HEADER HYDROLASE 21-AUG-06 2I47
TITLE CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF TACE WITH INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADAM 17;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: TACE, A DISINTEGRIN AND METALLOPROTEINASE DOMAIN 17, TNF-
COMPND 6 ALPHA-CONVERTING ENZYME, TNF-ALPHA CONVERTASE, SNAKE VENOM-LIKE
COMPND 7 PROTEASE, CD156B ANTIGEN;
COMPND 8 EC: 3.4.24.86;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TACE/ADAM-17, TACE-INHIBITOR COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XU,J.S.CONDON,F.E.LOVERING
REVDAT 5 20-OCT-21 2I47 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2I47 1 VERSN
REVDAT 3 24-FEB-09 2I47 1 VERSN
REVDAT 2 09-JAN-07 2I47 1 JRNL
REVDAT 1 05-DEC-06 2I47 0
JRNL AUTH J.S.CONDON,D.JOSEPH-MCCARTHY,J.I.LEVIN,H.G.LOMBART,
JRNL AUTH 2 F.E.LOVERING,L.SUN,W.WANG,W.XU,Y.ZHANG
JRNL TITL IDENTIFICATION OF POTENT AND SELECTIVE TACE INHIBITORS VIA
JRNL TITL 2 THE S1 POCKET.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 34 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17064892
JRNL DOI 10.1016/J.BMCL.2006.10.004
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 89581
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 SET) : 0.198
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4528
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2542
REMARK 3 BIN FREE R VALUE : 0.2599
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 67
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8078
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 716
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2I47 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000039115.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105942
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 20% ISOPROPANOL, 0.1M
REMARK 280 SODIUM CITRATE, PH 5.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.09650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 VAL A 212
REMARK 465 LYS A 213
REMARK 465 ARG A 214
REMARK 465 ARG A 215
REMARK 465 ALA A 216
REMARK 465 ASP A 217
REMARK 465 PRO A 218
REMARK 465 ASP A 219
REMARK 465 ASN A 475
REMARK 465 LYS A 476
REMARK 465 VAL A 477
REMARK 465 CYS A 478
REMARK 465 GLY A 479
REMARK 465 ASN A 480
REMARK 465 SER A 481
REMARK 465 ARG A 482
REMARK 465 VAL A 483
REMARK 465 ASP A 484
REMARK 465 GLU A 485
REMARK 465 GLY A 486
REMARK 465 GLU A 487
REMARK 465 GLU A 488
REMARK 465 CYS A 489
REMARK 465 ASP A 490
REMARK 465 PRO A 491
REMARK 465 GLY A 492
REMARK 465 SER A 493
REMARK 465 HIS A 494
REMARK 465 HIS A 495
REMARK 465 HIS A 496
REMARK 465 HIS A 497
REMARK 465 HIS A 498
REMARK 465 HIS A 499
REMARK 465 VAL B 212
REMARK 465 LYS B 213
REMARK 465 ARG B 214
REMARK 465 ARG B 215
REMARK 465 ALA B 216
REMARK 465 ASP B 217
REMARK 465 PRO B 218
REMARK 465 ASP B 219
REMARK 465 PRO B 220
REMARK 465 ASN B 475
REMARK 465 LYS B 476
REMARK 465 VAL B 477
REMARK 465 CYS B 478
