIX 57 57 CYS L 327 GLU L 332 1 6
HELIX 58 58 LYS L 334 CYS L 351 1 18
SHEET 1 A 3 PHE A 289 ALA A 291 0
SHEET 2 A 3 VAL A 298 CYS A 300 -1 O LYS A 299 N TYR A 290
SHEET 3 A 3 GLY A 306 LEU A 307 -1 O LEU A 307 N VAL A 298
SHEET 1 B 3 PHE B 289 ALA B 291 0
SHEET 2 B 3 VAL B 298 CYS B 300 -1 O LYS B 299 N TYR B 290
SHEET 3 B 3 GLY B 306 LEU B 307 -1 O LEU B 307 N VAL B 298
SHEET 1 C 3 PHE C 289 ALA C 291 0
SHEET 2 C 3 VAL C 298 CYS C 300 -1 O LYS C 299 N TYR C 290
SHEET 3 C 3 GLY C 306 LEU C 307 -1 O LEU C 307 N VAL C 298
SHEET 1 D 3 PHE D 289 ALA D 291 0
SHEET 2 D 3 VAL D 298 CYS D 300 -1 O LYS D 299 N TYR D 290
SHEET 3 D 3 GLY D 306 LEU D 307 -1 O LEU D 307 N VAL D 298
SHEET 1 E 3 PHE E 289 ALA E 291 0
SHEET 2 E 3 VAL E 298 CYS E 300 -1 O LYS E 299 N TYR E 290
SHEET 3 E 3 GLY E 306 LEU E 307 -1 O LEU E 307 N VAL E 298
SHEET 1 F 3 PHE J 289 ALA J 291 0
SHEET 2 F 3 VAL J 298 CYS J 300 -1 O LYS J 299 N TYR J 290
SHEET 3 F 3 GLY J 306 LEU J 307 -1 O LEU J 307 N VAL J 298
SHEET 1 G 3 PHE F 289 ALA F 291 0
SHEET 2 G 3 VAL F 298 CYS F 300 -1 O LYS F 299 N TYR F 290
SHEET 3 G 3 GLY F 306 LEU F 307 -1 O LEU F 307 N VAL F 298
SHEET 1 H 3 PHE G 289 ALA G 291 0
SHEET 2 H 3 VAL G 298 CYS G 300 -1 O LYS G 299 N TYR G 290
SHEET 3 H 3 GLY G 306 LEU G 307 -1 O LEU G 307 N VAL G 298
SHEET 1 I 3 PHE K 289 ALA K 291 0
SHEET 2 I 3 VAL K 298 CYS K 300 -1 O LYS K 299 N TYR K 290
SHEET 3 I 3 GLY K 306 LEU K 307 -1 O LEU K 307 N VAL K 298
SHEET 1 J 3 PHE L 289 ALA L 291 0
SHEET 2 J 3 VAL L 298 CYS L 300 -1 O LYS L 299 N TYR L 290
SHEET 3 J 3 GLY L 306 LEU L 307 -1 O LEU L 307 N VAL L 298
SSBOND 1 CYS A 351 CYS J 351 1555 1555 2.05
SSBOND 2 CYS E 351 CYS G 351 1555 1555 2.03
LINK SG CYS A 300 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 303 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 320 ZN ZN A 401 1555 1555 2.15
LINK SG CYS A 327 ZN ZN A 401 1555 1555 2.32
LINK SG CYS B 300 ZN ZN B 401 1555 1555 2.32
LINK SG CYS B 303 ZN ZN B 401 1555 1555 2.40
LINK NE2 HIS B 320 ZN ZN B 401 1555 1555 2.14
LINK SG CYS B 327 ZN ZN B 401 1555 1555 2.33
LINK SG CYS C 300 ZN ZN C 401 1555 1555 2.33
LINK SG CYS C 303 ZN ZN C 401 1555 1555 2.30
LINK NE2 HIS C 320 ZN ZN C 401 1555 1555 2.14
LINK SG CYS C 327 ZN ZN C 401 1555 1555 2.44
LINK SG CYS D 300 ZN ZN D 401 1555 1555 2.34
LINK SG CYS D 303 ZN ZN D 401 1555 1555 2.34
LINK NE2 HIS D 320 ZN ZN D 401 1555 1555 2.13
LINK SG CYS D 327 ZN ZN D 401 1555 1555 2.30
LINK SG CYS E 300 ZN ZN E 401 1555 1555 2.31
LINK SG CYS E 303 ZN ZN E 401 1555 1555 2.32
LINK NE2 HIS E 320 ZN ZN E 401 1555 1555 2.14
LINK SG CYS E 327 ZN ZN E 401 1555 1555 2.32
LINK SG CYS J 300 ZN ZN J 402 1555 1555 2.31
LINK SG CYS J 303 ZN ZN J 402 1555 1555 2.31
LINK NE2 HIS J 320 ZN ZN J 402 1555 1555 2.14
LINK SG CYS J 327 ZN ZN J 402 1555 1555 2.30
LINK SG CYS F 300 ZN ZN F 401 1555 1555 2.34
LINK SG CYS F 303 ZN ZN F 401 1555 1555 2.33
LINK NE2 HIS F 320 ZN ZN F 401 1555 1555 2.13
LINK SG CYS F 327 ZN ZN F 401 1555 1555 2.32
LINK SG CYS G 300 ZN ZN G 401 1555 1555 2.33
LINK SG CYS G 303 ZN ZN G 401 1555 1555 2.33
LINK NE2 HIS G 320 ZN ZN G 401 1555 1555 2.15
LINK SG CYS G 327 ZN ZN G 401 1555 1555 2.33
LINK SG CYS K 300 ZN ZN K 401 1555 1555 2.34
