HEADER LIGASE/LIGASE INHIBITOR 30-NOV-12 4I7D
TITLE SIAH1 BOUND TO SYNTHETIC PEPTIDE (ACE)KLRPVAMVRP(PRK)VR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE SIAH1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 90-282);
COMPND 5 SYNONYM: SEVEN IN ABSENTIA HOMOLOG 1, SIAH-1, SIAH-1A;
COMPND 6 EC: 6.3.2.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN PHYLLOPOD;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: SIAH-BINDING PEPTIDE (UNP RESIDUES 113-125);
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HUMSIAH, SIAH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 14 ORGANISM_COMMON: FRUIT FLY;
SOURCE 15 ORGANISM_TAXID: 7227
KEYWDS SINA, BETA SANDWICH, ZINC FINGER, UBIQUITIN LIGASE, COVALENT
KEYWDS 2 INHIBITOR, LIGASE-LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SANTELLI,J.L.STEBBINS,Y.FENG,S.K.DE,A.PURVES,K.MOTAMEDCHABOKI,B.WU,
AUTHOR 2 Z.A.RONAI,R.C.LIDDINGTON,M.PELLECCHIA
REVDAT 3 20-SEP-23 4I7D 1 REMARK SEQADV LINK
REVDAT 2 11-SEP-13 4I7D 1 JRNL
REVDAT 1 14-AUG-13 4I7D 0
JRNL AUTH J.L.STEBBINS,E.SANTELLI,Y.FENG,S.K.DE,A.PURVES,
JRNL AUTH 2 K.MOTAMEDCHABOKI,B.WU,Z.A.RONAI,R.C.LIDDINGTON,M.PELLECCHIA
JRNL TITL STRUCTURE-BASED DESIGN OF COVALENT SIAH INHIBITORS.
JRNL REF CHEM.BIOL. V. 20 973 2013
JRNL REFN ISSN 1074-5521
JRNL PMID 23891150
JRNL DOI 10.1016/J.CHEMBIOL.2013.06.008
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 27176
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1390
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1770
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3180
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.59
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.217
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.165
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3267 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2224 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4419 ; 1.030 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5418 ; 0.780 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 398 ; 5.224 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;34.498 ;23.851
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 551 ;12.046 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.941 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 488 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3603 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 667 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 156 A 282
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6450 20.9010 65.7670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.0916
REMARK 3 T33: 0.0215 T12: -0.0102
REMARK 3 T13: 0.0006 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 2.0339 L22: 4.0761
REMARK 3 L33: 2.3073 L12: 0.3427
REMARK 3 L13: -0.0939 L23: -0.6826
REMARK 3 S TENSOR
REMARK 3 S11: 0.1128 S12: 0.2351 S13: 0.0163
REMARK 3 S21: -0.0362 S22: -0.0901 S23: -0.0561
REMARK 3 S31: 0.2670 S32: 0.0665 S33: -0.0227
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 112 B 125
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5930 14.7070 63.7750
REMARK 3 T TENSOR
REMARK 3 T11: 0.1860 T22: 0.2028
REMARK 3 T33: 0.2232 T12: 0.1325
REMARK 3 T13: 0.0537 T23: 0.1120
REMARK 3 L TENSOR