REMARK 465 GLY B 479
REMARK 465 ASN B 480
REMARK 465 SER B 481
REMARK 465 ARG B 482
REMARK 465 VAL B 483
REMARK 465 ASP B 484
REMARK 465 GLU B 485
REMARK 465 GLY B 486
REMARK 465 GLU B 487
REMARK 465 GLU B 488
REMARK 465 CYS B 489
REMARK 465 ASP B 490
REMARK 465 PRO B 491
REMARK 465 GLY B 492
REMARK 465 SER B 493
REMARK 465 HIS B 494
REMARK 465 HIS B 495
REMARK 465 HIS B 496
REMARK 465 HIS B 497
REMARK 465 HIS B 498
REMARK 465 HIS B 499
REMARK 465 VAL C 212
REMARK 465 LYS C 213
REMARK 465 ARG C 214
REMARK 465 ARG C 215
REMARK 465 ALA C 216
REMARK 465 ASP C 217
REMARK 465 PRO C 218
REMARK 465 ASP C 219
REMARK 465 PRO C 220
REMARK 465 ASN C 475
REMARK 465 LYS C 476
REMARK 465 VAL C 477
REMARK 465 CYS C 478
REMARK 465 GLY C 479
REMARK 465 ASN C 480
REMARK 465 SER C 481
REMARK 465 ARG C 482
REMARK 465 VAL C 483
REMARK 465 ASP C 484
REMARK 465 GLU C 485
REMARK 465 GLY C 486
REMARK 465 GLU C 487
REMARK 465 GLU C 488
REMARK 465 CYS C 489
REMARK 465 ASP C 490
REMARK 465 PRO C 491
REMARK 465 GLY C 492
REMARK 465 SER C 493
REMARK 465 HIS C 494
REMARK 465 HIS C 495
REMARK 465 HIS C 496
REMARK 465 HIS C 497
REMARK 465 HIS C 498
REMARK 465 HIS C 499
REMARK 465 VAL D 212
REMARK 465 LYS D 213
REMARK 465 ARG D 214
REMARK 465 ARG D 215
REMARK 465 ALA D 216
REMARK 465 ASP D 217
REMARK 465 PRO D 218
REMARK 465 ASP D 219
REMARK 465 ASN D 475
REMARK 465 LYS D 476
REMARK 465 VAL D 477
REMARK 465 CYS D 478
REMARK 465 GLY D 479
REMARK 465 ASN D 480
REMARK 465 SER D 481
REMARK 465 ARG D 482
REMARK 465 VAL D 483
REMARK 465 ASP D 484
REMARK 465 GLU D 485
REMARK 465 GLY D 486
REMARK 465 GLU D 487
REMARK 465 GLU D 488
REMARK 465 CYS D 489
REMARK 465 ASP D 490
REMARK 465 PRO D 491
REMARK 465 GLY D 492
REMARK 465 SER D 493
REMARK 465 HIS D 494
REMARK 465 HIS D 495
REMARK 465 HIS D 496
REMARK 465 HIS D 497
REMARK 465 HIS D 498
REMARK 465 HIS D 499
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 270 -114.13 -135.63
REMARK 500 TRP A 312 160.31 -44.43
REMARK 500 CYS A 365 123.66 77.72
REMARK 500 ALA A 368 142.43 -36.69
REMARK 500 VAL A 373 -34.84 141.18
REMARK 500 LEU A 380 35.70 -94.42
REMARK 500 ASN A 381 51.84 -93.90
REMARK 500 LYS B 222 80.61 -69.48
REMARK 500 ALA B 270 -125.08 -146.45
REMARK 500 TRP B 312 160.43 -47.76
REMARK 500 ASN B 359 44.93 -108.35
REMARK 500 CYS B 365 120.69 74.88
REMARK 500 ASN B 381 52.83 -91.05
REMARK 500 LYS B 448 34.56 -97.37
REMARK 500 CYS B 469 -6.11 -151.90
REMARK 500 ALA C 270 -114.53 -137.93
REMARK 500 CYS C 365 119.27 78.48
REMARK 500 LEU C 420 87.40 -17.54
REMARK 500 ALA C 421 129.57 177.46
REMARK 500 ALA D 270 -109.37 -148.10
REMARK 500 ASN D 359 54.58 -106.53
REMARK 500 CYS D 365 122.37 80.29
REMARK 500 ASN D 381 55.05 -92.48
REMARK 500 LEU D 420 89.44 55.04
REMARK 500 ALA D 421 -121.03 59.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TRP A 312 ASP A 313 146.52
REMARK 500 LEU B 227 LEU B 228 149.13
REMARK 500 TRP B 312 ASP B 313 145.34
