HEADER LIGASE/SIGNALING PROTEIN 17-FEB-15 5AIT
TITLE A COMPLEX OF OF RNF4-RING DOMAIN, UBEV2, UBC13-UB (ISOPEPTIDE
TITLE 2 CROSSLINK)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RING DOMAIN, UNP RESIDUES 131-194,131-194;
COMPND 5 SYNONYM: RING FINGER PROTEIN 4, SMALL NUCLEAR RING FINGER PROTEIN, P
COMPND 6 ROTEIN SNURF, RING DOMAIN;
COMPND 7 EC: 6.3.2.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: THE RING DOMAIN IS DUPLICATED BUT AS A FUSED DIMER.
COMPND 10 THAT IS THE SEQUENCE OF THE RING DOMAIN FROM RNF4 (RESIDUES 131 TO
COMPND 11 194) IS LINKED BY A SINGLE GLYCINE RESIDUE TO ANOTHER RING DOMAIN
COMPND 12 (RESIDUES 131 TO 194).;
COMPND 13 MOL_ID: 2;
COMPND 14 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;
COMPND 15 CHAIN: B, E;
COMPND 16 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME, UBC13, UBCH13,
COMPND 17 UBIQUITIN CARRIER PROTEIN N, UBIQUITIN-PROTEIN LIGASE N;
COMPND 18 EC: 6.3.2.19;
COMPND 19 ENGINEERED: YES;
COMPND 20 MUTATION: YES;
COMPND 21 MOL_ID: 3;
COMPND 22 MOLECULE: POLYUBIQUITIN-C;
COMPND 23 CHAIN: C, F;
COMPND 24 FRAGMENT: UNP RESIDUES 1-76;
COMPND 25 ENGINEERED: YES;
COMPND 26 MOL_ID: 4;
COMPND 27 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2;
COMPND 28 CHAIN: D, G;
COMPND 29 FRAGMENT: UNP RESIDUES 1-145;
COMPND 30 SYNONYM: DDVIT 1, ENTEROCYTE DIFFERENTIATION-ASSOCIATED FACTOR 1, ED
COMPND 31 AF-1, ENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1, EDPF-1, MMS2
COMPND 32 HOMOLOG, VITAMIN D3-INDUCIBLE PROTEIN;
COMPND 33 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 15 ORGANISM_COMMON: CATTLE;
SOURCE 16 ORGANISM_TAXID: 9913;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIGASE-SIGNALING PROTEIN COMPLEX, COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.BRANIGAN,J.H.NAISMITH
REVDAT 4 31-JUL-19 5AIT 1 REMARK LINK
REVDAT 3 19-AUG-15 5AIT 1 JRNL
REVDAT 2 15-JUL-15 5AIT 1 TITLE JRNL MASTER
REVDAT 1 08-JUL-15 5AIT 0
JRNL AUTH E.BRANIGAN,A.PLECHANOVOVA,E.JAFFRAY,J.H.NAISMITH,R.T.HAY
JRNL TITL STRUCTURAL BASIS FOR THE RING CATALYZED SYNTHESIS OF K63
JRNL TITL 2 LINKED UBIQUITIN CHAINS
JRNL REF NAT.STRUCT.MOL.BIOL. V. 22 597 2015
JRNL REFN ISSN 1545-9993
JRNL PMID 26148049
JRNL DOI 10.1038/NSMB.3052
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 14864
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 753
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 407
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 35.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.3490
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6738
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 139.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.88000
REMARK 3 B22 (A**2) : 0.88000
REMARK 3 B33 (A**2) : -2.86000
REMARK 3 B12 (A**2) : 0.44000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.711
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.575
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.502
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6893 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6717 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9332 ; 1.556 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15497 ; 2.340 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 844 ; 6.584 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 306 ;30.257 ;24.314
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1248 ;13.832 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;15.824 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1036 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7678 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1478 ; 0.010 ; 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): 3397 ;11.752 ;13.231
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3396 ;11.749 ;13.231
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4234 ;17.504 ;19.850
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3494 ;13.800 ;14.441
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
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. U VALUES REFINED INDIVIDUALLY. DISORDERED REGIONS
REMARK 3 WERE MODELED STEREOCHEMICALLY. THE ISOPEPTIDE LINKAGE WAS
REMARK 3 INCLUDED AS A RESTRAINT. THE PDB FILE CANONOCAL PDB SHOWS THE
REMARK 3 BIOLOGICAL CONTEXT, HOWEVER DUE TO THE CHEMICAL CROSS LINK
REMARK 3 CANONICAL IS NOT FOUND IN THE CRYSTAL PER SE.