REMARK 3 L11: 10.1132 L22: 15.2510
REMARK 3 L33: 14.3001 L12: 6.3454
REMARK 3 L13: 5.9282 L23: 8.2795
REMARK 3 S TENSOR
REMARK 3 S11: 0.1278 S12: 0.4661 S13: -0.1154
REMARK 3 S21: -0.3270 S22: 0.2126 S23: -0.4180
REMARK 3 S31: 0.0645 S32: 0.5346 S33: -0.3404
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 156 C 282
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1040 42.8610 58.5280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0582 T22: 0.1005
REMARK 3 T33: 0.0711 T12: -0.0531
REMARK 3 T13: -0.0303 T23: 0.0726
REMARK 3 L TENSOR
REMARK 3 L11: 2.3213 L22: 3.0671
REMARK 3 L33: 2.7247 L12: -0.1985
REMARK 3 L13: -0.6664 L23: -0.8521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0272 S12: -0.0009 S13: 0.0111
REMARK 3 S21: -0.1845 S22: 0.1016 S23: 0.1939
REMARK 3 S31: -0.1107 S32: -0.0204 S33: -0.0744
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 112 D 125
REMARK 3 ORIGIN FOR THE GROUP (A): -33.7630 50.0200 61.6850
REMARK 3 T TENSOR
REMARK 3 T11: 0.1713 T22: 0.1220
REMARK 3 T33: 0.2959 T12: 0.0918
REMARK 3 T13: 0.0014 T23: 0.0906
REMARK 3 L TENSOR
REMARK 3 L11: 6.1515 L22: 3.5197
REMARK 3 L33: 15.5949 L12: 2.7944
REMARK 3 L13: 1.6288 L23: 0.7974
REMARK 3 S TENSOR
REMARK 3 S11: 0.1204 S12: -0.3507 S13: 0.0901
REMARK 3 S21: -0.0215 S22: 0.0315 S23: 0.4959
REMARK 3 S31: -0.2415 S32: -0.6431 S33: -0.1519
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 : A 125 A 155
REMARK 3 RESIDUE RANGE : A 601 A 601
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4060 2.6540 71.2240
REMARK 3 T TENSOR
REMARK 3 T11: 0.4001 T22: 0.0453
REMARK 3 T33: 0.3744 T12: -0.0219
REMARK 3 T13: -0.0487 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 13.3026 L22: 9.7804
REMARK 3 L33: 9.0476 L12: -0.7974
REMARK 3 L13: -5.6661 L23: 2.0071
REMARK 3 S TENSOR
REMARK 3 S11: -0.1428 S12: 0.1523 S13: -1.7071
REMARK 3 S21: 0.0970 S22: -0.3742 S23: 0.5945
REMARK 3 S31: 0.6558 S32: 0.0460 S33: 0.5170
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 : C 125 C 155
REMARK 3 RESIDUE RANGE : C 601 C 601
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8420 57.5780 45.8790
REMARK 3 T TENSOR
REMARK 3 T11: 0.2048 T22: 0.1625
REMARK 3 T33: 0.1806 T12: 0.0228
REMARK 3 T13: 0.0110 T23: 0.1448
REMARK 3 L TENSOR
REMARK 3 L11: 5.8825 L22: 7.4790
REMARK 3 L33: 5.8393 L12: 3.2008
REMARK 3 L13: -0.4030 L23: 0.0738
REMARK 3 S TENSOR
REMARK 3 S11: 0.3770 S12: 0.5452 S13: 0.5777
REMARK 3 S21: 0.0023 S22: -0.1814 S23: 0.3430
REMARK 3 S31: -0.6449 S32: -0.0944 S33: -0.1957
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 : A 91 A 124
REMARK 3 RESIDUE RANGE : A 602 A 602
REMARK 3 ORIGIN FOR THE GROUP (A): -47.7480 9.2580 79.4680
REMARK 3 T TENSOR
REMARK 3 T11: 0.3530 T22: 0.2375
REMARK 3 T33: 0.1407 T12: -0.1216
REMARK 3 T13: 0.0658 T23: 0.0650
REMARK 3 L TENSOR
REMARK 3 L11: 11.7993 L22: 4.7580
REMARK 3 L33: 6.6625 L12: -2.6691
REMARK 3 L13: -3.7340 L23: 1.6732
REMARK 3 S TENSOR
REMARK 3 S11: 0.3735 S12: 0.6374 S13: 0.9769
REMARK 3 S21: -0.8026 S22: -0.0858 S23: -0.4723
REMARK 3 S31: -0.8750 S32: 0.2005 S33: -0.2877
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 : C 92 C 124
REMARK 3 RESIDUE RANGE : C 602 C 602
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5220 49.8280 35.8990
REMARK 3 T TENSOR