REMARK 500 TRP C 312 ASP C 313 145.77
REMARK 500 GLY C 419 LEU C 420 -146.40
REMARK 500 TRP D 312 ASP D 313 146.02
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 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 405 NE2
REMARK 620 2 HIS A 409 NE2 98.6
REMARK 620 3 HIS A 415 NE2 102.0 98.6
REMARK 620 4 INN A 901 O4 104.1 86.2 152.5
REMARK 620 5 INN A 901 O 110.1 149.7 85.1 77.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 405 NE2
REMARK 620 2 HIS B 409 NE2 102.2
REMARK 620 3 HIS B 415 NE2 107.4 101.1
REMARK 620 4 INN B 902 O 106.2 149.1 82.1
REMARK 620 5 INN B 902 O4 101.8 86.7 147.2 75.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 804 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 405 NE2
REMARK 620 2 HIS C 409 NE2 97.8
REMARK 620 3 HIS C 415 NE2 108.8 100.5
REMARK 620 4 KGY C1001 O35 103.8 95.3 141.2
REMARK 620 5 KGY C1001 O19 108.7 153.6 72.9 77.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 803 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 405 NE2
REMARK 620 2 HIS D 409 NE2 97.1
REMARK 620 3 HIS D 415 NE2 110.1 98.2
REMARK 620 4 KGY D1002 O19 108.3 154.3 77.3
REMARK 620 5 KGY D1002 O35 101.4 92.4 145.1 78.9
REMARK 620 N 1 2 3 4
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ENZYME INHIBITOR
REMARK 630 MOLECULE NAME: N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4-
REMARK 630 METHYLPENTANOYL}-3-METHYL-L-VALYL-N-(2-AMINOETHYL)-L-ALANINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 INN A 901
REMARK 630 INN B 902
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: 2HM TBG ALA EDN
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INN A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INN B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KGY C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KGY D 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A8H RELATED DB: PDB
REMARK 900 TACE CATALYTIC DOMAIN WITH INHIBITOR
REMARK 900 RELATED ID: 1BKC RELATED DB: PDB
REMARK 900 TACE CATALYTIC DOMAIN WITH TAPI
DBREF 2I47 A 212 492 UNP P78536 ADA17_HUMAN 212 492
DBREF 2I47 B 212 492 UNP P78536 ADA17_HUMAN 212 492
DBREF 2I47 C 212 492 UNP P78536 ADA17_HUMAN 212 492
DBREF 2I47 D 212 492 UNP P78536 ADA17_HUMAN 212 492
SEQADV 2I47 ALA A 266 UNP P78536 SER 266 ENGINEERED MUTATION
SEQADV 2I47 GLN A 452 UNP P78536 ASN 452 ENGINEERED MUTATION
SEQADV 2I47 SER A 493 UNP P78536 CLONING ARTIFACT
SEQADV 2I47 HIS A 494 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS A 495 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS A 496 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS A 497 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS A 498 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS A 499 UNP P78536 EXPRESSION TAG
SEQADV 2I47 ALA B 266 UNP P78536 SER 266 ENGINEERED MUTATION
SEQADV 2I47 GLN B 452 UNP P78536 ASN 452 ENGINEERED MUTATION
SEQADV 2I47 SER B 493 UNP P78536 CLONING ARTIFACT
