HEADER SIGNALING PROTEIN 28-JAN-05 1YOV
TITLE INSIGHTS INTO THE UBIQUITIN TRANSFER CASCADE FROM THE REFINED
TITLE 2 STRUCTURE OF THE ACTIVATING ENZYME FOR NEDD8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMYLOID PROTEIN-BINDING PROTEIN 1;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: AMYLOID BETA PRECURSOR PROTEIN-BINDING PROTEIN 1, 59 KDA,
COMPND 5 APP-BP1, PROTOONCOGENE PROTEIN 1, HPP1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UBIQUITIN-ACTIVATING ENZYME E1C;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: NEDD8-ACTIVATING ENZYME E1C, UBIQUITIN-ACTIVATING ENZYME 3
COMPND 11 HOMOLOG;
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: APPBP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: UBE1C, UBA3;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS UBIQUITIN, NEDD8, E1, APPBP1, UBA3, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WALDEN,M.S.PODGORSKI,B.A.SCHULMAN
REVDAT 4 14-FEB-24 1YOV 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1YOV 1 VERSN
REVDAT 2 15-MAR-05 1YOV 1 JRNL
REVDAT 1 08-MAR-05 1YOV 0
SPRSDE 08-MAR-05 1YOV 1NGV
JRNL AUTH H.WALDEN,M.S.PODGORSKI,B.A.SCHULMAN
JRNL TITL INSIGHTS INTO THE UBIQUITIN TRANSFER CASCADE FROM THE
JRNL TITL 2 REFINED STRUCTURE OF THE ACTIVATING ENZYME FOR NEDD8
JRNL REF NATURE V. 422 330 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12646924
JRNL DOI 10.1038/NATURE01456
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 67993
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3445
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14452
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ACCORDING TO AUTHORS:
REMARK 3 THIS IS A CORRECTION OF THE MISALIGNED 2 C-TERMINAL STRANDS,
REMARK 3 AND DATA IS PUBLISHED ACCORDING TO 1Y8X
REMARK 4
REMARK 4 1YOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031763.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; NSLS
REMARK 200 BEAMLINE : 5.0.2; X25
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.15; 0.9799, 0.98, 0.95
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL; NULL
REMARK 200 DETECTOR MANUFACTURER : NULL; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67993
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
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; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PME5500, HEPES, DTT, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 46.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.10000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 99.10000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.80000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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: 6390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 -2
REMARK 465 LYS A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 LEU A 4
REMARK 465 GLY A 5
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 VAL B 3
REMARK 465 ASP B 4
REMARK 465 GLY B 5
REMARK 465 GLY B 6
REMARK 465 CYS B 7
REMARK 465 GLY B 8
REMARK 465 ASP B 9
REMARK 465 THR B 10
REMARK 465 GLY B 11
REMARK 465 PHE B 355
REMARK 465 SER B 356
REMARK 465 PRO B 357
REMARK 465 SER B 358
REMARK 465 ALA B 359
REMARK 465 LYS B 360
REMARK 465 LEU B 385
REMARK 465 GLU B 386
REMARK 465 GLY B 387
REMARK 465 LYS B 388
REMARK 465 ASN B 389
REMARK 465 VAL B 397
REMARK 465 THR B 398
REMARK 465 SER B 399
REMARK 465 ILE B 400
REMARK 465 SER B 409
REMARK 465 LYS B 410
REMARK 465 THR B 411
REMARK 465 LEU B 412
REMARK 465 LYS B 413
REMARK 465 GLU B 414