REMARK 3 T11: 0.3788 T22: 0.3710
REMARK 3 T33: 0.3906 T12: -0.0820
REMARK 3 T13: 0.1089 T23: 0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 25.2191 L22: 5.4093
REMARK 3 L33: 12.8046 L12: -10.9747
REMARK 3 L13: -11.9098 L23: 7.1313
REMARK 3 S TENSOR
REMARK 3 S11: 0.0689 S12: 0.7801 S13: -1.1574
REMARK 3 S21: 0.2111 S22: -0.3973 S23: 0.4095
REMARK 3 S31: 0.5724 S32: -1.0730 S33: 0.3284
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4I7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27179
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.66200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2A25 CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 65% MPD, 100 MM BICINE, PH 9.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 80.48850
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 80.48850
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 80.48850
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 80.48850
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 80.48850
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 80.48850
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 80.48850
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 80.48850
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 80.48850
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 80.48850
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 80.48850
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 80.48850
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 80.48850
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 80.48850
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 80.48850
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 80.48850
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 80.48850
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 80.48850
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 80.48850
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 80.48850
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 80.48850
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 80.48850
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 80.48850
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 80.48850
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 80.48850
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 80.48850
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 701 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE MODIFIED PROTEIN PHYLLOPOD PEPTIDE BI-117F7 IS OLIGOPEPTIDE, A
REMARK 400 MEMBER OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: MODIFIED PROTEIN PHYLLOPOD PEPTIDE BI-117F7
REMARK 400 CHAIN: B, 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 GLY A 87
REMARK 465 SER A 88
REMARK 465 HIS A 89
REMARK 465 VAL A 90
REMARK 465 LYS A 198
REMARK 465 TYR A 199
REMARK 465 ASP A 200
REMARK 465 GLY A 201
REMARK 465 HIS A 202
REMARK 465 GLY C 87
REMARK 465 SER C 88
REMARK 465 HIS C 89
REMARK 465 VAL C 90
REMARK 465 ALA C 91
REMARK 465 TYR C 199
REMARK 465 ASP C 200
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 CYS A 256 -175.46 -173.41
REMARK 500 SER C 154 113.83 -24.20
REMARK 500 CYS C 256 -176.00 -176.26
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 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 98 SG