SEQADV 2I47 HIS B 494 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS B 495 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS B 496 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS B 497 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS B 498 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS B 499 UNP P78536 EXPRESSION TAG
SEQADV 2I47 ALA C 266 UNP P78536 SER 266 ENGINEERED MUTATION
SEQADV 2I47 GLN C 452 UNP P78536 ASN 452 ENGINEERED MUTATION
SEQADV 2I47 SER C 493 UNP P78536 CLONING ARTIFACT
SEQADV 2I47 HIS C 494 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS C 495 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS C 496 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS C 497 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS C 498 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS C 499 UNP P78536 EXPRESSION TAG
SEQADV 2I47 ALA D 266 UNP P78536 SER 266 ENGINEERED MUTATION
SEQADV 2I47 GLN D 452 UNP P78536 ASN 452 ENGINEERED MUTATION
SEQADV 2I47 SER D 493 UNP P78536 CLONING ARTIFACT
SEQADV 2I47 HIS D 494 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS D 495 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS D 496 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS D 497 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS D 498 UNP P78536 EXPRESSION TAG
SEQADV 2I47 HIS D 499 UNP P78536 EXPRESSION TAG
SEQRES 1 A 288 VAL LYS ARG ARG ALA ASP PRO ASP PRO MET LYS ASN THR
SEQRES 2 A 288 CYS LYS LEU LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG
SEQRES 3 A 288 TYR MET GLY ARG GLY GLU GLU SER THR THR THR ASN TYR
SEQRES 4 A 288 LEU ILE GLU LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG
SEQRES 5 A 288 ASN THR ALA TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY
SEQRES 6 A 288 ILE GLN ILE GLU GLN ILE ARG ILE LEU LYS SER PRO GLN
SEQRES 7 A 288 GLU VAL LYS PRO GLY GLU LYS HIS TYR ASN MET ALA LYS
SEQRES 8 A 288 SER TYR PRO ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS
SEQRES 9 A 288 MET LEU LEU GLU GLN PHE SER PHE ASP ILE ALA GLU GLU
SEQRES 10 A 288 ALA SER LYS VAL CYS LEU ALA HIS LEU PHE THR TYR GLN
SEQRES 11 A 288 ASP PHE ASP MET GLY THR LEU GLY LEU ALA TYR VAL GLY
SEQRES 12 A 288 SER PRO ARG ALA ASN SER HIS GLY GLY VAL CYS PRO LYS
SEQRES 13 A 288 ALA TYR TYR SER PRO VAL GLY LYS LYS ASN ILE TYR LEU
SEQRES 14 A 288 ASN SER GLY LEU THR SER THR LYS ASN TYR GLY LYS THR
SEQRES 15 A 288 ILE LEU THR LYS GLU ALA ASP LEU VAL THR THR HIS GLU
SEQRES 16 A 288 LEU GLY HIS ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY
SEQRES 17 A 288 LEU ALA GLU CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS
SEQRES 18 A 288 TYR VAL MET TYR PRO ILE ALA VAL SER GLY ASP HIS GLU
SEQRES 19 A 288 ASN ASN LYS MET PHE SER GLN CYS SER LYS GLN SER ILE
SEQRES 20 A 288 TYR LYS THR ILE GLU SER LYS ALA GLN GLU CYS PHE GLN
SEQRES 21 A 288 GLU ARG SER ASN LYS VAL CYS GLY ASN SER ARG VAL ASP
