HEADER HYDROLASE 30-JUN-09 3I3T
TITLE CRYSTAL STRUCTURE OF COVALENT UBIQUITIN-USP21 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 21;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN: UNP RESIDUES 209-563;
COMPND 5 SYNONYM: UBIQUITIN THIOESTERASE 21, UBIQUITIN-SPECIFIC-PROCESSING
COMPND 6 PROTEASE 21, DEUBIQUITINATING ENZYME 21;
COMPND 7 EC: 3.1.2.15;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UBIQUITIN;
COMPND 11 CHAIN: B, D, F, H;
COMPND 12 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: PP1490, USP21, USP23;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28ALIC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2, UBQ;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET28ALIC
KEYWDS UBIQUITIN-SPECIFIC PROTEASE ACTIVITY, HYDROLASE, UBIQUITIN BIOLOGY,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, ACTIVATOR, CHROMATIN REGULATOR,
KEYWDS 3 NUCLEUS, PROTEASE, THIOL PROTEASE, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 4 REGULATION, UBL CONJUGATION PATHWAY, ISOPEPTIDE BOND, PHOSPHOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.NECULAI,G.V.AVVAKUMOV,J.R.WALKER,S.XUE,C.BUTLER-COLE,J.WEIGELT,
AUTHOR 2 C.BOUNTRA,A.M.EDWARDS,C.H.ARROWSMITH,A.BOCHKAREV,S.DHE-PAGANON,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 06-SEP-23 3I3T 1 REMARK LINK
REVDAT 2 27-FEB-13 3I3T 1 JRNL VERSN
REVDAT 1 21-JUL-09 3I3T 0
JRNL AUTH A.ERNST,G.AVVAKUMOV,J.TONG,Y.FAN,Y.ZHAO,P.ALBERTS,A.PERSAUD,
JRNL AUTH 2 J.R.WALKER,A.M.NECULAI,D.NECULAI,A.VOROBYOV,P.GARG,L.BEATTY,
JRNL AUTH 3 P.K.CHAN,Y.C.JUANG,M.C.LANDRY,C.YEH,E.ZEQIRAJ,K.KARAMBOULAS,
JRNL AUTH 4 A.ALLALI-HASSANI,M.VEDADI,M.TYERS,J.MOFFAT,F.SICHERI,
JRNL AUTH 5 L.PELLETIER,D.DUROCHER,B.RAUGHT,D.ROTIN,J.YANG,M.F.MORAN,
JRNL AUTH 6 S.DHE-PAGANON,S.S.SIDHU
JRNL TITL A STRATEGY FOR MODULATION OF ENZYMES IN THE UBIQUITIN
JRNL TITL 2 SYSTEM.
JRNL REF SCIENCE V. 339 590 2013
JRNL REFN ISSN 0036-8075
JRNL PMID 23287719
JRNL DOI 10.1126/SCIENCE.1230161
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 61793
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3293
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) : 2.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4277
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 219
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12293
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -14.90000
REMARK 3 B22 (A**2) : 13.28000
REMARK 3 B33 (A**2) : 1.62000
REMARK 3 B12 (A**2) : 5.35000
REMARK 3 B13 (A**2) : 4.35000
REMARK 3 B23 (A**2) : -24.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.055
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.519
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12578 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16924 ; 1.998 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1511 ; 7.466 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 621 ;34.513 ;23.237
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2273 ;22.173 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 121 ;22.749 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1872 ; 0.131 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9451 ; 0.008 ; 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): 7618 ; 0.978 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12282 ; 1.900 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4960 ; 2.857 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4641 ; 4.852 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C E G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 5
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 211 A 249 1
REMARK 3 1 C 211 C 249 1
REMARK 3 1 E 211 E 249 1
REMARK 3 1 G 211 G 249 1
REMARK 3 2 A 256 A 320 1
REMARK 3 2 C 256 C 320 1
REMARK 3 2 E 256 E 320 1
REMARK 3 2 G 256 G 320 1
REMARK 3 3 A 349 A 406 1
REMARK 3 3 C 349 C 406 1
REMARK 3 3 E 349 E 406 1
REMARK 3 3 G 349 G 406 1
REMARK 3 4 A 414 A 494 1
REMARK 3 4 C 414 C 494 1
REMARK 3 4 E 414 E 494 1
REMARK 3 4 G 414 G 494 1
REMARK 3 5 A 499 A 558 1
REMARK 3 5 C 499 C 558 1
REMARK 3 5 E 499 E 558 1