REMARK 4
REMARK 4 5AIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1290063077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979490
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14922
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 67.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 35.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: DATA ARE 96 TO 3.5. THE DETECTOR WAS POSITION TO AVOID
REMARK 200 OVERLAP, DATA IN CORNERS 3.49 TO 3.4 ARE INCOMPLETE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 219.22667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 109.61333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 109.61333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 219.22667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 127
REMARK 465 ALA A 128
REMARK 465 MET A 129
REMARK 465 GLY A 130
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 3
REMARK 465 ASN B 151
REMARK 465 ILE B 152
REMARK 465 MET C 1
REMARK 465 GLY D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 VAL D 3
REMARK 465 SER D 4
REMARK 465 THR D 5
REMARK 465 GLY E -1
REMARK 465 ALA E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLY E 3
REMARK 465 ASN E 151
REMARK 465 ILE E 152
REMARK 465 MET F 1
REMARK 465 GLY G -1
REMARK 465 ALA G 0
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 VAL G 3
REMARK 465 SER G 4
REMARK 465 THR G 5
REMARK 465 ASN G 144
REMARK 465 ASN G 145
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 NZ LYS B 87 C GLY C 76 1.35
REMARK 500 NZ LYS E 87 C GLY F 76 1.43
REMARK 500 NH1 ARG B 7 OH TYR B 62 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER C 57 OG SER C 57 5675 1.70
REMARK 500 CB SER C 57 OG SER C 57 5675 1.96
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 TRP G 46 CB TRP G 46 CG -0.113
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 CYS A 223 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 PRO B 120 C - N - CD ANGL. DEV. = -13.6 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 ILE A 138 -72.38 -72.18
REMARK 500 MET A 140 33.90 72.87
REMARK 500 PRO A 178 -17.52 -48.28
REMARK 500 ARG A 181 5.80 80.38
REMARK 500 HIS A 186 158.37 59.87
REMARK 500 ILE A 203 -71.79 -66.79
REMARK 500 ARG A 246 -14.19 104.65
REMARK 500 ARG B 33 3.90 -68.15
REMARK 500 ALA B 92 -82.93 -132.19
REMARK 500 LYS C 63 117.72 -31.93
REMARK 500 LYS D 108 43.75 -102.91
REMARK 500 ALA E 92 -90.43 -122.32
REMARK 500 GLN E 100 164.48 58.86
REMARK 500 ALA E 114 76.72 -117.60
REMARK 500 GLN F 62 -76.60 -138.88
REMARK 500 ARG G 55 49.06 39.61
REMARK 500 LYS G 108 37.29 -97.52
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 A1260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 136 SG
REMARK 620 2 CYS A 139 SG 118.8
REMARK 620 3 CYS A 163 SG 100.9 123.1
