HEADER DNA BINDING PROTEIN/DNA 01-JUL-15 5CC1
TITLE S425G GLUCOCORTICOID RECEPTOR DNA BINDING DOMAIN - (+)GRE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOCORTICOID RECEPTOR;
COMPND 3 CHAIN: A, B, W, X;
COMPND 4 SYNONYM: GR,NUCLEAR RECEPTOR SUBFAMILY 3 GROUP C MEMBER 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(*CP*CP*AP*GP*AP*AP*CP*AP*GP*AP*GP*TP*GP*TP*TP*CP*TP*G)-3');
COMPND 10 CHAIN: C, Z;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-
COMPND 14 D(*TP*CP*AP*GP*AP*AP*CP*AP*CP*TP*CP*TP*GP*TP*TP*CP*TP*G)-3');
COMPND 15 CHAIN: D, Y;
COMPND 16 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: NR3C1, GRL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 15 ORGANISM_TAXID: 32630
KEYWDS DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR W.H.HUDSON,E.A.WEIKUM,E.A.ORTLUND
REVDAT 5 06-MAR-24 5CC1 1 REMARK
REVDAT 4 25-DEC-19 5CC1 1 REMARK
REVDAT 3 20-SEP-17 5CC1 1 JRNL REMARK
REVDAT 2 16-MAR-16 5CC1 1 JRNL
REVDAT 1 23-DEC-15 5CC1 0
JRNL AUTH W.H.HUDSON,B.R.KOSSMANN,I.M.DE VERA,S.W.CHUO,E.R.WEIKUM,
JRNL AUTH 2 G.N.EICK,J.W.THORNTON,I.N.IVANOV,D.J.KOJETIN,E.A.ORTLUND
JRNL TITL DISTAL SUBSTITUTIONS DRIVE DIVERGENT DNA SPECIFICITY AMONG
JRNL TITL 2 PARALOGOUS TRANSCRIPTION FACTORS THROUGH SUBDIVISION OF
JRNL TITL 3 CONFORMATIONAL SPACE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 326 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 26715749
JRNL DOI 10.1073/PNAS.1518960113
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 36667
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1945
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 32.4101 - 5.5397 0.88 2524 141 0.1535 0.1688
REMARK 3 2 5.5397 - 4.4005 0.96 2671 149 0.1748 0.2377
REMARK 3 3 4.4005 - 3.8453 0.95 2614 146 0.1874 0.2355
REMARK 3 4 3.8453 - 3.4942 0.95 2582 145 0.2287 0.2646
REMARK 3 5 3.4942 - 3.2440 0.94 2541 138 0.2603 0.2654
REMARK 3 6 3.2440 - 3.0529 0.95 2589 146 0.3018 0.3489
REMARK 3 7 3.0529 - 2.9001 0.98 2650 149 0.3357 0.3776
REMARK 3 8 2.9001 - 2.7739 0.97 2602 145 0.3565 0.3215
REMARK 3 9 2.7739 - 2.6672 0.97 2622 147 0.3715 0.4039
REMARK 3 10 2.6672 - 2.5752 0.95 2565 145 0.3991 0.5191
REMARK 3 11 2.5752 - 2.4947 0.91 2432 136 0.4104 0.3948
REMARK 3 12 2.4947 - 2.4234 0.86 2294 131 0.4230 0.4673
REMARK 3 13 2.4234 - 2.3596 0.82 2215 124 0.4341 0.4286
REMARK 3 14 2.3596 - 2.3021 0.69 1821 103 0.4516 0.4601
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 50.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.010 3936
REMARK 3 ANGLE : 1.409 5586
REMARK 3 CHIRALITY : 0.058 608
REMARK 3 PLANARITY : 0.009 472
REMARK 3 DIHEDRAL : 24.563 1588
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36884
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 20% PEG 8000, AND 4%
REMARK 280 ETHYLENE GLYCOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 88.36050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.56100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.36050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.56100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, X, Y, Z
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 MET A 393
REMARK 465 HIS A 394
REMARK 465 HIS A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 SER A 400
REMARK 465 SER A 401
REMARK 465 GLY A 402
REMARK 465 VAL A 403
REMARK 465 ASP A 404
REMARK 465 LEU A 405
REMARK 465 GLY A 406
REMARK 465 THR A 407
REMARK 465 GLU A 408
REMARK 465 ASN A 409
REMARK 465 LEU A 410
REMARK 465 TYR A 411
REMARK 465 PHE A 412
REMARK 465 GLN A 413
REMARK 465 SER A 414
REMARK 465 ASN A 415
REMARK 465 ALA A 416
REMARK 465 LYS A 492
REMARK 465 THR A 493
REMARK 465 LYS A 494
REMARK 465 LYS A 495