REMARK 3 5 G 499 G 558 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2425 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 2425 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 2425 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 G (A): 2425 ; 0.07 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 2425 ; 0.18 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 2425 ; 0.18 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 2425 ; 0.19 ; 0.50
REMARK 3 TIGHT THERMAL 1 G (A**2): 2425 ; 0.18 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D F H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 75 1
REMARK 3 1 D 1 D 75 1
REMARK 3 1 F 1 F 75 1
REMARK 3 1 H 1 H 75 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 597 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 597 ; 0.12 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 F (A): 597 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 H (A): 597 ; 0.07 ; 0.05
REMARK 3 TIGHT THERMAL 2 B (A**2): 597 ; 0.17 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 597 ; 0.18 ; 0.50
REMARK 3 TIGHT THERMAL 2 F (A**2): 597 ; 0.16 ; 0.50
REMARK 3 TIGHT THERMAL 2 H (A**2): 597 ; 0.16 ; 0.50
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.540
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, -K, -H+L
REMARK 3 TWIN FRACTION : 0.460
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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: NULL
REMARK 4
REMARK 4 3I3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000053928.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65088
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 83.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 2.540
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.56
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : 0.52900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.080
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 2IBI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 3350, 0.1 M BIS-TRIS, 0.1 M
REMARK 280 AMMONIUM SULFATE, 5 MM TCEP, PH 6.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.4 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: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.4 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 350
REMARK 350 BIOMOLECULE: 3
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: 3490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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: 4
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: 3440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 209
REMARK 465 GLY A 210
REMARK 465 PRO A 250
REMARK 465 GLY A 251
REMARK 465 GLY A 252
REMARK 465 GLY A 253
REMARK 465 ARG A 254
REMARK 465 ALA A 255
REMARK 465 GLY A 321
REMARK 465 ARG A 322
REMARK 465 ARG A 323
REMARK 465 ALA A 324
REMARK 465 PRO A 325
REMARK 465 PRO A 326
REMARK 465 ILE A 327
REMARK 465 LEU A 328
REMARK 465 ALA A 329
REMARK 465 ASN A 330
REMARK 465 GLY A 331
REMARK 465 PRO A 332
REMARK 465 VAL A 333
REMARK 465 PRO A 334
REMARK 465 SER A 335
REMARK 465 PRO A 336
REMARK 465 PRO A 337
REMARK 465 ARG A 338
REMARK 465 ARG A 339
REMARK 465 GLY A 340
REMARK 465 GLY A 341
REMARK 465 ALA A 342
REMARK 465 LEU A 343
REMARK 465 LEU A 344
REMARK 465 GLU A 345
REMARK 465 GLU A 346
REMARK 465 PRO A 347
REMARK 465 GLU A 348
REMARK 465 LYS A 407
REMARK 465 GLY A 408
REMARK 465 PHE A 409
REMARK 465 ALA A 410
REMARK 465 GLY A 411
REMARK 465 GLY A 412
REMARK 465 LYS A 413
REMARK 465 ASP A 495
REMARK 465 LYS A 496
REMARK 465 ALA A 497
REMARK 465 GLY A 498
REMARK 465 GLN A 559
REMARK 465 GLU A 560
REMARK 465 PRO A 561
REMARK 465 PRO A 562
REMARK 465 ARG A 563
REMARK 465 SER C 209
REMARK 465 GLY C 210
REMARK 465 PRO C 250
REMARK 465 GLY C 251
REMARK 465 GLY C 252
REMARK 465 GLY C 253
REMARK 465 ARG C 254
REMARK 465 ALA C 255
REMARK 465 GLY C 321
REMARK 465 ARG C 322
REMARK 465 ARG C 323
REMARK 465 ALA C 324
REMARK 465 PRO C 325
REMARK 465 PRO C 326
REMARK 465 ILE C 327
REMARK 465 LEU C 328
REMARK 465 ALA C 329
REMARK 465 ASN C 330
REMARK 465 GLY C 331
REMARK 465 PRO C 332
REMARK 465 VAL C 333
REMARK 465 PRO C 334
REMARK 465 SER C 335
REMARK 465 PRO C 336
REMARK 465 PRO C 337
REMARK 465 ARG C 338
REMARK 465 ARG C 339
REMARK 465 GLY C 340
REMARK 465 GLY C 341
REMARK 465 ALA C 342
REMARK 465 LEU C 343
REMARK 465 LEU C 344
REMARK 465 GLU C 345
REMARK 465 GLU C 346
REMARK 465 PRO C 347
REMARK 465 GLU C 348
REMARK 465 ASP C 495
REMARK 465 LYS C 496