REMARK 620 4 CYS A 166 SG 117.1 106.0 87.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1261 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 158 SG
REMARK 620 2 HIS A 160 ND1 96.8
REMARK 620 3 CYS A 177 SG 104.8 121.1
REMARK 620 4 CYS A 180 SG 102.9 112.0 115.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1262 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 201 SG
REMARK 620 2 CYS A 204 SG 89.4
REMARK 620 3 CYS A 228 SG 122.6 120.0
REMARK 620 4 CYS A 231 SG 118.0 115.0 94.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1263 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 223 SG
REMARK 620 2 HIS A 225 ND1 95.6
REMARK 620 3 CYS A 242 SG 98.7 140.0
REMARK 620 4 CYS A 245 SG 100.9 117.6 96.1
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 1260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1263
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS IS A HEAD TO TAIL FUSION OF TWO RING DOMAINS. THE
REMARK 999 GAMG AT THE N-TERMINUS IS A CLONING ARTEFACT
REMARK 999 THE ACTIVE SITE C87 HAS BEEN MUTATED TO K87 FOR ATTACHMENT
REMARK 999 OF UBIQUITIN (MOLECULES IN CHAIN C AND F). SECOND MUTATION
REMARK 999 K92 TO A. THE N-TERMINAL GA IS A CLONING ARTIFACT
REMARK 999 NOTE TERMINAL GLY OF CHAIN C IS ATTACHED TO LYS 87 OF
REMARK 999 CHAIN B CHAIN F TERMINAL GLY IS ATTACHED TO CHAIN E LYS 87
REMARK 999 THE GA ARE CLONING ARTEFACTS
DBREF 5AIT A 131 194 UNP O88846 RNF4_RAT 131 194
DBREF 5AIT A 196 259 UNP O88846 RNF4_RAT 131 194
DBREF 5AIT B 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 5AIT C 1 76 UNP P0CH28 UBC_BOVIN 77 152
DBREF 5AIT D 1 145 UNP Q15819 UB2V2_HUMAN 1 145
DBREF 5AIT E 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 5AIT F 1 76 UNP P0CH28 UBC_BOVIN 77 152
DBREF 5AIT G 1 145 UNP Q15819 UB2V2_HUMAN 1 145
SEQADV 5AIT GLY A 127 UNP O88846 EXPRESSION TAG
SEQADV 5AIT ALA A 128 UNP O88846 EXPRESSION TAG
SEQADV 5AIT MET A 129 UNP O88846 EXPRESSION TAG
SEQADV 5AIT GLY A 130 UNP O88846 EXPRESSION TAG
SEQADV 5AIT GLY A 195 UNP O88846 LINKER
SEQADV 5AIT GLY B -1 UNP P61088 EXPRESSION TAG
SEQADV 5AIT ALA B 0 UNP P61088 EXPRESSION TAG
SEQADV 5AIT LYS B 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQADV 5AIT ALA B 92 UNP P61088 LYS 92 ENGINEERED MUTATION
SEQADV 5AIT GLY D -1 UNP Q15819 EXPRESSION TAG
SEQADV 5AIT ALA D 0 UNP Q15819 EXPRESSION TAG
SEQADV 5AIT GLY E -1 UNP P61088 EXPRESSION TAG
SEQADV 5AIT ALA E 0 UNP P61088 EXPRESSION TAG
SEQADV 5AIT LYS E 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQADV 5AIT ALA E 92 UNP P61088 LYS 92 ENGINEERED MUTATION
SEQADV 5AIT GLY G -1 UNP Q15819 EXPRESSION TAG
SEQADV 5AIT ALA G 0 UNP Q15819 EXPRESSION TAG
SEQRES 1 A 133 GLY ALA MET GLY SER GLY THR VAL SER CYS PRO ILE CYS
SEQRES 2 A 133 MET ASP GLY TYR SER GLU ILE VAL GLN ASN GLY ARG LEU
SEQRES 3 A 133 ILE VAL SER THR GLU CYS GLY HIS VAL PHE CYS SER GLN
SEQRES 4 A 133 CYS LEU ARG ASP SER LEU LYS ASN ALA ASN THR CYS PRO
