HEADER LIGASE 23-JUL-19 6SC7
TITLE DAB3/HOIP-RBR-LIGAND3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF31;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HOIL-1-INTERACTING PROTEIN,HOIP,RING FINGER PROTEIN 31,RING-
COMPND 5 TYPE E3 UBIQUITIN TRANSFERASE RNF31,ZINC IN-BETWEEN-RING-FINGER
COMPND 6 UBIQUITIN-ASSOCIATED DOMAIN PROTEIN;
COMPND 7 EC: 2.3.2.31;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: SINGLE DOMAIN ANTIBODY;
COMPND 11 CHAIN: B, C;
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: RNF31, ZIBRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 10 ORGANISM_TAXID: 32630;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HUMAN SINGLE DOMAIN ANTIBODY, HOIP, RBR, INHIBITOR, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-C.I.TSAI,H.JOHANSSON,D.HOUSE,K.RITTINGER
REVDAT 3 29-JAN-20 6SC7 1 JRNL
REVDAT 2 18-DEC-19 6SC7 1 JRNL
REVDAT 1 27-NOV-19 6SC7 0
JRNL AUTH Y.I.TSAI,H.JOHANSSON,D.DIXON,S.MARTIN,C.W.CHUNG,J.CLARKSON,
JRNL AUTH 2 D.HOUSE,K.RITTINGER
JRNL TITL SINGLE-DOMAIN ANTIBODIES AS CRYSTALLIZATION CHAPERONES TO
JRNL TITL 2 ENABLE STRUCTURE-BASED INHIBITOR DEVELOPMENT FOR RBR E3
JRNL TITL 3 UBIQUITIN LIGASES.
JRNL REF CELL CHEM BIOL V. 27 83 2020
JRNL REFN ESSN 2451-9456
JRNL PMID 31813847
JRNL DOI 10.1016/J.CHEMBIOL.2019.11.007
REMARK 2
REMARK 2 RESOLUTION. 2.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22649
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1132
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 63.3900 - 5.1200 1.00 2861 135 0.2145 0.2379
REMARK 3 2 5.1200 - 4.0600 1.00 2730 142 0.1734 0.2030
REMARK 3 3 4.0600 - 3.5500 1.00 2678 150 0.2122 0.2680
REMARK 3 4 3.5500 - 3.2300 1.00 2670 134 0.2388 0.3352
REMARK 3 5 3.2300 - 2.9900 1.00 2658 138 0.2791 0.3332
REMARK 3 6 2.9900 - 2.8200 1.00 2659 141 0.2871 0.3280
REMARK 3 7 2.8200 - 2.6800 1.00 2646 148 0.3052 0.3796
REMARK 3 8 2.6800 - 2.5600 1.00 2615 144 0.3164 0.3524
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.441
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.351
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.18
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 4819
REMARK 3 ANGLE : 0.473 6530
REMARK 3 CHIRALITY : 0.039 683
REMARK 3 PLANARITY : 0.004 841
REMARK 3 DIHEDRAL : 10.966 2842
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'B'
REMARK 3 SELECTION : (CHAIN 'C' AND (RESID 1 THROUGH 10 OR
REMARK 3 (RESID 11 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB OR NAME CG )) OR
REMARK 3 RESID 12 OR (RESID 13 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 14 THROUGH 64 OR (RESID 65 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB OR NAME CG OR NAME CD )) OR RESID
REMARK 3 66 THROUGH 119))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6SC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1292103462.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-18
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) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22664
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560
REMARK 200 RESOLUTION RANGE LOW (A) : 63.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.03656
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50460
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: PHENIX
REMARK 200 STARTING MODEL: DAB3/HOIP-RBR APO STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM CHLORIDE,
REMARK 280 HEPES, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.85600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.35050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 120.27550
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.85600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.35050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 120.27550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.85600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.35050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 120.27550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.85600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.35050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 120.27550
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 218 LIES ON A SPECIAL POSITION.