REMARK 465 ALA C 497
REMARK 465 GLY C 498
REMARK 465 GLN C 559
REMARK 465 GLU C 560
REMARK 465 PRO C 561
REMARK 465 PRO C 562
REMARK 465 ARG C 563
REMARK 465 SER E 209
REMARK 465 GLY E 210
REMARK 465 PRO E 250
REMARK 465 GLY E 251
REMARK 465 GLY E 252
REMARK 465 GLY E 253
REMARK 465 ARG E 254
REMARK 465 ALA E 255
REMARK 465 GLY E 321
REMARK 465 ARG E 322
REMARK 465 ARG E 323
REMARK 465 ALA E 324
REMARK 465 PRO E 325
REMARK 465 PRO E 326
REMARK 465 ILE E 327
REMARK 465 LEU E 328
REMARK 465 ALA E 329
REMARK 465 ASN E 330
REMARK 465 GLY E 331
REMARK 465 PRO E 332
REMARK 465 VAL E 333
REMARK 465 PRO E 334
REMARK 465 SER E 335
REMARK 465 PRO E 336
REMARK 465 PRO E 337
REMARK 465 ARG E 338
REMARK 465 ARG E 339
REMARK 465 GLY E 340
REMARK 465 GLY E 341
REMARK 465 ALA E 342
REMARK 465 LEU E 343
REMARK 465 LEU E 344
REMARK 465 GLU E 345
REMARK 465 GLU E 346
REMARK 465 PRO E 347
REMARK 465 GLU E 348
REMARK 465 ASP E 495
REMARK 465 LYS E 496
REMARK 465 ALA E 497
REMARK 465 GLY E 498
REMARK 465 GLN E 559
REMARK 465 GLU E 560
REMARK 465 PRO E 561
REMARK 465 PRO E 562
REMARK 465 ARG E 563
REMARK 465 SER G 209
REMARK 465 GLY G 210
REMARK 465 PRO G 250
REMARK 465 GLY G 251
REMARK 465 GLY G 252
REMARK 465 GLY G 253
REMARK 465 ARG G 254
REMARK 465 ALA G 255
REMARK 465 GLY G 321
REMARK 465 ARG G 322
REMARK 465 ARG G 323
REMARK 465 ALA G 324
REMARK 465 PRO G 325
REMARK 465 PRO G 326
REMARK 465 ILE G 327
REMARK 465 LEU G 328
REMARK 465 ALA G 329
REMARK 465 ASN G 330
REMARK 465 GLY G 331
REMARK 465 PRO G 332
REMARK 465 VAL G 333
REMARK 465 PRO G 334
REMARK 465 SER G 335
REMARK 465 PRO G 336
REMARK 465 PRO G 337
REMARK 465 ARG G 338
REMARK 465 ARG G 339
REMARK 465 GLY G 340
REMARK 465 GLY G 341
REMARK 465 ALA G 342
REMARK 465 LEU G 343
REMARK 465 LEU G 344
REMARK 465 GLU G 345
REMARK 465 GLU G 346
REMARK 465 PRO G 347
REMARK 465 GLU G 348
REMARK 465 GLY G 408
REMARK 465 PHE G 409
REMARK 465 ALA G 410
REMARK 465 GLY G 411
REMARK 465 GLY G 412
REMARK 465 LYS G 413
REMARK 465 ASP G 495
REMARK 465 LYS G 496
REMARK 465 ALA G 497
REMARK 465 GLY G 498
REMARK 465 GLN G 559
REMARK 465 GLU G 560
REMARK 465 PRO G 561
REMARK 465 PRO G 562
REMARK 465 ARG G 563
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY B 75 N NEH B 76 1.56
REMARK 500 O GLY D 75 N NEH D 76 1.79
REMARK 500 SG CYS C 221 CB NEH D 76 1.80
REMARK 500 SG CYS E 221 CB NEH F 76 1.80
REMARK 500 SG CYS A 221 CB NEH B 76 1.83
REMARK 500 NE2 GLN G 503 NH1 ARG G 524 1.84
REMARK 500 SG CYS G 221 CB NEH H 76 1.85
REMARK 500 NE2 GLN E 503 NH1 ARG E 524 1.92
REMARK 500 NE2 GLN C 503 NH1 ARG C 524 1.96
REMARK 500 OE1 GLN C 256 O HOH C 86 1.97
REMARK 500 NH1 ARG E 282 NE ARG D 54 2.00
REMARK 500 N ARG A 457 O HOH A 58 2.04
REMARK 500 NE2 GLN A 503 NH1 ARG A 524 2.08
REMARK 500 OD1 ASP A 534 O HOH A 73 2.15
REMARK 500 O GLY H 75 N NEH H 76 2.15
REMARK 500 NE2 HIS D 68 O HOH D 81 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 229 CB CYS A 229 SG 0.113
REMARK 500 VAL A 545 CB VAL A 545 CG1 -0.276
REMARK 500 VAL A 545 CB VAL A 545 CG2 -0.282
REMARK 500 CYS C 523 CB CYS C 523 SG 0.105
REMARK 500 PHE E 374 CG PHE E 374 CD2 -0.128
REMARK 500 PHE E 374 CG PHE E 374 CD1 -0.148
REMARK 500 PHE E 374 CE1 PHE E 374 CZ -0.190
REMARK 500 PHE E 374 CZ PHE E 374 CE2 -0.178
REMARK 500 CYS G 525 CB CYS G 525 SG -0.103
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 235 C - N - CA ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 264 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 284 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 365 CD - NE - CZ ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG A 365 NE - CZ - NH1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG A 365 NE - CZ - NH2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 LEU A 507 CB - CA - C ANGL. DEV. = -12.8 DEGREES
REMARK 500 LEU A 507 CB - CG - CD2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 524 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 VAL A 545 CG1 - CB - CG2 ANGL. DEV. = -24.4 DEGREES
REMARK 500 PRO C 235 C - N - CA ANGL. DEV. = -11.9 DEGREES