REMARK 465 LYS A 496
REMARK 465 ILE A 497
REMARK 465 LYS A 498
REMARK 465 GLY A 499
REMARK 465 ILE A 500
REMARK 465 GLN A 501
REMARK 465 GLN A 502
REMARK 465 ALA A 503
REMARK 465 THR A 504
REMARK 465 THR A 505
REMARK 465 GLY A 506
REMARK 465 MET B 393
REMARK 465 HIS B 394
REMARK 465 HIS B 395
REMARK 465 HIS B 396
REMARK 465 HIS B 397
REMARK 465 HIS B 398
REMARK 465 HIS B 399
REMARK 465 SER B 400
REMARK 465 SER B 401
REMARK 465 GLY B 402
REMARK 465 VAL B 403
REMARK 465 ASP B 404
REMARK 465 LEU B 405
REMARK 465 GLY B 406
REMARK 465 THR B 407
REMARK 465 GLU B 408
REMARK 465 ASN B 409
REMARK 465 LEU B 410
REMARK 465 TYR B 411
REMARK 465 PHE B 412
REMARK 465 GLN B 413
REMARK 465 SER B 414
REMARK 465 ASN B 415
REMARK 465 ALA B 416
REMARK 465 PRO B 417
REMARK 465 ARG B 491
REMARK 465 LYS B 492
REMARK 465 THR B 493
REMARK 465 LYS B 494
REMARK 465 LYS B 495
REMARK 465 LYS B 496
REMARK 465 ILE B 497
REMARK 465 LYS B 498
REMARK 465 GLY B 499
REMARK 465 ILE B 500
REMARK 465 GLN B 501
REMARK 465 GLN B 502
REMARK 465 ALA B 503
REMARK 465 THR B 504
REMARK 465 THR B 505
REMARK 465 GLY B 506
REMARK 465 MET W 393
REMARK 465 HIS W 394
REMARK 465 HIS W 395
REMARK 465 HIS W 396
REMARK 465 HIS W 397
REMARK 465 HIS W 398
REMARK 465 HIS W 399
REMARK 465 SER W 400
REMARK 465 SER W 401
REMARK 465 GLY W 402
REMARK 465 VAL W 403
REMARK 465 ASP W 404
REMARK 465 LEU W 405
REMARK 465 GLY W 406
REMARK 465 THR W 407
REMARK 465 GLU W 408
REMARK 465 ASN W 409
REMARK 465 LEU W 410
REMARK 465 TYR W 411
REMARK 465 PHE W 412
REMARK 465 GLN W 413
REMARK 465 SER W 414
REMARK 465 ASN W 415
REMARK 465 ALA W 416
REMARK 465 LYS W 492
REMARK 465 THR W 493
REMARK 465 LYS W 494
REMARK 465 LYS W 495
REMARK 465 LYS W 496
REMARK 465 ILE W 497
REMARK 465 LYS W 498
REMARK 465 GLY W 499
REMARK 465 ILE W 500
REMARK 465 GLN W 501
REMARK 465 GLN W 502
REMARK 465 ALA W 503
REMARK 465 THR W 504
REMARK 465 THR W 505
REMARK 465 GLY W 506
REMARK 465 MET X 393
REMARK 465 HIS X 394
REMARK 465 HIS X 395
REMARK 465 HIS X 396
REMARK 465 HIS X 397
REMARK 465 HIS X 398
REMARK 465 HIS X 399
REMARK 465 SER X 400
REMARK 465 SER X 401
REMARK 465 GLY X 402
REMARK 465 VAL X 403
REMARK 465 ASP X 404
REMARK 465 LEU X 405
REMARK 465 GLY X 406
REMARK 465 THR X 407
REMARK 465 GLU X 408
REMARK 465 ASN X 409
REMARK 465 LEU X 410
REMARK 465 TYR X 411
REMARK 465 PHE X 412
REMARK 465 GLN X 413
REMARK 465 SER X 414
REMARK 465 ASN X 415
REMARK 465 ALA X 416
REMARK 465 PRO X 417
REMARK 465 ARG X 491
REMARK 465 LYS X 492
REMARK 465 THR X 493
REMARK 465 LYS X 494
REMARK 465 LYS X 495
REMARK 465 LYS X 496
REMARK 465 ILE X 497
REMARK 465 LYS X 498
REMARK 465 GLY X 499
REMARK 465 ILE X 500
REMARK 465 GLN X 501
REMARK 465 GLN X 502
REMARK 465 ALA X 503
REMARK 465 THR X 504
REMARK 465 THR X 505
REMARK 465 GLY X 506
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 DT D 12 O3' DT D 12 C3' -0.041
REMARK 500 DT D 17 O3' DT D 17 C3' -0.040
REMARK 500 DT Y 12 O3' DT Y 12 C3' -0.041
REMARK 500 DT Y 17 O3' DT Y 17 C3' -0.043
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 418 C - N - CA ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLN X 452 CB - CA - C ANGL. DEV. = 15.2 DEGREES
REMARK 500 GLN X 452 CA - CB - CG ANGL. DEV. = 17.1 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 VAL A 423 -60.80 -98.84
REMARK 500 ALA A 490 -131.63 47.31
REMARK 500 VAL B 423 -64.57 -102.99
REMARK 500 GLN B 452 -74.44 -55.73
REMARK 500 GLU B 489 -71.07 -61.25
REMARK 500 VAL W 423 -60.92 -97.47
REMARK 500 ALA W 490 -134.53 49.40
REMARK 500 VAL X 423 -65.71 -100.66
REMARK 500 GLN X 452 -169.48 166.74
REMARK 500 GLU X 489 -70.56 -82.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN B 452 HIS B 453 -55.30