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 PRO A 750
REMARK 465 ASP A 751
REMARK 465 LEU A 752
REMARK 465 THR A 753
REMARK 465 ASP A 754
REMARK 465 ASP A 755
REMARK 465 THR A 756
REMARK 465 GLN A 757
REMARK 465 ALA A 959
REMARK 465 GLY A 960
REMARK 465 ALA A 961
REMARK 465 ARG A 962
REMARK 465 ALA A 963
REMARK 465 VAL A 964
REMARK 465 PRO A 965
REMARK 465 GLY A 966
REMARK 465 GLY A 967
REMARK 465 ARG A 1070
REMARK 465 ARG A 1071
REMARK 465 LYS A 1072
REMARK 465 SER B 120
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 697 CG CD OE1 NE2
REMARK 470 ARG A 710 NH1 NH2
REMARK 470 LYS A 735 CD CE NZ
REMARK 470 LYS A 737 CG CD CE NZ
REMARK 470 ARG A 749 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 774 CG CD OE1 OE2
REMARK 470 ARG A 810 CZ NH1 NH2
REMARK 470 GLN A 812 CD OE1 NE2
REMARK 470 ARG A 827 CZ NH1 NH2
REMARK 470 GLU A 834 CG CD OE1 OE2
REMARK 470 ARG A 849 CG CD NE CZ NH1 NH2
REMARK 470 MET A 850 CG SD CE
REMARK 470 GLU A 854 CG CD OE1 OE2
REMARK 470 ARG A 894 NE CZ NH1 NH2
REMARK 470 LYS A 908 CD CE NZ
REMARK 470 ARG A 917 CD NE CZ NH1 NH2
REMARK 470 LYS A 919 CD CE NZ
REMARK 470 LYS A 975 CD CE NZ
REMARK 470 ARG A 982 CZ NH1 NH2
REMARK 470 GLN A1055 CD OE1 NE2
REMARK 470 LEU B 11 CD1 CD2
REMARK 470 GLN B 13 CG CD OE1 NE2
REMARK 470 LYS B 65 CE NZ
REMARK 470 GLN B 112 CD OE1 NE2
REMARK 470 GLN C 112 CD OE1 NE2
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 MET A 742 42.38 -97.26
REMARK 500 CYS A 747 -65.67 -95.51
REMARK 500 GLN A 819 -60.88 -101.42
REMARK 500 ALA A 907 -167.35 -75.57
REMARK 500 ASN A 979 53.70 -99.62
REMARK 500 VAL B 48 -60.84 -103.27
REMARK 500 VAL C 48 -60.78 -104.61
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 A2002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 699 SG
REMARK 620 2 CYS A 702 SG 93.6
REMARK 620 3 CYS A 722 SG 98.6 109.7
REMARK 620 4 CYS A 725 SG 137.8 120.3 93.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 717 SG
REMARK 620 2 CYS A 719 SG 81.5
REMARK 620 3 CYS A 744 SG 88.5 96.3
REMARK 620 4 CYS A 747 SG 110.6 158.1 102.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2004 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 799 SG
REMARK 620 2 CYS A 802 SG 116.1
REMARK 620 3 CYS A 817 SG 104.4 97.4
REMARK 620 4 CYS A 820 SG 99.5 118.0 121.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2005 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 825 SG
REMARK 620 2 CYS A 828 SG 140.4
REMARK 620 3 HIS A 836 NE2 113.8 102.3
REMARK 620 4 CYS A 841 SG 105.2 91.7 87.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2006 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 871 SG
REMARK 620 2 CYS A 874 SG 114.4
REMARK 620 3 CYS A 890 SG 100.8 100.2
REMARK 620 4 CYS A 893 SG 101.5 125.6 112.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2007 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 898 SG
REMARK 620 2 CYS A 901 SG 115.6
REMARK 620 3 HIS A 926 ND1 90.5 110.1