REMARK 500 ASP C 264 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP C 399 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG E 246 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP E 264 CB - CG - OD1 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG E 365 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU E 507 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 PRO G 235 C - N - CA ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG G 243 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG G 246 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ASP G 264 CB - CG - OD1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG G 365 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG G 524 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG H 42 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 270 -73.14 -82.18
REMARK 500 TYR A 297 13.52 -140.87
REMARK 500 SER A 431 -129.86 55.20
REMARK 500 ARG A 439 -71.28 -79.55
REMARK 500 LYS A 443 56.13 -91.74
REMARK 500 SER A 469 171.64 175.67
REMARK 500 VAL A 478 114.41 -33.72
REMARK 500 ALA A 506 143.18 -175.41
REMARK 500 SER A 513 -168.57 -120.81
REMARK 500 CYS A 525 -167.63 -123.11
REMARK 500 ASP A 534 -116.31 50.25
REMARK 500 TYR A 551 -50.49 -130.07
REMARK 500 TRP C 270 -72.89 -85.47
REMARK 500 HIS C 271 77.01 -115.46
REMARK 500 ASP C 367 117.26 -160.89
REMARK 500 ALA C 410 43.33 -101.94
REMARK 500 SER C 431 -130.31 55.89
REMARK 500 SER C 469 175.98 177.76
REMARK 500 VAL C 478 114.47 -36.38
REMARK 500 ASP C 534 -112.99 49.28
REMARK 500 TYR C 551 -50.77 -125.57
REMARK 500 TRP E 270 -70.09 -86.34
REMARK 500 HIS E 271 78.44 -115.31
REMARK 500 SER E 431 -129.71 54.71
REMARK 500 ARG E 439 -72.40 -78.34
REMARK 500 LYS E 443 58.43 -90.74
REMARK 500 ARG E 470 -72.68 -65.21
REMARK 500 VAL E 478 110.10 -37.36
REMARK 500 CYS E 525 -165.19 -122.65
REMARK 500 ASP E 534 -111.88 46.21
REMARK 500 ALA G 263 -52.49 -25.06
REMARK 500 TRP G 270 -70.96 -77.97
REMARK 500 GLU G 276 132.85 -37.58
REMARK 500 TYR G 297 15.09 -140.39
REMARK 500 SER G 431 -132.01 53.78
REMARK 500 ARG G 439 -70.32 -80.39
REMARK 500 ARG G 439 -73.37 -77.90
REMARK 500 ARG G 465 53.88 -65.98
REMARK 500 ASP G 534 -117.94 50.91
REMARK 500 GLU G 542 3.32 -65.19
REMARK 500 TYR G 551 -55.93 -125.93
REMARK 500 PRO B 19 -5.70 -56.91
REMARK 500 ASN B 60 40.60 71.76
REMARK 500 LYS B 63 133.04 -39.15
REMARK 500 LEU B 71 -157.95 -108.56
REMARK 500 PRO D 19 -8.05 -59.02
REMARK 500 ASN D 60 40.45 76.63
REMARK 500 LEU D 71 -161.16 -109.38
REMARK 500 PRO F 19 -7.64 -54.13
REMARK 500 ASN F 60 39.11 73.10
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
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 700 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 384 SG
REMARK 620 2 CYS A 387 SG 114.5
REMARK 620 3 CYS A 437 SG 107.5 99.2
REMARK 620 4 CYS A 440 SG 106.1 128.4 97.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 700 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 384 SG
REMARK 620 2 CYS C 387 SG 118.6
REMARK 620 3 CYS C 437 SG 99.3 95.0
REMARK 620 4 CYS C 440 SG 107.0 131.2 93.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 700 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 384 SG
REMARK 620 2 CYS E 387 SG 126.4
REMARK 620 3 CYS E 437 SG 96.7 96.1
REMARK 620 4 CYS E 440 SG 105.3 126.9 88.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 700 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 384 SG
REMARK 620 2 CYS G 387 SG 108.5
REMARK 620 3 CYS G 437 SG 92.4 100.7
REMARK 620 4 CYS G 440 SG 101.9 139.7 104.0
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 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEH B 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEH D 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEH F 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEH H 76
DBREF 3I3T A 209 563 UNP Q9UK80 UBP21_HUMAN 209 563
DBREF 3I3T C 209 563 UNP Q9UK80 UBP21_HUMAN 209 563
DBREF 3I3T E 209 563 UNP Q9UK80 UBP21_HUMAN 209 563
DBREF 3I3T G 209 563 UNP Q9UK80 UBP21_HUMAN 209 563
DBREF 3I3T B 1 75 UNP P62988 UBIQ_HUMAN 1 75
DBREF 3I3T D 1 75 UNP P62988 UBIQ_HUMAN 1 75
DBREF 3I3T F 1 75 UNP P62988 UBIQ_HUMAN 1 75
DBREF 3I3T H 1 75 UNP P62988 UBIQ_HUMAN 1 75
SEQRES 1 A 355 SER GLY HIS VAL GLY LEU ARG ASN LEU GLY ASN THR CYS
SEQRES 2 A 355 PHE LEU ASN ALA VAL LEU GLN CYS LEU SER SER THR ARG
SEQRES 3 A 355 PRO LEU ARG ASP PHE CYS LEU ARG ARG ASP PHE ARG GLN
SEQRES 4 A 355 GLU VAL PRO GLY GLY GLY ARG ALA GLN GLU LEU THR GLU