SEQRES 5 A 133 THR CYS ARG LYS LYS ILE ASN HIS LYS ARG TYR HIS PRO
SEQRES 6 A 133 ILE TYR ILE GLY SER GLY THR VAL SER CYS PRO ILE CYS
SEQRES 7 A 133 MET ASP GLY TYR SER GLU ILE VAL GLN ASN GLY ARG LEU
SEQRES 8 A 133 ILE VAL SER THR GLU CYS GLY HIS VAL PHE CYS SER GLN
SEQRES 9 A 133 CYS LEU ARG ASP SER LEU LYS ASN ALA ASN THR CYS PRO
SEQRES 10 A 133 THR CYS ARG LYS LYS ILE ASN HIS LYS ARG TYR HIS PRO
SEQRES 11 A 133 ILE TYR ILE
SEQRES 1 B 154 GLY ALA MET ALA GLY LEU PRO ARG ARG ILE ILE LYS GLU
SEQRES 2 B 154 THR GLN ARG LEU LEU ALA GLU PRO VAL PRO GLY ILE LYS
SEQRES 3 B 154 ALA GLU PRO ASP GLU SER ASN ALA ARG TYR PHE HIS VAL
SEQRES 4 B 154 VAL ILE ALA GLY PRO GLN ASP SER PRO PHE GLU GLY GLY
SEQRES 5 B 154 THR PHE LYS LEU GLU LEU PHE LEU PRO GLU GLU TYR PRO
SEQRES 6 B 154 MET ALA ALA PRO LYS VAL ARG PHE MET THR LYS ILE TYR
SEQRES 7 B 154 HIS PRO ASN VAL ASP LYS LEU GLY ARG ILE LYS LEU ASP
SEQRES 8 B 154 ILE LEU ALA ASP LYS TRP SER PRO ALA LEU GLN ILE ARG
SEQRES 9 B 154 THR VAL LEU LEU SER ILE GLN ALA LEU LEU SER ALA PRO
SEQRES 10 B 154 ASN PRO ASP ASP PRO LEU ALA ASN ASP VAL ALA GLU GLN
SEQRES 11 B 154 TRP LYS THR ASN GLU ALA GLN ALA ILE GLU THR ALA ARG
SEQRES 12 B 154 ALA TRP THR ARG LEU TYR ALA MET ASN ASN ILE
SEQRES 1 C 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 C 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 C 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 C 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 C 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 C 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 D 147 GLY ALA MET ALA VAL SER THR GLY VAL LYS VAL PRO ARG
SEQRES 2 D 147 ASN PHE ARG LEU LEU GLU GLU LEU GLU GLU GLY GLN LYS
SEQRES 3 D 147 GLY VAL GLY ASP GLY THR VAL SER TRP GLY LEU GLU ASP
SEQRES 4 D 147 ASP GLU ASP MET THR LEU THR ARG TRP THR GLY MET ILE
SEQRES 5 D 147 ILE GLY PRO PRO ARG THR ASN TYR GLU ASN ARG ILE TYR
SEQRES 6 D 147 SER LEU LYS VAL GLU CYS GLY PRO LYS TYR PRO GLU ALA
SEQRES 7 D 147 PRO PRO SER VAL ARG PHE VAL THR LYS ILE ASN MET ASN
SEQRES 8 D 147 GLY ILE ASN ASN SER SER GLY MET VAL ASP ALA ARG SER
SEQRES 9 D 147 ILE PRO VAL LEU ALA LYS TRP GLN ASN SER TYR SER ILE
SEQRES 10 D 147 LYS VAL VAL LEU GLN GLU LEU ARG ARG LEU MET MET SER
SEQRES 11 D 147 LYS GLU ASN MET LYS LEU PRO GLN PRO PRO GLU GLY GLN
SEQRES 12 D 147 THR TYR ASN ASN
SEQRES 1 E 154 GLY ALA MET ALA GLY LEU PRO ARG ARG ILE ILE LYS GLU
SEQRES 2 E 154 THR GLN ARG LEU LEU ALA GLU PRO VAL PRO GLY ILE LYS
SEQRES 3 E 154 ALA GLU PRO ASP GLU SER ASN ALA ARG TYR PHE HIS VAL
SEQRES 4 E 154 VAL ILE ALA GLY PRO GLN ASP SER PRO PHE GLU GLY GLY
SEQRES 5 E 154 THR PHE LYS LEU GLU LEU PHE LEU PRO GLU GLU TYR PRO
SEQRES 6 E 154 MET ALA ALA PRO LYS VAL ARG PHE MET THR LYS ILE TYR
SEQRES 7 E 154 HIS PRO ASN VAL ASP LYS LEU GLY ARG ILE LYS LEU ASP