REMARK 500 PRO W 417 PRO W 418 148.80
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 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 421 SG
REMARK 620 2 CYS A 424 SG 116.9
REMARK 620 3 CYS A 438 SG 119.6 104.2
REMARK 620 4 CYS A 441 SG 116.3 104.9 91.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 457 SG
REMARK 620 2 CYS A 463 SG 105.6
REMARK 620 3 CYS A 473 SG 114.0 108.6
REMARK 620 4 CYS A 476 SG 114.4 108.9 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 421 SG
REMARK 620 2 CYS B 424 SG 116.5
REMARK 620 3 CYS B 438 SG 117.7 105.8
REMARK 620 4 CYS B 441 SG 107.6 114.0 93.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 457 SG
REMARK 620 2 CYS B 463 SG 101.8
REMARK 620 3 CYS B 473 SG 115.6 115.1
REMARK 620 4 CYS B 476 SG 112.6 108.2 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN W 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS W 421 SG
REMARK 620 2 CYS W 424 SG 116.6
REMARK 620 3 CYS W 438 SG 115.9 105.8
REMARK 620 4 CYS W 441 SG 115.4 107.3 93.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN W 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS W 457 SG
REMARK 620 2 CYS W 463 SG 104.2
REMARK 620 3 CYS W 473 SG 114.6 110.0
REMARK 620 4 CYS W 476 SG 112.3 109.0 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN X 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS X 421 SG
REMARK 620 2 CYS X 424 SG 116.0
REMARK 620 3 CYS X 438 SG 117.3 106.6
REMARK 620 4 CYS X 441 SG 107.7 113.7 93.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN X 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS X 457 SG
REMARK 620 2 CYS X 463 SG 100.5
REMARK 620 3 CYS X 473 SG 113.4 114.5
REMARK 620 4 CYS X 476 SG 113.5 110.0 105.2
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN W 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN W 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN X 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN X 602
DBREF 5CC1 A 417 506 UNP P04150 GCR_HUMAN 391 480
DBREF 5CC1 B 417 506 UNP P04150 GCR_HUMAN 391 480
DBREF 5CC1 C 1 18 PDB 5CC1 5CC1 1 18
DBREF 5CC1 D 1 18 PDB 5CC1 5CC1 1 18
DBREF 5CC1 W 417 506 UNP P04150 GCR_HUMAN 391 480
DBREF 5CC1 X 417 506 UNP P04150 GCR_HUMAN 391 480
DBREF 5CC1 Y 1 18 PDB 5CC1 5CC1 1 18
DBREF 5CC1 Z 1 18 PDB 5CC1 5CC1 1 18
SEQADV 5CC1 MET A 393 UNP P04150 INITIATING METHIONINE
SEQADV 5CC1 HIS A 394 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS A 395 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS A 396 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS A 397 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS A 398 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS A 399 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER A 400 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER A 401 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY A 402 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 VAL A 403 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASP A 404 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU A 405 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY A 406 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 THR A 407 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLU A 408 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN A 409 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU A 410 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 TYR A 411 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 PHE A 412 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLN A 413 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER A 414 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN A 415 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ALA A 416 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY A 425 UNP P04150 SER 399 ENGINEERED MUTATION