REMARK 620 2 CYS A 105 SG 112.1
REMARK 620 3 HIS A 117 NE2 102.4 105.0
REMARK 620 4 CYS A 121 SG 113.5 110.2 113.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 128 SG
REMARK 620 2 CYS A 135 SG 114.8
REMARK 620 3 HIS A 147 NE2 109.4 98.2
REMARK 620 4 HIS A 152 NE2 106.4 118.9 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 98 SG
REMARK 620 2 CYS C 105 SG 112.5
REMARK 620 3 HIS C 117 NE2 104.9 102.8
REMARK 620 4 CYS C 121 SG 109.4 111.9 115.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 128 SG
REMARK 620 2 CYS C 135 SG 116.5
REMARK 620 3 HIS C 147 NE2 91.5 114.4
REMARK 620 4 HIS C 152 NE2 105.9 118.6 106.3
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 ACE B 112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE D 112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF PROTEIN PHYLLOPOD
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF PROTEIN PHYLLOPOD
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K2F RELATED DB: PDB
REMARK 900 RELATED ID: 2A25 RELATED DB: PDB
REMARK 900 RELATED ID: 2AN6 RELATED DB: PDB
REMARK 900 RELATED ID: 4I7B RELATED DB: PDB
REMARK 900 RELATED ID: 4I7C RELATED DB: PDB
DBREF 4I7D A 90 282 UNP Q8IUQ4 SIAH1_HUMAN 90 282
DBREF 4I7D B 113 125 UNP Q27934 PHYL_DROME 113 125
DBREF 4I7D C 90 282 UNP Q8IUQ4 SIAH1_HUMAN 90 282
DBREF 4I7D D 113 125 UNP Q27934 PHYL_DROME 113 125
SEQADV 4I7D GLY A 87 UNP Q8IUQ4 EXPRESSION TAG
SEQADV 4I7D SER A 88 UNP Q8IUQ4 EXPRESSION TAG
SEQADV 4I7D HIS A 89 UNP Q8IUQ4 EXPRESSION TAG
SEQADV 4I7D ACE B 112 UNP Q27934 ACETYLATION
SEQADV 4I7D PRK B 123 UNP Q27934 THR 123 ENGINEERED MUTATION
SEQADV 4I7D GLY C 87 UNP Q8IUQ4 EXPRESSION TAG
SEQADV 4I7D SER C 88 UNP Q8IUQ4 EXPRESSION TAG
SEQADV 4I7D HIS C 89 UNP Q8IUQ4 EXPRESSION TAG
SEQADV 4I7D ACE D 112 UNP Q27934 ACETYLATION
SEQADV 4I7D PRK D 123 UNP Q27934 THR 123 ENGINEERED MUTATION
SEQRES 1 A 196 GLY SER HIS VAL ALA ASN SER VAL LEU PHE PRO CYS LYS
SEQRES 2 A 196 TYR ALA SER SER GLY CYS GLU ILE THR LEU PRO HIS THR
SEQRES 3 A 196 GLU LYS ALA ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO
SEQRES 4 A 196 TYR SER CYS PRO CYS PRO GLY ALA SER CYS LYS TRP GLN
SEQRES 5 A 196 GLY SER LEU ASP ALA VAL MET PRO HIS LEU MET HIS GLN
SEQRES 6 A 196 HIS LYS SER ILE THR THR LEU GLN GLY GLU ASP ILE VAL
SEQRES 7 A 196 PHE LEU ALA THR ASP ILE ASN LEU PRO GLY ALA VAL ASP
SEQRES 8 A 196 TRP VAL MET MET GLN SER CYS PHE GLY PHE HIS PHE MET
SEQRES 9 A 196 LEU VAL LEU GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN
SEQRES 10 A 196 GLN PHE PHE ALA ILE VAL GLN LEU ILE GLY THR ARG LYS
SEQRES 11 A 196 GLN ALA GLU ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY
SEQRES 12 A 196 HIS ARG ARG ARG LEU THR TRP GLU ALA THR PRO ARG SER
SEQRES 13 A 196 ILE HIS GLU GLY ILE ALA THR ALA ILE MET ASN SER ASP
SEQRES 14 A 196 CYS LEU VAL PHE ASP THR SER ILE ALA GLN LEU PHE ALA
SEQRES 15 A 196 GLU ASN GLY ASN LEU GLY ILE ASN VAL THR ILE SER MET
SEQRES 16 A 196 CYS
SEQRES 1 B 14 ACE LYS LEU ARG PRO VAL ALA MET VAL ARG PRO PRK VAL
SEQRES 2 B 14 ARG
SEQRES 1 C 196 GLY SER HIS VAL ALA ASN SER VAL LEU PHE PRO CYS LYS
SEQRES 2 C 196 TYR ALA SER SER GLY CYS GLU ILE THR LEU PRO HIS THR
SEQRES 3 C 196 GLU LYS ALA ASP HIS GLU GLU LEU CYS GLU PHE ARG PRO