SEQRES 5 A 355 ALA PHE ALA ASP VAL ILE GLY ALA LEU TRP HIS PRO ASP
SEQRES 6 A 355 SER CYS GLU ALA VAL ASN PRO THR ARG PHE ARG ALA VAL
SEQRES 7 A 355 PHE GLN LYS TYR VAL PRO SER PHE SER GLY TYR SER GLN
SEQRES 8 A 355 GLN ASP ALA GLN GLU PHE LEU LYS LEU LEU MET GLU ARG
SEQRES 9 A 355 LEU HIS LEU GLU ILE ASN ARG ARG GLY ARG ARG ALA PRO
SEQRES 10 A 355 PRO ILE LEU ALA ASN GLY PRO VAL PRO SER PRO PRO ARG
SEQRES 11 A 355 ARG GLY GLY ALA LEU LEU GLU GLU PRO GLU LEU SER ASP
SEQRES 12 A 355 ASP ASP ARG ALA ASN LEU MET TRP LYS ARG TYR LEU GLU
SEQRES 13 A 355 ARG GLU ASP SER LYS ILE VAL ASP LEU PHE VAL GLY GLN
SEQRES 14 A 355 LEU LYS SER CYS LEU LYS CYS GLN ALA CYS GLY TYR ARG
SEQRES 15 A 355 SER THR THR PHE GLU VAL PHE CYS ASP LEU SER LEU PRO
SEQRES 16 A 355 ILE PRO LYS LYS GLY PHE ALA GLY GLY LYS VAL SER LEU
SEQRES 17 A 355 ARG ASP CYS PHE ASN LEU PHE THR LYS GLU GLU GLU LEU
SEQRES 18 A 355 GLU SER GLU ASN ALA PRO VAL CYS ASP ARG CYS ARG GLN
SEQRES 19 A 355 LYS THR ARG SER THR LYS LYS LEU THR VAL GLN ARG PHE
SEQRES 20 A 355 PRO ARG ILE LEU VAL LEU HIS LEU ASN ARG PHE SER ALA
SEQRES 21 A 355 SER ARG GLY SER ILE LYS LYS SER SER VAL GLY VAL ASP
SEQRES 22 A 355 PHE PRO LEU GLN ARG LEU SER LEU GLY ASP PHE ALA SER
SEQRES 23 A 355 ASP LYS ALA GLY SER PRO VAL TYR GLN LEU TYR ALA LEU
SEQRES 24 A 355 CYS ASN HIS SER GLY SER VAL HIS TYR GLY HIS TYR THR
SEQRES 25 A 355 ALA LEU CYS ARG CYS GLN THR GLY TRP HIS VAL TYR ASN
SEQRES 26 A 355 ASP SER ARG VAL SER PRO VAL SER GLU ASN GLN VAL ALA
SEQRES 27 A 355 SER SER GLU GLY TYR VAL LEU PHE TYR GLN LEU MET GLN
SEQRES 28 A 355 GLU PRO PRO ARG
SEQRES 1 C 355 SER GLY HIS VAL GLY LEU ARG ASN LEU GLY ASN THR CYS
SEQRES 2 C 355 PHE LEU ASN ALA VAL LEU GLN CYS LEU SER SER THR ARG
SEQRES 3 C 355 PRO LEU ARG ASP PHE CYS LEU ARG ARG ASP PHE ARG GLN
SEQRES 4 C 355 GLU VAL PRO GLY GLY GLY ARG ALA GLN GLU LEU THR GLU
SEQRES 5 C 355 ALA PHE ALA ASP VAL ILE GLY ALA LEU TRP HIS PRO ASP
SEQRES 6 C 355 SER CYS GLU ALA VAL ASN PRO THR ARG PHE ARG ALA VAL
SEQRES 7 C 355 PHE GLN LYS TYR VAL PRO SER PHE SER GLY TYR SER GLN
SEQRES 8 C 355 GLN ASP ALA GLN GLU PHE LEU LYS LEU LEU MET GLU ARG
SEQRES 9 C 355 LEU HIS LEU GLU ILE ASN ARG ARG GLY ARG ARG ALA PRO
SEQRES 10 C 355 PRO ILE LEU ALA ASN GLY PRO VAL PRO SER PRO PRO ARG
SEQRES 11 C 355 ARG GLY GLY ALA LEU LEU GLU GLU PRO GLU LEU SER ASP
SEQRES 12 C 355 ASP ASP ARG ALA ASN LEU MET TRP LYS ARG TYR LEU GLU
SEQRES 13 C 355 ARG GLU ASP SER LYS ILE VAL ASP LEU PHE VAL GLY GLN
SEQRES 14 C 355 LEU LYS SER CYS LEU LYS CYS GLN ALA CYS GLY TYR ARG
SEQRES 15 C 355 SER THR THR PHE GLU VAL PHE CYS ASP LEU SER LEU PRO
SEQRES 16 C 355 ILE PRO LYS LYS GLY PHE ALA GLY GLY LYS VAL SER LEU
SEQRES 17 C 355 ARG ASP CYS PHE ASN LEU PHE THR LYS GLU GLU GLU LEU
SEQRES 18 C 355 GLU SER GLU ASN ALA PRO VAL CYS ASP ARG CYS ARG GLN
SEQRES 19 C 355 LYS THR ARG SER THR LYS LYS LEU THR VAL GLN ARG PHE
SEQRES 20 C 355 PRO ARG ILE LEU VAL LEU HIS LEU ASN ARG PHE SER ALA
SEQRES 21 C 355 SER ARG GLY SER ILE LYS LYS SER SER VAL GLY VAL ASP
SEQRES 22 C 355 PHE PRO LEU GLN ARG LEU SER LEU GLY ASP PHE ALA SER
SEQRES 23 C 355 ASP LYS ALA GLY SER PRO VAL TYR GLN LEU TYR ALA LEU
SEQRES 24 C 355 CYS ASN HIS SER GLY SER VAL HIS TYR GLY HIS TYR THR
SEQRES 25 C 355 ALA LEU CYS ARG CYS GLN THR GLY TRP HIS VAL TYR ASN
SEQRES 26 C 355 ASP SER ARG VAL SER PRO VAL SER GLU ASN GLN VAL ALA
SEQRES 27 C 355 SER SER GLU GLY TYR VAL LEU PHE TYR GLN LEU MET GLN
SEQRES 28 C 355 GLU PRO PRO ARG
SEQRES 1 E 355 SER GLY HIS VAL GLY LEU ARG ASN LEU GLY ASN THR CYS
SEQRES 2 E 355 PHE LEU ASN ALA VAL LEU GLN CYS LEU SER SER THR ARG
SEQRES 3 E 355 PRO LEU ARG ASP PHE CYS LEU ARG ARG ASP PHE ARG GLN
SEQRES 4 E 355 GLU VAL PRO GLY GLY GLY ARG ALA GLN GLU LEU THR GLU
SEQRES 5 E 355 ALA PHE ALA ASP VAL ILE GLY ALA LEU TRP HIS PRO ASP
SEQRES 6 E 355 SER CYS GLU ALA VAL ASN PRO THR ARG PHE ARG ALA VAL
SEQRES 7 E 355 PHE GLN LYS TYR VAL PRO SER PHE SER GLY TYR SER GLN
SEQRES 8 E 355 GLN ASP ALA GLN GLU PHE LEU LYS LEU LEU MET GLU ARG
SEQRES 9 E 355 LEU HIS LEU GLU ILE ASN ARG ARG GLY ARG ARG ALA PRO
SEQRES 10 E 355 PRO ILE LEU ALA ASN GLY PRO VAL PRO SER PRO PRO ARG
SEQRES 11 E 355 ARG GLY GLY ALA LEU LEU GLU GLU PRO GLU LEU SER ASP
SEQRES 12 E 355 ASP ASP ARG ALA ASN LEU MET TRP LYS ARG TYR LEU GLU
SEQRES 13 E 355 ARG GLU ASP SER LYS ILE VAL ASP LEU PHE VAL GLY GLN