SEQRES 8 E 154 ILE LEU ALA ASP LYS TRP SER PRO ALA LEU GLN ILE ARG
SEQRES 9 E 154 THR VAL LEU LEU SER ILE GLN ALA LEU LEU SER ALA PRO
SEQRES 10 E 154 ASN PRO ASP ASP PRO LEU ALA ASN ASP VAL ALA GLU GLN
SEQRES 11 E 154 TRP LYS THR ASN GLU ALA GLN ALA ILE GLU THR ALA ARG
SEQRES 12 E 154 ALA TRP THR ARG LEU TYR ALA MET ASN ASN ILE
SEQRES 1 F 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 F 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 F 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 F 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 F 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 F 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 G 147 GLY ALA MET ALA VAL SER THR GLY VAL LYS VAL PRO ARG
SEQRES 2 G 147 ASN PHE ARG LEU LEU GLU GLU LEU GLU GLU GLY GLN LYS
SEQRES 3 G 147 GLY VAL GLY ASP GLY THR VAL SER TRP GLY LEU GLU ASP
SEQRES 4 G 147 ASP GLU ASP MET THR LEU THR ARG TRP THR GLY MET ILE
SEQRES 5 G 147 ILE GLY PRO PRO ARG THR ASN TYR GLU ASN ARG ILE TYR
SEQRES 6 G 147 SER LEU LYS VAL GLU CYS GLY PRO LYS TYR PRO GLU ALA
SEQRES 7 G 147 PRO PRO SER VAL ARG PHE VAL THR LYS ILE ASN MET ASN
SEQRES 8 G 147 GLY ILE ASN ASN SER SER GLY MET VAL ASP ALA ARG SER
SEQRES 9 G 147 ILE PRO VAL LEU ALA LYS TRP GLN ASN SER TYR SER ILE
SEQRES 10 G 147 LYS VAL VAL LEU GLN GLU LEU ARG ARG LEU MET MET SER
SEQRES 11 G 147 LYS GLU ASN MET LYS LEU PRO GLN PRO PRO GLU GLY GLN
SEQRES 12 G 147 THR TYR ASN ASN
HET ZN A1260 1
HET ZN A1261 1
HET ZN A1262 1
HET ZN A1263 1
HETNAM ZN ZINC ION
FORMUL 8 ZN 4(ZN 2+)
HELIX 1 1 TYR A 143 ASN A 149 1 7
HELIX 2 2 SER A 164 LYS A 172 1 9
HELIX 3 3 TYR A 208 ASN A 214 1 7
HELIX 4 4 SER A 229 ALA A 239 1 11
HELIX 5 5 ASN A 250 LYS A 252 5 3
HELIX 6 6 PRO B 5 GLU B 18 1 14
HELIX 7 7 LEU B 88 ALA B 92 5 5
HELIX 8 8 GLN B 100 ALA B 114 1 15
HELIX 9 9 ALA B 122 ASN B 132 1 11
HELIX 10 10 ASN B 132 MET B 149 1 18
HELIX 11 11 THR C 22 GLY C 35 1 14
HELIX 12 12 PRO C 37 ASP C 39 5 3
HELIX 13 13 PRO D 10 GLY D 25 1 16
HELIX 14 14 ILE D 103 LYS D 108 1 6
HELIX 15 15 SER D 114 SER D 128 1 15
HELIX 16 16 SER D 128 LYS D 133 1 6
HELIX 17 17 PRO E 5 GLU E 18 1 14
HELIX 18 18 LEU E 88 ALA E 92 5 5
HELIX 19 19 SER E 96 ALA E 98 5 3
HELIX 20 20 LEU E 99 ALA E 114 1 16
HELIX 21 21 ALA E 122 ASN E 132 1 11
HELIX 22 22 ASN E 132 MET E 149 1 18
HELIX 23 23 THR F 22 GLY F 35 1 14
HELIX 24 24 PRO G 10 GLY G 25 1 16
HELIX 25 25 ILE G 103 LYS G 108 1 6
HELIX 26 26 SER G 114 SER G 128 1 15
HELIX 27 27 SER G 128 LYS G 133 1 6
SHEET 1 AA 2 SER A 135 CYS A 136 0
SHEET 2 AA 2 ASP A 141 GLY A 142 -1 O ASP A 141 N CYS A 136
SHEET 1 AB 3 VAL A 161 CYS A 163 0
SHEET 2 AB 3 ILE A 153 THR A 156 -1 O VAL A 154 N PHE A 162
SHEET 3 AB 3 TYR A 189 ILE A 192 -1 O HIS A 190 N SER A 155
SHEET 1 AC 2 SER A 200 CYS A 201 0
SHEET 2 AC 2 ASP A 206 GLY A 207 -1 O ASP A 206 N CYS A 201