SEQRES 22 A 288 GLU GLY GLU GLU CYS ASP PRO GLY SER HIS HIS HIS HIS
SEQRES 23 A 288 HIS HIS
SEQRES 1 B 288 VAL LYS ARG ARG ALA ASP PRO ASP PRO MET LYS ASN THR
SEQRES 2 B 288 CYS LYS LEU LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG
SEQRES 3 B 288 TYR MET GLY ARG GLY GLU GLU SER THR THR THR ASN TYR
SEQRES 4 B 288 LEU ILE GLU LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG
SEQRES 5 B 288 ASN THR ALA TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY
SEQRES 6 B 288 ILE GLN ILE GLU GLN ILE ARG ILE LEU LYS SER PRO GLN
SEQRES 7 B 288 GLU VAL LYS PRO GLY GLU LYS HIS TYR ASN MET ALA LYS
SEQRES 8 B 288 SER TYR PRO ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS
SEQRES 9 B 288 MET LEU LEU GLU GLN PHE SER PHE ASP ILE ALA GLU GLU
SEQRES 10 B 288 ALA SER LYS VAL CYS LEU ALA HIS LEU PHE THR TYR GLN
SEQRES 11 B 288 ASP PHE ASP MET GLY THR LEU GLY LEU ALA TYR VAL GLY
SEQRES 12 B 288 SER PRO ARG ALA ASN SER HIS GLY GLY VAL CYS PRO LYS
SEQRES 13 B 288 ALA TYR TYR SER PRO VAL GLY LYS LYS ASN ILE TYR LEU
SEQRES 14 B 288 ASN SER GLY LEU THR SER THR LYS ASN TYR GLY LYS THR
SEQRES 15 B 288 ILE LEU THR LYS GLU ALA ASP LEU VAL THR THR HIS GLU
SEQRES 16 B 288 LEU GLY HIS ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY
SEQRES 17 B 288 LEU ALA GLU CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS
SEQRES 18 B 288 TYR VAL MET TYR PRO ILE ALA VAL SER GLY ASP HIS GLU
SEQRES 19 B 288 ASN ASN LYS MET PHE SER GLN CYS SER LYS GLN SER ILE
SEQRES 20 B 288 TYR LYS THR ILE GLU SER LYS ALA GLN GLU CYS PHE GLN
SEQRES 21 B 288 GLU ARG SER ASN LYS VAL CYS GLY ASN SER ARG VAL ASP
SEQRES 22 B 288 GLU GLY GLU GLU CYS ASP PRO GLY SER HIS HIS HIS HIS
SEQRES 23 B 288 HIS HIS
SEQRES 1 C 288 VAL LYS ARG ARG ALA ASP PRO ASP PRO MET LYS ASN THR
SEQRES 2 C 288 CYS LYS LEU LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG
SEQRES 3 C 288 TYR MET GLY ARG GLY GLU GLU SER THR THR THR ASN TYR
SEQRES 4 C 288 LEU ILE GLU LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG
SEQRES 5 C 288 ASN THR ALA TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY
SEQRES 6 C 288 ILE GLN ILE GLU GLN ILE ARG ILE LEU LYS SER PRO GLN
SEQRES 7 C 288 GLU VAL LYS PRO GLY GLU LYS HIS TYR ASN MET ALA LYS
SEQRES 8 C 288 SER TYR PRO ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS
SEQRES 9 C 288 MET LEU LEU GLU GLN PHE SER PHE ASP ILE ALA GLU GLU
SEQRES 10 C 288 ALA SER LYS VAL CYS LEU ALA HIS LEU PHE THR TYR GLN
SEQRES 11 C 288 ASP PHE ASP MET GLY THR LEU GLY LEU ALA TYR VAL GLY
SEQRES 12 C 288 SER PRO ARG ALA ASN SER HIS GLY GLY VAL CYS PRO LYS
SEQRES 13 C 288 ALA TYR TYR SER PRO VAL GLY LYS LYS ASN ILE TYR LEU
SEQRES 14 C 288 ASN SER GLY LEU THR SER THR LYS ASN TYR GLY LYS THR
SEQRES 15 C 288 ILE LEU THR LYS GLU ALA ASP LEU VAL THR THR HIS GLU
SEQRES 16 C 288 LEU GLY HIS ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY
SEQRES 17 C 288 LEU ALA GLU CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS
SEQRES 18 C 288 TYR VAL MET TYR PRO ILE ALA VAL SER GLY ASP HIS GLU
SEQRES 19 C 288 ASN ASN LYS MET PHE SER GLN CYS SER LYS GLN SER ILE
SEQRES 20 C 288 TYR LYS THR ILE GLU SER LYS ALA GLN GLU CYS PHE GLN
SEQRES 21 C 288 GLU ARG SER ASN LYS VAL CYS GLY ASN SER ARG VAL ASP
SEQRES 22 C 288 GLU GLY GLU GLU CYS ASP PRO GLY SER HIS HIS HIS HIS
SEQRES 23 C 288 HIS HIS
SEQRES 1 D 288 VAL LYS ARG ARG ALA ASP PRO ASP PRO MET LYS ASN THR
SEQRES 2 D 288 CYS LYS LEU LEU VAL VAL ALA ASP HIS ARG PHE TYR ARG
SEQRES 3 D 288 TYR MET GLY ARG GLY GLU GLU SER THR THR THR ASN TYR
SEQRES 4 D 288 LEU ILE GLU LEU ILE ASP ARG VAL ASP ASP ILE TYR ARG
SEQRES 5 D 288 ASN THR ALA TRP ASP ASN ALA GLY PHE LYS GLY TYR GLY
SEQRES 6 D 288 ILE GLN ILE GLU GLN ILE ARG ILE LEU LYS SER PRO GLN
SEQRES 7 D 288 GLU VAL LYS PRO GLY GLU LYS HIS TYR ASN MET ALA LYS
SEQRES 8 D 288 SER TYR PRO ASN GLU GLU LYS ASP ALA TRP ASP VAL LYS
SEQRES 9 D 288 MET LEU LEU GLU GLN PHE SER PHE ASP ILE ALA GLU GLU
SEQRES 10 D 288 ALA SER LYS VAL CYS LEU ALA HIS LEU PHE THR TYR GLN
SEQRES 11 D 288 ASP PHE ASP MET GLY THR LEU GLY LEU ALA TYR VAL GLY
SEQRES 12 D 288 SER PRO ARG ALA ASN SER HIS GLY GLY VAL CYS PRO LYS
SEQRES 13 D 288 ALA TYR TYR SER PRO VAL GLY LYS LYS ASN ILE TYR LEU
SEQRES 14 D 288 ASN SER GLY LEU THR SER THR LYS ASN TYR GLY LYS THR
SEQRES 15 D 288 ILE LEU THR LYS GLU ALA ASP LEU VAL THR THR HIS GLU
SEQRES 16 D 288 LEU GLY HIS ASN PHE GLY ALA GLU HIS ASP PRO ASP GLY
SEQRES 17 D 288 LEU ALA GLU CYS ALA PRO ASN GLU ASP GLN GLY GLY LYS
SEQRES 18 D 288 TYR VAL MET TYR PRO ILE ALA VAL SER GLY ASP HIS GLU
SEQRES 19 D 288 ASN ASN LYS MET PHE SER GLN CYS SER LYS GLN SER ILE
SEQRES 20 D 288 TYR LYS THR ILE GLU SER LYS ALA GLN GLU CYS PHE GLN
SEQRES 21 D 288 GLU ARG SER ASN LYS VAL CYS GLY ASN SER ARG VAL ASP
SEQRES 22 D 288 GLU GLY GLU GLU CYS ASP PRO GLY SER HIS HIS HIS HIS
SEQRES 23 D 288 HIS HIS
HET ZN A 802 1
HET INN A 901 29
HET ZN B 801 1
HET INN B 902 29
HET ZN C 804 1
HET KGY C1001 35
HET ZN D 803 1
HET KGY D1002 35
HETNAM ZN ZINC ION
HETNAM INN N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4-
HETNAM 2 INN METHYLPENTANOYL}-3-METHYL-L-VALYL-N-(2-AMINOETHYL)-L-
HETNAM 3 INN ALANINAMIDE
HETNAM KGY 4-({[4-(BUT-2-YN-1-YLOXY)PHENYL]SULFONYL}METHYL)-1-[(3,
HETNAM 2 KGY 5-DIMETHYLISOXAZOL-4-YL)SULFONYL]-N-HYDROXYPIPERIDINE-
HETNAM 3 KGY 4-CARBOXAMIDE
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 INN 2(C19 H37 N5 O5)
FORMUL 10 KGY 2(C22 H27 N3 O8 S2)
FORMUL 13 HOH *716(H2 O)
HELIX 1 1 ASP A 232 MET A 239 1 8
HELIX 2 2 GLU A 243 ASN A 264 1 22
HELIX 3 3 ASP A 313 ILE A 325 1 13
HELIX 4 4 ILE A 325 SER A 330 1 6
HELIX 5 5 PHE A 343 THR A 347 5 5
HELIX 6 6 LEU A 395 PHE A 411 1 17
HELIX 7 7 ASN A 426 GLY A 430 5 5
HELIX 8 8 HIS A 444 MET A 449 5 6
HELIX 9 9 SER A 451 PHE A 470 1 20
HELIX 10 10 ASP B 232 MET B 239 1 8
HELIX 11 11 GLU B 243 ASN B 264 1 22
HELIX 12 12 ASP B 313 ILE B 325 1 13