REMARK 620 4 CYS A 930 SG 110.4 110.4 118.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2008 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 911 SG
REMARK 620 2 CYS A 916 SG 133.4
REMARK 620 3 HIS A 923 NE2 104.7 99.1
REMARK 620 4 HIS A 925 NE2 92.7 116.7 108.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2009 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 969 SG
REMARK 620 2 CYS A 986 SG 117.0
REMARK 620 3 HIS A1001 ND1 98.0 109.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L6H A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 202
DBREF 6SC7 A 697 1072 UNP Q96EP0 RNF31_HUMAN 697 1072
DBREF 6SC7 B 1 120 PDB 6SC7 6SC7 1 120
DBREF 6SC7 C 1 120 PDB 6SC7 6SC7 1 120
SEQRES 1 A 376 GLN GLU CYS ALA VAL CYS GLY TRP ALA LEU PRO HIS ASN
SEQRES 2 A 376 ARG MET GLN ALA LEU THR SER CYS GLU CYS THR ILE CYS
SEQRES 3 A 376 PRO ASP CYS PHE ARG GLN HIS PHE THR ILE ALA LEU LYS
SEQRES 4 A 376 GLU LYS HIS ILE THR ASP MET VAL CYS PRO ALA CYS GLY
SEQRES 5 A 376 ARG PRO ASP LEU THR ASP ASP THR GLN LEU LEU SER TYR
SEQRES 6 A 376 PHE SER THR LEU ASP ILE GLN LEU ARG GLU SER LEU GLU
SEQRES 7 A 376 PRO ASP ALA TYR ALA LEU PHE HIS LYS LYS LEU THR GLU
SEQRES 8 A 376 GLY VAL LEU MET ARG ASP PRO LYS PHE LEU TRP CYS ALA
SEQRES 9 A 376 GLN CYS SER PHE GLY PHE ILE TYR GLU ARG GLU GLN LEU
SEQRES 10 A 376 GLU ALA THR CYS PRO GLN CYS HIS GLN THR PHE CYS VAL
SEQRES 11 A 376 ARG CYS LYS ARG GLN TRP GLU GLU GLN HIS ARG GLY ARG
SEQRES 12 A 376 SER CYS GLU ASP PHE GLN ASN TRP LYS ARG MET ASN ASP
SEQRES 13 A 376 PRO GLU TYR GLN ALA GLN GLY LEU ALA MET TYR LEU GLN
SEQRES 14 A 376 GLU ASN GLY ILE ASP CYS PRO LYS CYS LYS PHE SER TYR
SEQRES 15 A 376 ALA LEU ALA ARG GLY GLY CYS MET HIS PHE HIS CYS THR
SEQRES 16 A 376 GLN CYS ARG HIS GLN PHE CYS SER GLY CYS TYR ASN ALA
SEQRES 17 A 376 PHE TYR ALA LYS ASN LYS CYS PRO GLU PRO ASN CYS ARG
SEQRES 18 A 376 VAL LYS LYS SER LEU HIS GLY HIS HIS PRO ARG ASP CYS
SEQRES 19 A 376 LEU PHE TYR LEU ARG ASP TRP THR ALA LEU ARG LEU GLN
SEQRES 20 A 376 LYS LEU LEU GLN ASP ASN ASN VAL MET PHE ASN THR GLU
SEQRES 21 A 376 PRO PRO ALA GLY ALA ARG ALA VAL PRO GLY GLY GLY CYS
SEQRES 22 A 376 ARG VAL ILE GLU GLN LYS GLU VAL PRO ASN GLY LEU ARG
SEQRES 23 A 376 ASP GLU ALA CYS GLY LYS GLU THR PRO ALA GLY TYR ALA
SEQRES 24 A 376 GLY LEU CYS GLN ALA HIS TYR LYS GLU TYR LEU VAL SER
SEQRES 25 A 376 LEU ILE ASN ALA HIS SER LEU ASP PRO ALA THR LEU TYR
SEQRES 26 A 376 GLU VAL GLU GLU LEU GLU THR ALA THR GLU ARG TYR LEU
SEQRES 27 A 376 HIS VAL ARG PRO GLN PRO LEU ALA GLY GLU ASP PRO PRO
SEQRES 28 A 376 ALA TYR GLN ALA ARG LEU LEU GLN LYS LEU THR GLU GLU
SEQRES 29 A 376 VAL PRO LEU GLY GLN SER ILE PRO ARG ARG ARG LYS
SEQRES 1 B 120 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 B 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 B 120 PHE THR PHE ARG GLY TYR SER MET ALA TRP VAL ARG GLN
SEQRES 4 B 120 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER THR ILE SER