SEQRES 14 E 355 LEU LYS SER CYS LEU LYS CYS GLN ALA CYS GLY TYR ARG
SEQRES 15 E 355 SER THR THR PHE GLU VAL PHE CYS ASP LEU SER LEU PRO
SEQRES 16 E 355 ILE PRO LYS LYS GLY PHE ALA GLY GLY LYS VAL SER LEU
SEQRES 17 E 355 ARG ASP CYS PHE ASN LEU PHE THR LYS GLU GLU GLU LEU
SEQRES 18 E 355 GLU SER GLU ASN ALA PRO VAL CYS ASP ARG CYS ARG GLN
SEQRES 19 E 355 LYS THR ARG SER THR LYS LYS LEU THR VAL GLN ARG PHE
SEQRES 20 E 355 PRO ARG ILE LEU VAL LEU HIS LEU ASN ARG PHE SER ALA
SEQRES 21 E 355 SER ARG GLY SER ILE LYS LYS SER SER VAL GLY VAL ASP
SEQRES 22 E 355 PHE PRO LEU GLN ARG LEU SER LEU GLY ASP PHE ALA SER
SEQRES 23 E 355 ASP LYS ALA GLY SER PRO VAL TYR GLN LEU TYR ALA LEU
SEQRES 24 E 355 CYS ASN HIS SER GLY SER VAL HIS TYR GLY HIS TYR THR
SEQRES 25 E 355 ALA LEU CYS ARG CYS GLN THR GLY TRP HIS VAL TYR ASN
SEQRES 26 E 355 ASP SER ARG VAL SER PRO VAL SER GLU ASN GLN VAL ALA
SEQRES 27 E 355 SER SER GLU GLY TYR VAL LEU PHE TYR GLN LEU MET GLN
SEQRES 28 E 355 GLU PRO PRO ARG
SEQRES 1 G 355 SER GLY HIS VAL GLY LEU ARG ASN LEU GLY ASN THR CYS
SEQRES 2 G 355 PHE LEU ASN ALA VAL LEU GLN CYS LEU SER SER THR ARG
SEQRES 3 G 355 PRO LEU ARG ASP PHE CYS LEU ARG ARG ASP PHE ARG GLN
SEQRES 4 G 355 GLU VAL PRO GLY GLY GLY ARG ALA GLN GLU LEU THR GLU
SEQRES 5 G 355 ALA PHE ALA ASP VAL ILE GLY ALA LEU TRP HIS PRO ASP
SEQRES 6 G 355 SER CYS GLU ALA VAL ASN PRO THR ARG PHE ARG ALA VAL
SEQRES 7 G 355 PHE GLN LYS TYR VAL PRO SER PHE SER GLY TYR SER GLN
SEQRES 8 G 355 GLN ASP ALA GLN GLU PHE LEU LYS LEU LEU MET GLU ARG
SEQRES 9 G 355 LEU HIS LEU GLU ILE ASN ARG ARG GLY ARG ARG ALA PRO
SEQRES 10 G 355 PRO ILE LEU ALA ASN GLY PRO VAL PRO SER PRO PRO ARG
SEQRES 11 G 355 ARG GLY GLY ALA LEU LEU GLU GLU PRO GLU LEU SER ASP
SEQRES 12 G 355 ASP ASP ARG ALA ASN LEU MET TRP LYS ARG TYR LEU GLU
SEQRES 13 G 355 ARG GLU ASP SER LYS ILE VAL ASP LEU PHE VAL GLY GLN
SEQRES 14 G 355 LEU LYS SER CYS LEU LYS CYS GLN ALA CYS GLY TYR ARG
SEQRES 15 G 355 SER THR THR PHE GLU VAL PHE CYS ASP LEU SER LEU PRO
SEQRES 16 G 355 ILE PRO LYS LYS GLY PHE ALA GLY GLY LYS VAL SER LEU
SEQRES 17 G 355 ARG ASP CYS PHE ASN LEU PHE THR LYS GLU GLU GLU LEU
SEQRES 18 G 355 GLU SER GLU ASN ALA PRO VAL CYS ASP ARG CYS ARG GLN
SEQRES 19 G 355 LYS THR ARG SER THR LYS LYS LEU THR VAL GLN ARG PHE
SEQRES 20 G 355 PRO ARG ILE LEU VAL LEU HIS LEU ASN ARG PHE SER ALA
SEQRES 21 G 355 SER ARG GLY SER ILE LYS LYS SER SER VAL GLY VAL ASP
SEQRES 22 G 355 PHE PRO LEU GLN ARG LEU SER LEU GLY ASP PHE ALA SER
SEQRES 23 G 355 ASP LYS ALA GLY SER PRO VAL TYR GLN LEU TYR ALA LEU
SEQRES 24 G 355 CYS ASN HIS SER GLY SER VAL HIS TYR GLY HIS TYR THR
SEQRES 25 G 355 ALA LEU CYS ARG CYS GLN THR GLY TRP HIS VAL TYR ASN
SEQRES 26 G 355 ASP SER ARG VAL SER PRO VAL SER GLU ASN GLN VAL ALA
SEQRES 27 G 355 SER SER GLU GLY TYR VAL LEU PHE TYR GLN LEU MET GLN
SEQRES 28 G 355 GLU PRO PRO ARG
SEQRES 1 B 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 1 D 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 1 F 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 F 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 F 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 F 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 F 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 F 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 1 H 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 H 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 H 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 H 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 H 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 H 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
HET ZN A 700 1
HET ZN C 700 1
HET ZN E 700 1
HET ZN G 700 1
HET NEH B 76 3
HET NEH D 76 3
HET NEH F 76 3
HET NEH H 76 3
HETNAM ZN ZINC ION
HETNAM NEH ETHANAMINE
FORMUL 9 ZN 4(ZN 2+)
FORMUL 13 NEH 4(C2 H7 N)
FORMUL 17 HOH *121(H2 O)
HELIX 1 1 THR A 220 SER A 232 1 13
HELIX 2 2 THR A 233 ARG A 243 1 11
HELIX 3 3 ASP A 244 VAL A 249 1 6
HELIX 4 4 GLN A 256 LEU A 269 1 14
HELIX 5 5 PRO A 280 VAL A 291 1 12
HELIX 6 6 PRO A 292 SER A 295 5 4
HELIX 7 7 ALA A 302 ASN A 318 1 17
HELIX 8 8 SER A 350 GLU A 366 1 17
HELIX 9 9 SER A 368 VAL A 375 1 8
HELIX 10 10 SER A 415 LYS A 425 1 11
HELIX 11 11 GLU A 430 ALA A 434 5 5