SEQADV 5CC1 MET B 393 UNP P04150 INITIATING METHIONINE
SEQADV 5CC1 HIS B 394 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS B 395 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS B 396 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS B 397 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS B 398 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS B 399 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER B 400 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER B 401 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY B 402 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 VAL B 403 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASP B 404 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU B 405 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY B 406 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 THR B 407 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLU B 408 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN B 409 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU B 410 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 TYR B 411 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 PHE B 412 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLN B 413 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER B 414 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN B 415 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ALA B 416 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY B 425 UNP P04150 SER 399 ENGINEERED MUTATION
SEQADV 5CC1 MET W 393 UNP P04150 INITIATING METHIONINE
SEQADV 5CC1 HIS W 394 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS W 395 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS W 396 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS W 397 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS W 398 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS W 399 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER W 400 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER W 401 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY W 402 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 VAL W 403 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASP W 404 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU W 405 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY W 406 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 THR W 407 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLU W 408 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN W 409 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU W 410 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 TYR W 411 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 PHE W 412 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLN W 413 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER W 414 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN W 415 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ALA W 416 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY W 425 UNP P04150 SER 399 ENGINEERED MUTATION
SEQADV 5CC1 MET X 393 UNP P04150 INITIATING METHIONINE