SEQRES 5 B 120 PRO ILE GLY THR TYR THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 B 120 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 B 120 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 B 120 ALA VAL TYR TYR CYS ALA LYS GLY SER TYR SER ARG GLY
SEQRES 9 B 120 THR PRO PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR
SEQRES 10 B 120 VAL SER SER
SEQRES 1 C 120 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 C 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 C 120 PHE THR PHE ARG GLY TYR SER MET ALA TRP VAL ARG GLN
SEQRES 4 C 120 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER THR ILE SER
SEQRES 5 C 120 PRO ILE GLY THR TYR THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 C 120 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 C 120 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 C 120 ALA VAL TYR TYR CYS ALA LYS GLY SER TYR SER ARG GLY
SEQRES 9 C 120 THR PRO PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR
SEQRES 10 C 120 VAL SER SER
HET L6H A2001 62
HET ZN A2002 1
HET ZN A2003 1
HET ZN A2004 1
HET ZN A2005 1
HET ZN A2006 1
HET ZN A2007 1
HET ZN A2008 1
HET ZN A2009 1
HET SO4 A2010 5
HET SO4 A2011 5
HET CL A2012 1
HET SO4 B 201 5
HET SO4 B 202 5
HETNAM L6H [2-[3-(CYCLOOCT-4-EN-1-YLOXYCARBONYLAMINO)PROPYLAMINO]-
HETNAM 2 L6H 2-OXIDANYLIDENE-ETHYL] (~{E})-4-[(2-OXIDANYLIDENE-5,6,
HETNAM 3 L6H 7,8-TETRAHYDRO-1~{H}-QUINOLIN-3-YL)CARBONYLAMINO]BUT-
HETNAM 4 L6H 2-ENOATE
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 4 L6H C28 H38 N4 O7
FORMUL 5 ZN 8(ZN 2+)
FORMUL 13 SO4 4(O4 S 2-)
FORMUL 15 CL CL 1-
FORMUL 18 HOH *74(H2 O)
HELIX 1 AA1 PRO A 707 MET A 711 5 5
HELIX 2 AA2 CYS A 722 GLU A 736 1 15
HELIX 3 AA3 HIS A 738 MET A 742 5 5
HELIX 4 AA4 LEU A 759 LEU A 773 1 15
HELIX 5 AA5 GLU A 774 VAL A 789 1 16
HELIX 6 AA6 GLU A 833 ARG A 837 5 5
HELIX 7 AA7 SER A 840 ASN A 851 1 12
HELIX 8 AA8 ASP A 852 GLN A 858 1 7
HELIX 9 AA9 LEU A 860 ASN A 867 1 8
HELIX 10 AB1 CYS A 930 ARG A 935 1 6
HELIX 11 AB2 THR A 938 ASP A 948 1 11
HELIX 12 AB3 CYS A 998 HIS A 1013 1 16
HELIX 13 AB4 ASP A 1016 TYR A 1021 5 6
HELIX 14 AB5 GLU A 1022 LEU A 1034 1 13
HELIX 15 AB6 ASP A 1045 VAL A 1061 1 17
HELIX 16 AB7 THR B 28 TYR B 32 5 5
HELIX 17 AB8 ARG B 87 THR B 91 5 5
HELIX 18 AB9 THR C 28 TYR C 32 5 5
HELIX 19 AC1 ARG C 87 THR C 91 5 5
SHEET 1 A 2 PHE A 796 TRP A 798 0
SHEET 2 A 2 GLY A 805 ILE A 807 -1
SHEET 1 B 2 GLU A 814 THR A 816 0
SHEET 2 B 2 THR A 823 CYS A 825 -1
SHEET 1 C 2 HIS A 887 HIS A 889 0
SHEET 2 C 2 GLN A 896 CYS A 898 -1
SHEET 1 D 2 ILE A 972 VAL A 977 0
SHEET 2 D 2 GLY A 980 ALA A 985 -1
SHEET 1 E 4 GLN B 3 SER B 7 0
SHEET 2 E 4 LEU B 18 SER B 25 -1
SHEET 3 E 4 THR B 78 MET B 83 -1
SHEET 4 E 4 PHE B 68 ASP B 73 -1
SHEET 1 F 5 THR B 114 VAL B 116 0
SHEET 2 F 5 ALA B 92 LYS B 98 -1
SHEET 3 F 5 MET B 34 ALA B 40 -1
SHEET 4 F 5 LEU B 45 ILE B 51 -1
SHEET 5 F 5 THR B 58 TYR B 60 -1
SHEET 1 G 2 ALA B 97 GLY B 99 0
SHEET 2 G 2 PHE B 107 TRP B 110 -1
SHEET 1 H 4 GLN C 3 SER C 7 0
SHEET 2 H 4 LEU C 18 SER C 25 -1
SHEET 3 H 4 THR C 78 MET C 83 -1