HELIX 12 12 GLY A 490 ALA A 493 5 4
HELIX 13 13 SER A 541 SER A 547 1 7
HELIX 14 14 THR C 220 SER C 232 1 13
HELIX 15 15 THR C 233 ARG C 243 1 11
HELIX 16 16 ASP C 244 GLU C 248 5 5
HELIX 17 17 GLN C 256 LEU C 269 1 14
HELIX 18 18 PRO C 280 VAL C 291 1 12
HELIX 19 19 PRO C 292 SER C 295 5 4
HELIX 20 20 ASP C 301 ASN C 318 1 18
HELIX 21 21 SER C 350 GLU C 366 1 17
HELIX 22 22 SER C 368 VAL C 375 1 8
HELIX 23 23 SER C 415 LYS C 425 1 11
HELIX 24 24 GLU C 430 ALA C 434 5 5
HELIX 25 25 GLY C 490 ALA C 493 5 4
HELIX 26 26 SER C 541 SER C 547 1 7
HELIX 27 27 THR E 220 SER E 232 1 13
HELIX 28 28 THR E 233 ARG E 242 1 10
HELIX 29 29 ASP E 244 VAL E 249 1 6
HELIX 30 30 GLN E 256 LEU E 269 1 14
HELIX 31 31 PRO E 280 VAL E 291 1 12
HELIX 32 32 PRO E 292 SER E 295 5 4
HELIX 33 33 ALA E 302 ASN E 318 1 17
HELIX 34 34 SER E 350 GLU E 366 1 17
HELIX 35 35 SER E 368 VAL E 375 1 8
HELIX 36 36 SER E 415 LYS E 425 1 11
HELIX 37 37 GLU E 430 ALA E 434 5 5
HELIX 38 38 GLY E 490 ALA E 493 5 4
HELIX 39 39 SER E 541 SER E 547 1 7
HELIX 40 40 THR G 220 SER G 232 1 13
HELIX 41 41 THR G 233 ARG G 242 1 10
HELIX 42 42 ASP G 244 VAL G 249 1 6
HELIX 43 43 GLN G 256 LEU G 269 1 14
HELIX 44 44 PRO G 280 VAL G 291 1 12
HELIX 45 45 PRO G 292 SER G 295 5 4
HELIX 46 46 ASP G 301 ASN G 318 1 18
HELIX 47 47 SER G 350 LEU G 363 1 14
HELIX 48 48 SER G 368 VAL G 375 1 8
HELIX 49 49 SER G 415 LYS G 425 1 11
HELIX 50 50 GLU G 430 ALA G 434 5 5
HELIX 51 51 GLY G 490 ALA G 493 5 4
HELIX 52 52 SER G 541 SER G 547 1 7
HELIX 53 53 THR B 22 GLY B 35 1 14
HELIX 54 54 PRO B 37 GLN B 41 5 5
HELIX 55 55 THR D 22 GLY D 35 1 14
HELIX 56 56 PRO D 37 GLN D 41 5 5
HELIX 57 57 THR D 55 ASN D 60 5 6
HELIX 58 58 THR F 22 GLY F 35 1 14
HELIX 59 59 PRO F 37 GLN F 41 5 5
HELIX 60 60 THR F 55 ASN F 60 5 6
HELIX 61 61 THR H 22 GLY H 35 1 14
HELIX 62 62 PRO H 37 GLN H 41 5 5
HELIX 63 63 THR H 55 ASN H 60 5 6
SHEET 1 A 2 GLN A 300 ASP A 301 0
SHEET 2 A 2 ARG B 74 GLY B 75 -1 O GLY B 75 N GLN A 300
SHEET 1 B 4 ARG A 390 PHE A 397 0
SHEET 2 B 4 GLY A 376 CYS A 384 -1 N LEU A 378 O GLU A 395
SHEET 3 B 4 SER A 446 ARG A 454 -1 O THR A 447 N LYS A 383
SHEET 4 B 4 GLU A 427 LEU A 429 -1 N LEU A 429 O SER A 446
SHEET 1 C 5 LEU A 400 LEU A 402 0
SHEET 2 C 5 ILE A 458 LEU A 463 1 O HIS A 462 N LEU A 400
SHEET 3 C 5 VAL A 552 LEU A 557 -1 O TYR A 555 N LEU A 459
SHEET 4 C 5 VAL A 501 SER A 513 -1 N ALA A 506 O PHE A 554
SHEET 5 C 5 LEU A 487 SER A 488 -1 N LEU A 487 O TYR A 502
SHEET 1 D 7 LEU A 400 LEU A 402 0
SHEET 2 D 7 ILE A 458 LEU A 463 1 O HIS A 462 N LEU A 400
SHEET 3 D 7 VAL A 552 LEU A 557 -1 O TYR A 555 N LEU A 459
SHEET 4 D 7 VAL A 501 SER A 513 -1 N ALA A 506 O PHE A 554
SHEET 5 D 7 TYR A 516 CYS A 525 -1 O ARG A 524 N TYR A 505
SHEET 6 D 7 GLY A 528 ASN A 533 -1 O GLY A 528 N CYS A 525
SHEET 7 D 7 ARG A 536 VAL A 540 -1 O ARG A 536 N ASN A 533
SHEET 1 E 2 PHE A 466 SER A 467 0
SHEET 2 E 2 LYS A 474 LYS A 475 -1 O LYS A 474 N SER A 467
SHEET 1 F 4 ARG C 390 PHE C 397 0
SHEET 2 F 4 GLY C 376 CYS C 384 -1 N LEU C 378 O GLU C 395
SHEET 3 F 4 SER C 446 ARG C 454 -1 O THR C 447 N LYS C 383
SHEET 4 F 4 GLU C 427 LEU C 429 -1 N LEU C 429 O SER C 446
SHEET 1 G 5 LEU C 400 LEU C 402 0
SHEET 2 G 5 ILE C 458 LEU C 463 1 O HIS C 462 N LEU C 400
SHEET 3 G 5 VAL C 552 LEU C 557 -1 O TYR C 555 N LEU C 459
SHEET 4 G 5 VAL C 501 SER C 513 -1 N ALA C 506 O PHE C 554
SHEET 5 G 5 LEU C 487 SER C 488 -1 N LEU C 487 O TYR C 502
SHEET 1 H 7 LEU C 400 LEU C 402 0
SHEET 2 H 7 ILE C 458 LEU C 463 1 O HIS C 462 N LEU C 400
SHEET 3 H 7 VAL C 552 LEU C 557 -1 O TYR C 555 N LEU C 459
SHEET 4 H 7 VAL C 501 SER C 513 -1 N ALA C 506 O PHE C 554
SHEET 5 H 7 TYR C 516 CYS C 525 -1 O ARG C 524 N TYR C 505
SHEET 6 H 7 GLY C 528 ASN C 533 -1 O GLY C 528 N CYS C 525
SHEET 7 H 7 ARG C 536 VAL C 540 -1 O ARG C 536 N ASN C 533
SHEET 1 I 2 PHE C 466 SER C 467 0
SHEET 2 I 2 LYS C 474 LYS C 475 -1 O LYS C 474 N SER C 467
SHEET 1 J 2 GLN E 300 ASP E 301 0
SHEET 2 J 2 ARG F 74 GLY F 75 -1 O GLY F 75 N GLN E 300
SHEET 1 K 4 ARG E 390 PHE E 397 0
SHEET 2 K 4 GLY E 376 CYS E 384 -1 N LEU E 378 O GLU E 395
SHEET 3 K 4 SER E 446 ARG E 454 -1 O THR E 447 N LYS E 383
SHEET 4 K 4 GLU E 427 LEU E 429 -1 N LEU E 429 O SER E 446
SHEET 1 L 5 LEU E 400 LEU E 402 0
SHEET 2 L 5 ILE E 458 LEU E 463 1 O HIS E 462 N LEU E 402