SEQRES 4 C 196 TYR SER CYS PRO CYS PRO GLY ALA SER CYS LYS TRP GLN
SEQRES 5 C 196 GLY SER LEU ASP ALA VAL MET PRO HIS LEU MET HIS GLN
SEQRES 6 C 196 HIS LYS SER ILE THR THR LEU GLN GLY GLU ASP ILE VAL
SEQRES 7 C 196 PHE LEU ALA THR ASP ILE ASN LEU PRO GLY ALA VAL ASP
SEQRES 8 C 196 TRP VAL MET MET GLN SER CYS PHE GLY PHE HIS PHE MET
SEQRES 9 C 196 LEU VAL LEU GLU LYS GLN GLU LYS TYR ASP GLY HIS GLN
SEQRES 10 C 196 GLN PHE PHE ALA ILE VAL GLN LEU ILE GLY THR ARG LYS
SEQRES 11 C 196 GLN ALA GLU ASN PHE ALA TYR ARG LEU GLU LEU ASN GLY
SEQRES 12 C 196 HIS ARG ARG ARG LEU THR TRP GLU ALA THR PRO ARG SER
SEQRES 13 C 196 ILE HIS GLU GLY ILE ALA THR ALA ILE MET ASN SER ASP
SEQRES 14 C 196 CYS LEU VAL PHE ASP THR SER ILE ALA GLN LEU PHE ALA
SEQRES 15 C 196 GLU ASN GLY ASN LEU GLY ILE ASN VAL THR ILE SER MET
SEQRES 16 C 196 CYS
SEQRES 1 D 14 ACE LYS LEU ARG PRO VAL ALA MET VAL ARG PRO PRK VAL
SEQRES 2 D 14 ARG
MODRES 4I7D PRK B 123 LYS N~6~-PROPANOYL-L-LYSINE
MODRES 4I7D PRK D 123 LYS N~6~-PROPANOYL-L-LYSINE
HET ACE B 112 3
HET PRK B 123 13
HET ACE D 112 3
HET PRK D 123 13
HET ZN A 601 1
HET ZN A 602 1
HET MPD A 603 8
HET ZN C 601 1
HET ZN C 602 1
HETNAM ACE ACETYL GROUP
HETNAM PRK N~6~-PROPANOYL-L-LYSINE
HETNAM ZN ZINC ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN PRK N(6)-PROPIONYLLYSINE
FORMUL 2 ACE 2(C2 H4 O)
FORMUL 2 PRK 2(C9 H18 N2 O3)
FORMUL 5 ZN 4(ZN 2+)
FORMUL 7 MPD C6 H14 O2
FORMUL 10 HOH *144(H2 O)
HELIX 1 1 LYS A 99 GLY A 104 5 6
HELIX 2 2 PRO A 110 THR A 112 5 3
HELIX 3 3 GLU A 113 CYS A 121 1 9
HELIX 4 4 SER A 140 ASP A 142 5 3
HELIX 5 5 ALA A 143 HIS A 152 1 10
HELIX 6 6 THR A 214 GLU A 219 1 6
HELIX 7 7 ILE A 247 ASN A 253 1 7
HELIX 8 8 THR A 261 ALA A 268 1 8
HELIX 9 9 TYR C 100 GLY C 104 5 5
HELIX 10 10 GLU C 113 CYS C 121 1 9
HELIX 11 11 SER C 140 ASP C 142 5 3
HELIX 12 12 ALA C 143 HIS C 152 1 10
HELIX 13 13 THR C 214 GLU C 219 1 6
HELIX 14 14 ILE C 247 ASN C 253 1 7
HELIX 15 15 THR C 261 ALA C 268 1 8
SHEET 1 A 2 PHE A 96 PRO A 97 0
SHEET 2 A 2 THR A 108 LEU A 109 -1 O LEU A 109 N PHE A 96
SHEET 1 B 2 TYR A 126 SER A 127 0
SHEET 2 B 2 GLN A 138 GLY A 139 -1 O GLY A 139 N TYR A 126
SHEET 1 C 5 THR A 156 GLN A 159 0
SHEET 2 C 5 VAL A 176 CYS A 184 1 O MET A 181 N THR A 156
SHEET 3 C 5 PHE A 187 GLN A 196 -1 O LYS A 195 N VAL A 176
SHEET 4 C 5 GLN A 204 LEU A 211 -1 O PHE A 206 N GLU A 194
SHEET 5 C 5 LEU A 257 ASP A 260 -1 O PHE A 259 N PHE A 205
SHEET 1 D 5 ARG A 241 SER A 242 0
SHEET 2 D 5 GLN A 204 LEU A 211 1 N LEU A 211 O ARG A 241
SHEET 3 D 5 PHE A 187 GLN A 196 -1 N GLU A 194 O PHE A 206
SHEET 4 D 5 VAL A 176 CYS A 184 -1 N VAL A 176 O LYS A 195
SHEET 5 D 5 PRK B 123 VAL B 124 -1 O PRK B 123 N ASP A 177
SHEET 1 E10 VAL B 117 VAL B 120 0
SHEET 2 E10 ASP A 162 ALA A 167 1 N LEU A 166 O VAL B 120
SHEET 3 E10 LEU A 273 MET A 281 -1 O ILE A 275 N PHE A 165
SHEET 4 E10 PHE A 221 GLY A 229 -1 N ALA A 222 O SER A 280
SHEET 5 E10 ARG A 232 ALA A 238 -1 O TRP A 236 N LEU A 225
SHEET 6 E10 ARG C 232 ALA C 238 -1 O THR C 235 N THR A 235
SHEET 7 E10 PHE C 221 GLY C 229 -1 N TYR C 223 O ALA C 238
SHEET 8 E10 LEU C 273 MET C 281 -1 O SER C 280 N ALA C 222
SHEET 9 E10 ASP C 162 ALA C 167 -1 N PHE C 165 O ILE C 275
SHEET 10 E10 VAL D 117 VAL D 120 1 O ALA D 118 N VAL C 164