LINK SG CYS K 303 ZN ZN K 401 1555 1555 2.33
LINK NE2 HIS K 320 ZN ZN K 401 1555 1555 2.14
LINK SG CYS K 327 ZN ZN K 401 1555 1555 2.38
LINK SG CYS L 300 ZN ZN L 401 1555 1555 2.33
LINK SG CYS L 303 ZN ZN L 401 1555 1555 2.34
LINK NE2 HIS L 320 ZN ZN L 401 1555 1555 2.13
LINK SG CYS L 327 ZN ZN L 401 1555 1555 2.32
CISPEP 1 LEU D 352 VAL D 353 0 -2.03
CISPEP 2 LEU J 352 VAL J 353 0 -5.13
CISPEP 3 ARG F 248 ASN F 249 0 -3.80
CISPEP 4 CYS K 351 LEU K 352 0 -2.23
CISPEP 5 LEU L 352 VAL L 353 0 -9.80
SITE 1 AC1 4 CYS A 300 CYS A 303 HIS A 320 CYS A 327
SITE 1 AC2 25 ASN A 249 LYS A 297 GLY A 306 LEU A 307
SITE 2 AC2 25 THR A 308 ASP A 309 TRP A 310 LYS A 311
SITE 3 AC2 25 GLU A 314 GLN A 319 TRP A 323 ARG F 248
SITE 4 AC2 25 ASN F 249 LEU F 292 LYS F 297 GLY F 306
SITE 5 AC2 25 LEU F 307 THR F 308 ASP F 309 TRP F 310
SITE 6 AC2 25 LYS F 311 GLU F 314 GLN F 319 TRP F 323
SITE 7 AC2 25 TYR F 324
SITE 1 AC3 6 TRP A 323 PRO A 325 HIS A 343 TRP F 323
SITE 2 AC3 6 PRO F 325 HIS F 343
SITE 1 AC4 4 CYS B 300 CYS B 303 HIS B 320 CYS B 327
SITE 1 AC5 22 ASN B 249 GLY B 306 LEU B 307 THR B 308
SITE 2 AC5 22 ASP B 309 TRP B 310 GLU B 314 GLN B 319
SITE 3 AC5 22 TRP B 323 TYR B 324 ASN G 249 LEU G 292
SITE 4 AC5 22 GLY G 306 LEU G 307 THR G 308 ASP G 309
SITE 5 AC5 22 TRP G 310 LYS G 311 GLU G 314 GLN G 319
SITE 6 AC5 22 TRP G 323 TYR G 324
SITE 1 AC6 4 CYS C 300 CYS C 303 HIS C 320 CYS C 327
SITE 1 AC7 4 CYS D 300 CYS D 303 HIS D 320 CYS D 327
SITE 1 AC8 20 ASN D 249 GLY D 306 LEU D 307 THR D 308
SITE 2 AC8 20 ASP D 309 GLU D 314 GLN D 319 TRP D 323
SITE 3 AC8 20 TYR D 324 ASN K 249 LEU K 292 GLY K 306
SITE 4 AC8 20 LEU K 307 THR K 308 ASP K 309 TRP K 310
SITE 5 AC8 20 GLU K 314 GLN K 319 TRP K 323 TYR K 324
SITE 1 AC9 3 TRP D 323 ASN D 340 TRP K 323
SITE 1 BC1 4 CYS E 300 CYS E 303 HIS E 320 CYS E 327
SITE 1 BC2 20 ASN E 249 LYS E 299 GLY E 306 LEU E 307
SITE 2 BC2 20 THR E 308 ASP E 309 GLU E 314 GLN E 319
SITE 3 BC2 20 TRP E 323 TYR E 324 ASN L 249 GLY L 306
SITE 4 BC2 20 LEU L 307 THR L 308 ASP L 309 TRP L 310
SITE 5 BC2 20 GLU L 314 GLN L 319 TRP L 323 TYR L 324
SITE 1 BC3 7 TRP E 323 ASN E 340 HIS E 343 SER E 347
SITE 2 BC3 7 SER L 253 TRP L 323 HIS L 343
SITE 1 BC4 22 ASN C 249 LEU C 292 GLY C 306 LEU C 307
SITE 2 BC4 22 THR C 308 ASP C 309 TRP C 310 LYS C 311
SITE 3 BC4 22 GLU C 314 GLN C 319 TRP C 323 TYR C 324
SITE 4 BC4 22 ASN J 249 GLY J 306 LEU J 307 THR J 308
SITE 5 BC4 22 ASP J 309 GLU J 314 GLN J 319 TRP J 323
SITE 6 BC4 22 TYR J 324 P33 J 403
SITE 1 BC5 4 CYS J 300 CYS J 303 HIS J 320 CYS J 327
SITE 1 BC6 5 TRP C 323 ASN J 340 HIS J 343 LEU J 344
SITE 2 BC6 5 0O6 J 401
SITE 1 BC7 4 CYS F 300 CYS F 303 HIS F 320 CYS F 327
SITE 1 BC8 4 CYS G 300 CYS G 303 HIS G 320 CYS G 327
SITE 1 BC9 7 TRP B 323 PRO B 325 HIS B 343 TRP G 323
SITE 2 BC9 7 PRO G 325 ASN G 340 LEU G 344
SITE 1 CC1 4 CYS K 300 CYS K 303 HIS K 320 CYS K 327
SITE 1 CC2 4 CYS L 300 CYS L 303 HIS L 320 CYS L 327
CRYST1 65.420 130.490 215.730 90.00 90.00 90.00 P 21 21 21 40
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 0.015286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004635 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