SHEET 3 L 5 VAL E 552 LEU E 557 -1 O TYR E 555 N LEU E 459
SHEET 4 L 5 VAL E 501 SER E 513 -1 N ALA E 506 O PHE E 554
SHEET 5 L 5 LEU E 487 SER E 488 -1 N LEU E 487 O TYR E 502
SHEET 1 M 7 LEU E 400 LEU E 402 0
SHEET 2 M 7 ILE E 458 LEU E 463 1 O HIS E 462 N LEU E 402
SHEET 3 M 7 VAL E 552 LEU E 557 -1 O TYR E 555 N LEU E 459
SHEET 4 M 7 VAL E 501 SER E 513 -1 N ALA E 506 O PHE E 554
SHEET 5 M 7 TYR E 516 CYS E 525 -1 O ARG E 524 N TYR E 505
SHEET 6 M 7 GLY E 528 ASN E 533 -1 O GLY E 528 N CYS E 525
SHEET 7 M 7 ARG E 536 VAL E 540 -1 O ARG E 536 N ASN E 533
SHEET 1 N 2 PHE E 466 SER E 467 0
SHEET 2 N 2 LYS E 474 LYS E 475 -1 O LYS E 474 N SER E 467
SHEET 1 O 4 ARG G 390 PHE G 397 0
SHEET 2 O 4 GLY G 376 CYS G 384 -1 N LEU G 378 O GLU G 395
SHEET 3 O 4 SER G 446 ARG G 454 -1 O THR G 447 N LYS G 383
SHEET 4 O 4 GLU G 427 LEU G 429 -1 N LEU G 429 O SER G 446
SHEET 1 P 5 LEU G 400 LEU G 402 0
SHEET 2 P 5 ILE G 458 LEU G 463 1 O HIS G 462 N LEU G 400
SHEET 3 P 5 VAL G 552 LEU G 557 -1 O TYR G 555 N LEU G 459
SHEET 4 P 5 VAL G 501 SER G 513 -1 N ALA G 506 O PHE G 554
SHEET 5 P 5 LEU G 487 SER G 488 -1 N LEU G 487 O TYR G 502
SHEET 1 Q 7 LEU G 400 LEU G 402 0
SHEET 2 Q 7 ILE G 458 LEU G 463 1 O HIS G 462 N LEU G 400
SHEET 3 Q 7 VAL G 552 LEU G 557 -1 O TYR G 555 N LEU G 459
SHEET 4 Q 7 VAL G 501 SER G 513 -1 N ALA G 506 O PHE G 554
SHEET 5 Q 7 TYR G 516 CYS G 525 -1 O ARG G 524 N TYR G 505
SHEET 6 Q 7 GLY G 528 ASN G 533 -1 O TYR G 532 N ALA G 521
SHEET 7 Q 7 ARG G 536 VAL G 540 -1 O SER G 538 N VAL G 531
SHEET 1 R 2 PHE G 466 SER G 467 0
SHEET 2 R 2 LYS G 474 LYS G 475 -1 O LYS G 474 N SER G 467
SHEET 1 S 5 THR B 12 GLU B 16 0
SHEET 2 S 5 GLN B 2 LYS B 6 -1 N VAL B 5 O ILE B 13
SHEET 3 S 5 THR B 66 VAL B 70 1 O LEU B 67 N PHE B 4
SHEET 4 S 5 ARG B 42 PHE B 45 -1 N ILE B 44 O HIS B 68
SHEET 5 S 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
SHEET 1 T 5 THR D 12 GLU D 16 0
SHEET 2 T 5 GLN D 2 LYS D 6 -1 N VAL D 5 O ILE D 13
SHEET 3 T 5 THR D 66 VAL D 70 1 O LEU D 67 N PHE D 4
SHEET 4 T 5 ARG D 42 PHE D 45 -1 N ILE D 44 O HIS D 68
SHEET 5 T 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
SHEET 1 U 5 THR F 12 GLU F 16 0
SHEET 2 U 5 GLN F 2 LYS F 6 -1 N VAL F 5 O ILE F 13
SHEET 3 U 5 THR F 66 VAL F 70 1 O LEU F 67 N PHE F 4
SHEET 4 U 5 ARG F 42 PHE F 45 -1 N ILE F 44 O HIS F 68
SHEET 5 U 5 LYS F 48 GLN F 49 -1 O LYS F 48 N PHE F 45
SHEET 1 V 5 THR H 12 GLU H 16 0
SHEET 2 V 5 GLN H 2 LYS H 6 -1 N VAL H 5 O ILE H 13
SHEET 3 V 5 THR H 66 VAL H 70 1 O LEU H 67 N PHE H 4
SHEET 4 V 5 ARG H 42 PHE H 45 -1 N ILE H 44 O HIS H 68
SHEET 5 V 5 LYS H 48 GLN H 49 -1 O LYS H 48 N PHE H 45
LINK C GLY B 75 N NEH B 76 1555 1555 1.43
LINK C GLY D 75 N NEH D 76 1555 1555 1.40
LINK C GLY F 75 N NEH F 76 1555 1555 1.42
LINK C GLY H 75 N NEH H 76 1555 1555 1.45
LINK SG CYS A 384 ZN ZN A 700 1555 1555 2.34
LINK SG CYS A 387 ZN ZN A 700 1555 1555 2.35
LINK SG CYS A 437 ZN ZN A 700 1555 1555 2.31
LINK SG CYS A 440 ZN ZN A 700 1555 1555 2.35
LINK SG CYS C 384 ZN ZN C 700 1555 1555 2.35
LINK SG CYS C 387 ZN ZN C 700 1555 1555 2.32
LINK SG CYS C 437 ZN ZN C 700 1555 1555 2.34
LINK SG CYS C 440 ZN ZN C 700 1555 1555 2.34
LINK SG CYS E 384 ZN ZN E 700 1555 1555 2.33
LINK SG CYS E 387 ZN ZN E 700 1555 1555 2.30
LINK SG CYS E 437 ZN ZN E 700 1555 1555 2.37
LINK SG CYS E 440 ZN ZN E 700 1555 1555 2.38
LINK SG CYS G 384 ZN ZN G 700 1555 1555 2.35
LINK SG CYS G 387 ZN ZN G 700 1555 1555 2.35
LINK SG CYS G 437 ZN ZN G 700 1555 1555 2.32
LINK SG CYS G 440 ZN ZN G 700 1555 1555 2.34
SITE 1 AC1 4 CYS A 384 CYS A 387 CYS A 437 CYS A 440
SITE 1 AC2 4 CYS C 384 CYS C 387 CYS C 437 CYS C 440
SITE 1 AC3 4 CYS E 384 CYS E 387 CYS E 437 CYS E 440
SITE 1 AC4 4 CYS G 384 CYS G 387 CYS G 437 CYS G 440
SITE 1 AC5 4 ASN A 219 CYS A 221 GLY A 517 GLY B 75
SITE 1 AC6 6 ASN C 219 CYS C 221 GLN C 299 GLY C 517
SITE 2 AC6 6 HIS C 518 GLY D 75
SITE 1 AC7 5 ASN E 219 CYS E 221 GLN E 299 GLY E 517
SITE 2 AC7 5 GLY F 75
SITE 1 AC8 5 ASN G 219 CYS G 221 GLN G 299 GLY G 517
SITE 2 AC8 5 GLY H 75
CRYST1 58.428 83.663 118.792 88.71 75.73 85.11 P 1 4
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 0.017115 -0.001464 -0.004351 0.00000
SCALE2 0.000000 0.011996 -0.000019 0.00000
SCALE3 0.000000 0.000000 0.008686 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