SEQADV 5CC1 HIS X 394 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS X 395 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS X 396 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS X 397 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS X 398 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 HIS X 399 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER X 400 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER X 401 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY X 402 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 VAL X 403 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASP X 404 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU X 405 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY X 406 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 THR X 407 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLU X 408 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN X 409 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 LEU X 410 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 TYR X 411 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 PHE X 412 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLN X 413 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 SER X 414 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ASN X 415 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 ALA X 416 UNP P04150 EXPRESSION TAG
SEQADV 5CC1 GLY X 425 UNP P04150 SER 399 ENGINEERED MUTATION
SEQRES 1 A 114 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 114 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA PRO PRO
SEQRES 3 A 114 LYS LEU CYS LEU VAL CYS GLY ASP GLU ALA SER GLY CYS
SEQRES 4 A 114 HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS VAL PHE
SEQRES 5 A 114 PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR LEU CYS
SEQRES 6 A 114 ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE ARG ARG
SEQRES 7 A 114 LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS LEU GLN
SEQRES 8 A 114 ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS LYS LYS
SEQRES 9 A 114 ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 B 114 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 114 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA PRO PRO
SEQRES 3 B 114 LYS LEU CYS LEU VAL CYS GLY ASP GLU ALA SER GLY CYS
SEQRES 4 B 114 HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS VAL PHE
SEQRES 5 B 114 PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR LEU CYS
SEQRES 6 B 114 ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE ARG ARG
SEQRES 7 B 114 LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS LEU GLN
SEQRES 8 B 114 ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS LYS LYS
SEQRES 9 B 114 ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 C 18 DC DC DA DG DA DA DC DA DG DA DG DT DG
SEQRES 2 C 18 DT DT DC DT DG
SEQRES 1 D 18 DT DC DA DG DA DA DC DA DC DT DC DT DG
SEQRES 2 D 18 DT DT DC DT DG
SEQRES 1 W 114 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 W 114 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA PRO PRO
SEQRES 3 W 114 LYS LEU CYS LEU VAL CYS GLY ASP GLU ALA SER GLY CYS
SEQRES 4 W 114 HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS VAL PHE
SEQRES 5 W 114 PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR LEU CYS
SEQRES 6 W 114 ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE ARG ARG
SEQRES 7 W 114 LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS LEU GLN
SEQRES 8 W 114 ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS LYS LYS
SEQRES 9 W 114 ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 X 114 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 X 114 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA PRO PRO
SEQRES 3 X 114 LYS LEU CYS LEU VAL CYS GLY ASP GLU ALA SER GLY CYS
SEQRES 4 X 114 HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS VAL PHE
SEQRES 5 X 114 PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR LEU CYS