SHEET 4 H 4 PHE C 68 ASP C 73 -1
SHEET 1 I 6 GLY C 10 VAL C 12 0
SHEET 2 I 6 THR C 114 VAL C 118 1
SHEET 3 I 6 ALA C 92 LYS C 98 -1
SHEET 4 I 6 MET C 34 ALA C 40 -1
SHEET 5 I 6 GLU C 46 ILE C 51 -1
SHEET 6 I 6 THR C 58 TYR C 60 -1
SHEET 1 J 2 ALA C 97 GLY C 99 0
SHEET 2 J 2 PHE C 107 TRP C 110 -1
SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.03
SSBOND 2 CYS C 22 CYS C 96 1555 1555 2.03
LINK SG CYS A 699 ZN ZN A2002 1555 1555 2.61
LINK SG CYS A 702 ZN ZN A2002 1555 1555 2.30
LINK SG CYS A 717 ZN ZN A2003 1555 1555 2.58
LINK SG CYS A 719 ZN ZN A2003 1555 1555 2.63
LINK SG CYS A 722 ZN ZN A2002 1555 1555 2.45
LINK SG CYS A 725 ZN ZN A2002 1555 1555 2.63
LINK SG CYS A 744 ZN ZN A2003 1555 1555 2.74
LINK SG CYS A 747 ZN ZN A2003 1555 1555 2.42
LINK SG CYS A 799 ZN ZN A2004 1555 1555 2.52
LINK SG CYS A 802 ZN ZN A2004 1555 1555 2.33
LINK SG CYS A 817 ZN ZN A2004 1555 1555 2.38
LINK SG CYS A 820 ZN ZN A2004 1555 1555 2.37
LINK SG CYS A 825 ZN ZN A2005 1555 1555 2.48
LINK SG CYS A 828 ZN ZN A2005 1555 1555 1.95
LINK NE2 HIS A 836 ZN ZN A2005 1555 1555 2.50
LINK SG CYS A 841 ZN ZN A2005 1555 1555 2.47
LINK SG CYS A 871 ZN ZN A2006 1555 1555 2.45
LINK SG CYS A 874 ZN ZN A2006 1555 1555 2.26
LINK SG CYS A 885 C16 L6H A2001 1555 1555 1.77
LINK SG CYS A 890 ZN ZN A2006 1555 1555 2.38
LINK SG CYS A 893 ZN ZN A2006 1555 1555 2.22
LINK SG CYS A 898 ZN ZN A2007 1555 1555 2.62
LINK SG CYS A 901 ZN ZN A2007 1555 1555 2.34
LINK SG CYS A 911 ZN ZN A2008 1555 1555 2.29
LINK SG CYS A 916 ZN ZN A2008 1555 1555 2.31
LINK NE2 HIS A 923 ZN ZN A2008 1555 1555 2.07
LINK NE2 HIS A 925 ZN ZN A2008 1555 1555 2.06
LINK ND1 HIS A 926 ZN ZN A2007 1555 1555 2.09
LINK SG CYS A 930 ZN ZN A2007 1555 1555 2.46
LINK SG CYS A 969 ZN ZN A2009 1555 1555 2.55
LINK SG CYS A 986 ZN ZN A2009 1555 1555 2.65
LINK ND1 HIS A1001 ZN ZN A2009 1555 1555 2.06
SITE 1 AC1 7 LEU A 880 CYS A 885 HIS A 887 PHE A 888
SITE 2 AC1 7 HIS A 889 GLU A 976 LYS A 988
SITE 1 AC2 5 CYS A 699 VAL A 701 CYS A 702 CYS A 722
SITE 2 AC2 5 CYS A 725
SITE 1 AC3 4 CYS A 717 CYS A 719 CYS A 744 CYS A 747
SITE 1 AC4 4 CYS A 799 CYS A 802 CYS A 817 CYS A 820
SITE 1 AC5 4 CYS A 825 CYS A 828 HIS A 836 CYS A 841
SITE 1 AC6 4 CYS A 871 CYS A 874 CYS A 890 CYS A 893
SITE 1 AC7 4 CYS A 898 CYS A 901 HIS A 926 CYS A 930
SITE 1 AC8 4 CYS A 911 CYS A 916 HIS A 923 HIS A 925
SITE 1 AC9 4 CYS A 969 CYS A 986 CYS A 998 HIS A1001
SITE 1 AD1 5 ASN A 903 PRO A 927 LEU A1063 GLN A1065
SITE 2 AD1 5 HOH A2113
SITE 1 AD2 6 GLY A 884 CYS A 885 MET A 886 HIS A 887
SITE 2 AD2 6 PHE A 932 ARG A 935
SITE 1 AD3 2 TRP A 798 GLY B 104
SITE 1 AD4 4 SER B 52 ILE B 54 GLY B 55 THR B 56
SITE 1 AD5 3 PHE B 27 THR B 28 TYR B 32
CRYST1 65.712 86.701 240.551 90.00 90.00 90.00 I 2 2 2 16
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 0.015218 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011534 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004157 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