HELIX 13 13 ILE B 325 SER B 330 1 6
HELIX 14 14 PHE B 343 THR B 347 5 5
HELIX 15 15 LEU B 395 PHE B 411 1 17
HELIX 16 16 SER B 451 PHE B 470 1 20
HELIX 17 17 ASP C 232 MET C 239 1 8
HELIX 18 18 GLU C 243 ASN C 264 1 22
HELIX 19 19 ASP C 313 ILE C 325 1 13
HELIX 20 20 ILE C 325 SER C 330 1 6
HELIX 21 21 PHE C 343 THR C 347 5 5
HELIX 22 22 LEU C 395 PHE C 411 1 17
HELIX 23 23 ASN C 426 GLY C 430 5 5
HELIX 24 24 HIS C 444 MET C 449 5 6
HELIX 25 25 SER C 451 PHE C 470 1 20
HELIX 26 26 ASP D 232 MET D 239 1 8
HELIX 27 27 GLU D 243 ASN D 264 1 22
HELIX 28 28 ASP D 313 SER D 330 1 18
HELIX 29 29 PHE D 343 THR D 347 5 5
HELIX 30 30 LEU D 395 PHE D 411 1 17
HELIX 31 31 ASN D 426 GLY D 430 5 5
HELIX 32 32 HIS D 444 MET D 449 5 6
HELIX 33 33 SER D 451 PHE D 470 1 20
SHEET 1 A 5 GLY A 276 ILE A 284 0
SHEET 2 A 5 THR A 224 ALA A 231 1 N LEU A 227 O GLU A 280
SHEET 3 A 5 LEU A 334 THR A 339 1 O PHE A 338 N VAL A 230
SHEET 4 A 5 SER A 382 SER A 386 1 O THR A 385 N LEU A 337
SHEET 5 A 5 GLY A 349 ALA A 351 -1 N LEU A 350 O LEU A 384
SHEET 1 B 2 TYR A 369 TYR A 370 0
SHEET 2 B 2 ASN A 377 ILE A 378 -1 O ILE A 378 N TYR A 369
SHEET 1 C 2 LYS A 388 ASN A 389 0
SHEET 2 C 2 LYS A 392 THR A 393 -1 O LYS A 392 N ASN A 389
SHEET 1 D 5 GLY B 276 ILE B 284 0
SHEET 2 D 5 THR B 224 ALA B 231 1 N LEU B 227 O GLU B 280
SHEET 3 D 5 LEU B 334 THR B 339 1 O PHE B 338 N VAL B 230
SHEET 4 D 5 SER B 382 SER B 386 1 O THR B 385 N LEU B 337
SHEET 5 D 5 GLY B 349 ALA B 351 -1 N LEU B 350 O LEU B 384
SHEET 1 E 2 TYR B 369 SER B 371 0
SHEET 2 E 2 LYS B 376 ILE B 378 -1 O LYS B 376 N SER B 371
SHEET 1 F 2 LYS B 388 ASN B 389 0
SHEET 2 F 2 LYS B 392 THR B 393 -1 O LYS B 392 N ASN B 389
SHEET 1 G 5 GLY C 276 ILE C 284 0
SHEET 2 G 5 LYS C 222 ALA C 231 1 N LEU C 227 O GLU C 280
SHEET 3 G 5 LEU C 334 THR C 339 1 O PHE C 338 N VAL C 230
SHEET 4 G 5 SER C 382 SER C 386 1 O THR C 385 N THR C 339
SHEET 5 G 5 GLY C 349 ALA C 351 -1 N LEU C 350 O LEU C 384
SHEET 1 H 3 GLY C 276 ILE C 284 0
SHEET 2 H 3 LYS C 222 ALA C 231 1 N LEU C 227 O GLU C 280
SHEET 3 H 3 GLN C 471 GLU C 472 -1 O GLN C 471 N THR C 224
SHEET 1 I 2 TYR C 369 SER C 371 0
SHEET 2 I 2 LYS C 376 ILE C 378 -1 O LYS C 376 N SER C 371
SHEET 1 J 2 LYS C 388 ASN C 389 0
SHEET 2 J 2 LYS C 392 THR C 393 -1 O LYS C 392 N ASN C 389
SHEET 1 K 5 GLY D 276 ILE D 284 0
SHEET 2 K 5 THR D 224 ALA D 231 1 N LEU D 227 O GLU D 280
SHEET 3 K 5 LEU D 334 THR D 339 1 O PHE D 338 N VAL D 230
SHEET 4 K 5 SER D 382 SER D 386 1 O THR D 385 N LEU D 337
SHEET 5 K 5 GLY D 349 ALA D 351 -1 N LEU D 350 O LEU D 384
SHEET 1 L 2 TYR D 369 TYR D 370 0
SHEET 2 L 2 ASN D 377 ILE D 378 -1 O ILE D 378 N TYR D 369
SHEET 1 M 2 LYS D 388 ASN D 389 0
SHEET 2 M 2 LYS D 392 THR D 393 -1 O LYS D 392 N ASN D 389
SSBOND 1 CYS A 225 CYS A 333 1555 1555 2.04
SSBOND 2 CYS A 365 CYS A 469 1555 1555 2.03
SSBOND 3 CYS A 423 CYS A 453 1555 1555 2.04
SSBOND 4 CYS B 225 CYS B 333 1555 1555 2.03