SHEET 1 AD 3 VAL A 226 CYS A 228 0
SHEET 2 AD 3 ILE A 218 THR A 221 -1 O VAL A 219 N PHE A 227
SHEET 3 AD 3 TYR A 254 PRO A 256 -1 O HIS A 255 N SER A 220
SHEET 1 BA 4 ILE B 23 PRO B 27 0
SHEET 2 BA 4 TYR B 34 ALA B 40 -1 O HIS B 36 N GLU B 26
SHEET 3 BA 4 THR B 51 PHE B 57 -1 O PHE B 52 N ILE B 39
SHEET 4 BA 4 LYS B 68 PHE B 71 -1 O LYS B 68 N PHE B 57
SHEET 1 CA 5 THR C 12 LEU C 15 0
SHEET 2 CA 5 ILE C 3 LYS C 6 -1 O ILE C 3 N LEU C 15
SHEET 3 CA 5 THR C 66 LEU C 71 1 O LEU C 67 N LYS C 6
SHEET 4 CA 5 GLN C 41 PHE C 45 -1 O ARG C 42 N VAL C 70
SHEET 5 CA 5 LYS C 48 GLN C 49 -1 O LYS C 48 N PHE C 45
SHEET 1 DA 4 VAL D 31 LEU D 35 0
SHEET 2 DA 4 ARG D 45 ILE D 51 -1 O THR D 47 N GLY D 34
SHEET 3 DA 4 ILE D 62 GLU D 68 -1 O TYR D 63 N ILE D 50
SHEET 4 DA 4 SER D 79 PHE D 82 -1 O SER D 79 N GLU D 68
SHEET 1 EA 4 ILE E 23 PRO E 27 0
SHEET 2 EA 4 TYR E 34 ALA E 40 -1 O HIS E 36 N GLU E 26
SHEET 3 EA 4 THR E 51 PHE E 57 -1 O PHE E 52 N ILE E 39
SHEET 4 EA 4 LYS E 68 PHE E 71 -1 O LYS E 68 N PHE E 57
SHEET 1 FA 5 THR F 12 LEU F 15 0
SHEET 2 FA 5 ILE F 3 THR F 7 -1 O ILE F 3 N LEU F 15
SHEET 3 FA 5 THR F 66 LEU F 71 1 O LEU F 67 N LYS F 6
SHEET 4 FA 5 GLN F 41 PHE F 45 -1 O ARG F 42 N VAL F 70
SHEET 5 FA 5 LYS F 48 GLN F 49 -1 O LYS F 48 N PHE F 45
SHEET 1 GA 4 VAL G 31 LEU G 35 0
SHEET 2 GA 4 ARG G 45 ILE G 51 -1 O THR G 47 N GLY G 34
SHEET 3 GA 4 ILE G 62 GLU G 68 -1 O TYR G 63 N ILE G 50
SHEET 4 GA 4 SER G 79 PHE G 82 -1 O SER G 79 N GLU G 68
LINK SG CYS A 136 ZN ZN A1260 1555 1555 2.33
LINK SG CYS A 139 ZN ZN A1260 1555 1555 2.24
LINK SG CYS A 158 ZN ZN A1261 1555 1555 2.32
LINK ND1 HIS A 160 ZN ZN A1261 1555 1555 2.10
LINK SG CYS A 163 ZN ZN A1260 1555 1555 2.31
LINK SG CYS A 166 ZN ZN A1260 1555 1555 2.28
LINK SG CYS A 177 ZN ZN A1261 1555 1555 2.24
LINK SG CYS A 180 ZN ZN A1261 1555 1555 2.28
LINK SG CYS A 201 ZN ZN A1262 1555 1555 2.35
LINK SG CYS A 204 ZN ZN A1262 1555 1555 2.24
LINK SG CYS A 223 ZN ZN A1263 1555 1555 2.35
LINK ND1 HIS A 225 ZN ZN A1263 1555 1555 2.12
LINK SG CYS A 228 ZN ZN A1262 1555 1555 2.32
LINK SG CYS A 231 ZN ZN A1262 1555 1555 2.30
LINK SG CYS A 242 ZN ZN A1263 1555 1555 2.32
LINK SG CYS A 245 ZN ZN A1263 1555 1555 2.30
CISPEP 1 TYR B 62 PRO B 63 0 7.57
CISPEP 2 TYR D 73 PRO D 74 0 7.98
CISPEP 3 TYR E 62 PRO E 63 0 11.49
CISPEP 4 TYR G 73 PRO G 74 0 4.02
SITE 1 AC1 5 CYS A 136 CYS A 139 ARG A 151 CYS A 163
SITE 2 AC1 5 CYS A 166
SITE 1 AC2 4 CYS A 158 HIS A 160 CYS A 177 CYS A 180
SITE 1 AC3 4 CYS A 201 CYS A 204 CYS A 228 CYS A 231
SITE 1 AC4 4 CYS A 223 HIS A 225 CYS A 242 CYS A 245
CRYST1 77.580 77.580 328.840 90.00 90.00 120.00 P 32 2 1 12
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 0.012890 0.007442 0.000000 0.00000
SCALE2 0.000000 0.014884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003041 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