SEQRES 6 X 114 ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE ARG ARG
SEQRES 7 X 114 LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS LEU GLN
SEQRES 8 X 114 ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS LYS LYS
SEQRES 9 X 114 ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 Y 18 DT DC DA DG DA DA DC DA DC DT DC DT DG
SEQRES 2 Y 18 DT DT DC DT DG
SEQRES 1 Z 18 DC DC DA DG DA DA DC DA DG DA DG DT DG
SEQRES 2 Z 18 DT DT DC DT DG
HET ZN A 601 1
HET ZN A 602 1
HET ZN B 601 1
HET ZN B 602 1
HET ZN W 601 1
HET ZN W 602 1
HET ZN X 601 1
HET ZN X 602 1
HETNAM ZN ZINC ION
FORMUL 9 ZN 8(ZN 2+)
FORMUL 17 HOH *20(H2 O)
HELIX 1 AA1 CYS A 438 GLY A 451 1 14
HELIX 2 AA2 ILE A 468 ASN A 472 5 5
HELIX 3 AA3 CYS A 473 GLY A 485 1 13
HELIX 4 AA4 CYS B 438 GLY B 451 1 14
HELIX 5 AA5 ILE B 468 ASN B 472 5 5
HELIX 6 AA6 CYS B 473 ALA B 484 1 12
HELIX 7 AA7 CYS W 438 GLY W 451 1 14
HELIX 8 AA8 ILE W 468 ASN W 472 5 5
HELIX 9 AA9 CYS W 473 GLY W 485 1 13
HELIX 10 AB1 CYS X 438 GLN X 452 1 15
HELIX 11 AB2 ILE X 468 ASN X 472 5 5
HELIX 12 AB3 CYS X 473 ALA X 484 1 12
SHEET 1 AA1 2 GLY A 430 HIS A 432 0
SHEET 2 AA1 2 VAL A 435 THR A 437 -1 O VAL A 435 N HIS A 432
SHEET 1 AA2 2 GLY B 430 HIS B 432 0
SHEET 2 AA2 2 VAL B 435 THR B 437 -1 O VAL B 435 N HIS B 432
SHEET 1 AA3 2 GLY W 430 HIS W 432 0
SHEET 2 AA3 2 VAL W 435 THR W 437 -1 O VAL W 435 N HIS W 432
SHEET 1 AA4 2 GLY X 430 HIS X 432 0
SHEET 2 AA4 2 VAL X 435 THR X 437 -1 O VAL X 435 N HIS X 432
LINK SG CYS A 421 ZN ZN A 601 1555 1555 2.17
LINK SG CYS A 424 ZN ZN A 601 1555 1555 2.35
LINK SG CYS A 438 ZN ZN A 601 1555 1555 2.36
LINK SG CYS A 441 ZN ZN A 601 1555 1555 2.38
LINK SG CYS A 457 ZN ZN A 602 1555 1555 2.23
LINK SG CYS A 463 ZN ZN A 602 1555 1555 2.25
LINK SG CYS A 473 ZN ZN A 602 1555 1555 2.25
LINK SG CYS A 476 ZN ZN A 602 1555 1555 2.25
LINK SG CYS B 421 ZN ZN B 601 1555 1555 2.38
LINK SG CYS B 424 ZN ZN B 601 1555 1555 2.20
LINK SG CYS B 438 ZN ZN B 601 1555 1555 2.45
LINK SG CYS B 441 ZN ZN B 601 1555 1555 2.33
LINK SG CYS B 457 ZN ZN B 602 1555 1555 2.26
LINK SG CYS B 463 ZN ZN B 602 1555 1555 2.27
LINK SG CYS B 473 ZN ZN B 602 1555 1555 2.28
LINK SG CYS B 476 ZN ZN B 602 1555 1555 2.30
LINK SG CYS W 421 ZN ZN W 601 1555 1555 2.13
LINK SG CYS W 424 ZN ZN W 601 1555 1555 2.37
LINK SG CYS W 438 ZN ZN W 601 1555 1555 2.28
LINK SG CYS W 441 ZN ZN W 601 1555 1555 2.40
LINK SG CYS W 457 ZN ZN W 602 1555 1555 2.25
LINK SG CYS W 463 ZN ZN W 602 1555 1555 2.26
LINK SG CYS W 473 ZN ZN W 602 1555 1555 2.27
LINK SG CYS W 476 ZN ZN W 602 1555 1555 2.30
LINK SG CYS X 421 ZN ZN X 601 1555 1555 2.38
LINK SG CYS X 424 ZN ZN X 601 1555 1555 2.21
LINK SG CYS X 438 ZN ZN X 601 1555 1555 2.45
LINK SG CYS X 441 ZN ZN X 601 1555 1555 2.33
LINK SG CYS X 457 ZN ZN X 602 1555 1555 2.23
LINK SG CYS X 463 ZN ZN X 602 1555 1555 2.28
LINK SG CYS X 473 ZN ZN X 602 1555 1555 2.20
LINK SG CYS X 476 ZN ZN X 602 1555 1555 2.32
CISPEP 1 GLN X 452 HIS X 453 0 28.89
SITE 1 AC1 4 CYS A 421 CYS A 424 CYS A 438 CYS A 441
SITE 1 AC2 4 CYS A 457 CYS A 463 CYS A 473 CYS A 476
SITE 1 AC3 4 CYS B 421 CYS B 424 CYS B 438 CYS B 441
SITE 1 AC4 4 CYS B 457 CYS B 463 CYS B 473 CYS B 476
SITE 1 AC5 4 CYS W 421 CYS W 424 CYS W 438 CYS W 441
SITE 1 AC6 4 CYS W 457 CYS W 463 CYS W 473 CYS W 476
SITE 1 AC7 4 CYS X 421 CYS X 424 CYS X 438 CYS X 441
SITE 1 AC8 4 CYS X 457 CYS X 463 CYS X 473 CYS X 476
CRYST1 176.721 39.122 132.099 90.00 101.10 90.00 C 1 2 1 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 0.005659 0.000000 0.001110 0.00000
SCALE2 0.000000 0.025561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007714 0.00000
(ATOM LINES ARE NOT SHOWN.)
END