SSBOND 5 CYS B 365 CYS B 469 1555 1555 1.83
SSBOND 6 CYS B 423 CYS B 453 1555 1555 2.03
SSBOND 7 CYS C 225 CYS C 333 1555 1555 2.03
SSBOND 8 CYS C 365 CYS C 469 1555 1555 2.03
SSBOND 9 CYS C 423 CYS C 453 1555 1555 2.03
SSBOND 10 CYS D 225 CYS D 333 1555 1555 2.03
SSBOND 11 CYS D 365 CYS D 469 1555 1555 2.03
SSBOND 12 CYS D 423 CYS D 453 1555 1555 2.03
LINK NE2 HIS A 405 ZN ZN A 802 1555 1555 2.12
LINK NE2 HIS A 409 ZN ZN A 802 1555 1555 2.10
LINK NE2 HIS A 415 ZN ZN A 802 1555 1555 2.08
LINK ZN ZN A 802 O4 INN A 901 1555 1555 2.08
LINK ZN ZN A 802 O INN A 901 1555 1555 2.14
LINK NE2 HIS B 405 ZN ZN B 801 1555 1555 2.10
LINK NE2 HIS B 409 ZN ZN B 801 1555 1555 2.08
LINK NE2 HIS B 415 ZN ZN B 801 1555 1555 2.06
LINK ZN ZN B 801 O INN B 902 1555 1555 2.13
LINK ZN ZN B 801 O4 INN B 902 1555 1555 2.23
LINK NE2 HIS C 405 ZN ZN C 804 1555 1555 2.11
LINK NE2 HIS C 409 ZN ZN C 804 1555 1555 2.13
LINK NE2 HIS C 415 ZN ZN C 804 1555 1555 2.11
LINK ZN ZN C 804 O35 KGY C1001 1555 1555 2.34
LINK ZN ZN C 804 O19 KGY C1001 1555 1555 2.04
LINK NE2 HIS D 405 ZN ZN D 803 1555 1555 2.12
LINK NE2 HIS D 409 ZN ZN D 803 1555 1555 2.13
LINK NE2 HIS D 415 ZN ZN D 803 1555 1555 2.11
LINK ZN ZN D 803 O19 KGY D1002 1555 1555 1.95
LINK ZN ZN D 803 O35 KGY D1002 1555 1555 2.29
CISPEP 1 TYR A 304 PRO A 305 0 0.27
CISPEP 2 TYR B 304 PRO B 305 0 -0.24
CISPEP 3 TYR C 304 PRO C 305 0 -0.09
CISPEP 4 TYR D 304 PRO D 305 0 0.18
SITE 1 AC1 4 HIS B 405 HIS B 409 HIS B 415 INN B 902
SITE 1 AC2 4 HIS A 405 HIS A 409 HIS A 415 INN A 901
SITE 1 AC3 4 HIS D 405 HIS D 409 HIS D 415 KGY D1002
SITE 1 AC4 4 HIS C 405 HIS C 409 HIS C 415 KGY C1001
SITE 1 AC5 19 MET A 345 GLY A 346 THR A 347 LEU A 348
SITE 2 AC5 19 GLY A 349 ASN A 389 TYR A 390 HIS A 405
SITE 3 AC5 19 GLU A 406 HIS A 409 HIS A 415 PRO A 437
SITE 4 AC5 19 ILE A 438 ALA A 439 ZN A 802 HOH A 927
SITE 5 AC5 19 HOH A 958 HOH A 987 HOH A1098
SITE 1 AC6 17 MET B 345 GLY B 346 THR B 347 LEU B 348
SITE 2 AC6 17 GLY B 349 ASN B 389 TYR B 390 HIS B 405
SITE 3 AC6 17 GLU B 406 HIS B 409 HIS B 415 PRO B 437
SITE 4 AC6 17 ILE B 438 ALA B 439 ZN B 801 HOH B 923
SITE 5 AC6 17 HOH B 926
SITE 1 AC7 20 VAL C 314 GLY C 346 THR C 347 LEU C 348
SITE 2 AC7 20 GLY C 349 LEU C 350 GLU C 398 LEU C 401
SITE 3 AC7 20 VAL C 402 HIS C 405 GLU C 406 HIS C 409
SITE 4 AC7 20 HIS C 415 PRO C 437 ALA C 439 VAL C 440
SITE 5 AC7 20 ZN C 804 HOH C1008 HOH C1025 HOH C1144
SITE 1 AC8 18 VAL D 314 THR D 347 LEU D 348 GLY D 349
SITE 2 AC8 18 LEU D 350 GLU D 398 LEU D 401 VAL D 402
SITE 3 AC8 18 HIS D 405 GLU D 406 HIS D 409 HIS D 415
SITE 4 AC8 18 PRO D 437 ALA D 439 VAL D 440 ZN D 803
SITE 5 AC8 18 HOH D1012 HOH D1049
CRYST1 61.775 126.193 81.224 90.00 107.41 90.00 P 1 21 1 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 0.016188 0.000000 0.005076 0.00000
SCALE2 0.000000 0.007924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012903 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