SHEET 1 F 2 PHE C 96 PRO C 97 0
SHEET 2 F 2 THR C 108 LEU C 109 -1 O LEU C 109 N PHE C 96
SHEET 1 G 2 TYR C 126 SER C 127 0
SHEET 2 G 2 GLN C 138 GLY C 139 -1 O GLY C 139 N TYR C 126
SHEET 1 H 5 THR C 157 GLN C 159 0
SHEET 2 H 5 VAL C 176 CYS C 184 1 O SER C 183 N LEU C 158
SHEET 3 H 5 PHE C 187 GLU C 197 -1 O LEU C 191 N MET C 180
SHEET 4 H 5 GLN C 203 LEU C 211 -1 O PHE C 206 N GLU C 194
SHEET 5 H 5 LEU C 257 ASP C 260 -1 O PHE C 259 N PHE C 205
SHEET 1 I 5 ARG C 241 SER C 242 0
SHEET 2 I 5 GLN C 203 LEU C 211 1 N LEU C 211 O ARG C 241
SHEET 3 I 5 PHE C 187 GLU C 197 -1 N GLU C 194 O PHE C 206
SHEET 4 I 5 VAL C 176 CYS C 184 -1 N MET C 180 O LEU C 191
SHEET 5 I 5 PRK D 123 VAL D 124 -1 O PRK D 123 N ASP C 177
LINK SG CYS A 130 CAA PRK B 123 1555 1555 1.77
LINK C ACE B 112 N LYS B 113 1555 1555 1.34
LINK C PRO B 122 N PRK B 123 1555 1555 1.33
LINK C PRK B 123 N VAL B 124 1555 1555 1.33
LINK SG CYS C 130 CAA PRK D 123 1555 1555 1.77
LINK C ACE D 112 N LYS D 113 1555 1555 1.33
LINK C PRO D 122 N PRK D 123 1555 1555 1.33
LINK C PRK D 123 N VAL D 124 1555 1555 1.33
LINK SG CYS A 98 ZN ZN A 602 1555 1555 2.32
LINK SG CYS A 105 ZN ZN A 602 1555 1555 2.25
LINK NE2 HIS A 117 ZN ZN A 602 1555 1555 2.04
LINK SG CYS A 121 ZN ZN A 602 1555 1555 2.36
LINK SG CYS A 128 ZN ZN A 601 1555 1555 2.27
LINK SG CYS A 135 ZN ZN A 601 1555 1555 2.14
LINK NE2 HIS A 147 ZN ZN A 601 1555 1555 2.02
LINK NE2 HIS A 152 ZN ZN A 601 1555 1555 2.24
LINK SG CYS C 98 ZN ZN C 602 1555 1555 2.28
LINK SG CYS C 105 ZN ZN C 602 1555 1555 2.29
LINK NE2 HIS C 117 ZN ZN C 602 1555 1555 2.00
LINK SG CYS C 121 ZN ZN C 602 1555 1555 2.33
LINK SG CYS C 128 ZN ZN C 601 1555 1555 2.29
LINK SG CYS C 135 ZN ZN C 601 1555 1555 2.30
LINK NE2 HIS C 147 ZN ZN C 601 1555 1555 2.11
LINK NE2 HIS C 152 ZN ZN C 601 1555 1555 2.01
SITE 1 AC1 2 PRO A 97 LYS B 113
SITE 1 AC2 2 PRO C 97 LYS D 113
SITE 1 AC3 4 CYS A 128 CYS A 135 HIS A 147 HIS A 152
SITE 1 AC4 4 CYS A 98 CYS A 105 HIS A 117 CYS A 121
SITE 1 AC5 5 ARG A 231 ARG A 233 ALA C 222 ALA C 238
SITE 2 AC5 5 HOH C 732
SITE 1 AC6 4 CYS C 128 CYS C 135 HIS C 147 HIS C 152
SITE 1 AC7 4 CYS C 98 CYS C 105 HIS C 117 CYS C 121
SITE 1 AC8 31 ALA A 91 ASN A 92 SER A 93 VAL A 94
SITE 2 AC8 31 LEU A 95 PHE A 96 PRO A 97 THR A 108
SITE 3 AC8 31 CYS A 130 LEU A 158 ASP A 162 ILE A 163
SITE 4 AC8 31 VAL A 164 PHE A 165 LEU A 166 THR A 168
SITE 5 AC8 31 LEU A 172 VAL A 176 ASP A 177 TRP A 178
SITE 6 AC8 31 VAL A 179 MET A 180 GLU A 194 ARG A 224
SITE 7 AC8 31 VAL A 277 THR A 278 ACE B 112 HOH B 201
SITE 8 AC8 31 HOH B 202 HOH B 203 HOH B 204
SITE 1 AC9 33 SER A 134 ASN C 92 SER C 93 VAL C 94
SITE 2 AC9 33 LEU C 95 PHE C 96 THR C 108 CYS C 130
SITE 3 AC9 33 PRO C 131 THR C 156 LEU C 158 GLN C 159
SITE 4 AC9 33 GLU C 161 ASP C 162 ILE C 163 VAL C 164
SITE 5 AC9 33 PHE C 165 LEU C 166 THR C 168 PRO C 173
SITE 6 AC9 33 ALA C 175 VAL C 176 ASP C 177 TRP C 178
SITE 7 AC9 33 VAL C 179 GLU C 194 GLU C 197 ACE D 112
SITE 8 AC9 33 HOH D 201 HOH D 202 HOH D 203 HOH D 204
SITE 9 AC9 33 HOH D 205
CRYST1 160.977 160.977 160.977 90.00 90.00 90.00 I 2 3 48
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 0.006212 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006212 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