REMARK 465 LEU B 415
REMARK 465 GLY B 416
REMARK 465 LEU B 417
REMARK 465 VAL B 418
REMARK 465 ASP B 419
REMARK 465 GLY B 420
REMARK 465 GLN B 421
REMARK 465 GLU B 422
REMARK 465 LEU B 438
REMARK 465 HIS B 439
REMARK 465 PHE B 440
REMARK 465 THR B 441
REMARK 465 SER B 442
REMARK 465 MET C -2
REMARK 465 LYS C -1
REMARK 465 LEU C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLN C 3
REMARK 465 LEU C 4
REMARK 465 GLY C 5
REMARK 465 LYS C 6
REMARK 465 LEU C 7
REMARK 465 LEU C 8
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 VAL D 3
REMARK 465 ASP D 4
REMARK 465 GLY D 5
REMARK 465 GLY D 6
REMARK 465 CYS D 7
REMARK 465 GLY D 8
REMARK 465 ASP D 9
REMARK 465 THR D 10
REMARK 465 GLY D 11
REMARK 465 ASP D 12
REMARK 465 TRP D 13
REMARK 465 GLU D 14
REMARK 465 GLY D 15
REMARK 465 ARG D 16
REMARK 465 TRP D 17
REMARK 465 ASN D 18
REMARK 465 PHE D 355
REMARK 465 SER D 356
REMARK 465 PRO D 357
REMARK 465 SER D 358
REMARK 465 ALA D 359
REMARK 465 LYS D 360
REMARK 465 ALA D 383
REMARK 465 THR D 384
REMARK 465 LEU D 385
REMARK 465 GLU D 386
REMARK 465 GLY D 387
REMARK 465 LYS D 388
REMARK 465 VAL D 397
REMARK 465 GLU D 402
REMARK 465 ARG D 403
REMARK 465 THR D 404
REMARK 465 ARG D 405
REMARK 465 PRO D 406
REMARK 465 ASN D 407
REMARK 465 LEU D 408
REMARK 465 SER D 409
REMARK 465 LYS D 410
REMARK 465 THR D 411
REMARK 465 LEU D 412
REMARK 465 LYS D 413
REMARK 465 GLU D 414
REMARK 465 LEU D 415
REMARK 465 GLY D 416
REMARK 465 LEU D 417
REMARK 465 VAL D 418
REMARK 465 ASP D 419
REMARK 465 GLY D 420
REMARK 465 GLN D 421
REMARK 465 GLU D 422
REMARK 465 LEU D 423
REMARK 465 ALA D 424
REMARK 465 LYS D 437
REMARK 465 LEU D 438
REMARK 465 HIS D 439
REMARK 465 PHE D 440
REMARK 465 THR D 441
REMARK 465 SER D 442
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 ARG B 390 CG CD NE CZ NH1 NH2
REMARK 470 THR B 391 OG1 CG2
REMARK 470 LEU B 392 CG CD1 CD2
REMARK 470 TYR B 393 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 394 CG CD1 CD2
REMARK 470 GLN B 395 CG CD OE1 NE2
REMARK 470 SER B 396 OG
REMARK 470 GLU B 401 CG CD OE1 OE2
REMARK 470 GLU B 402 CG CD OE1 OE2
REMARK 470 ARG B 403 CG CD NE CZ NH1 NH2
REMARK 470 THR B 404 OG1 CG2
REMARK 470 ARG B 405 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 407 CG OD1 ND2
REMARK 470 LEU B 408 CG CD1 CD2
REMARK 470 LYS B 437 CG CD CE NZ
REMARK 470 ASN D 389 CG OD1 ND2
REMARK 470 ARG D 390 CG CD NE CZ NH1 NH2
REMARK 470 THR D 391 OG1 CG2
REMARK 470 LEU D 392 CG CD1 CD2
REMARK 470 TYR D 393 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU D 394 CG CD1 CD2
REMARK 470 GLN D 395 CG CD OE1 NE2
REMARK 470 SER D 396 OG
REMARK 470 THR D 398 OG1 CG2
REMARK 470 SER D 399 OG
REMARK 470 ILE D 400 CG1 CG2 CD1
REMARK 470 GLU D 401 CG CD OE1 OE2
REMARK 470 THR D 433 OG1 CG2
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 TRP B 237 O GLU B 240 2.09
REMARK 500 O GLU A 173 O GLN A 512 2.09
REMARK 500 N LYS D 377 OD2 ASP D 427 2.13
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 ASN B 320 C - N - CA ANGL. DEV. = 15.6 DEGREES
REMARK 500 ASN B 320 N - CA - C ANGL. DEV. = 20.8 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 36 -91.27 -81.65
REMARK 500 ALA A 38 45.13 -95.31
REMARK 500 GLU A 106 30.38 -71.03
REMARK 500 ASN A 115 -80.51 -79.25
REMARK 500 SER A 118 -0.47 -58.26
REMARK 500 ILE A 172 -61.49 -100.77
REMARK 500 MET A 204 143.98 -174.11
REMARK 500 GLU A 228 -86.66 -100.85
REMARK 500 ASN A 230 4.24 108.32
REMARK 500 ILE A 233 66.36 76.59
REMARK 500 THR A 236 -62.09 -19.33
REMARK 500 LYS A 238 -81.22 -134.16
REMARK 500 THR A 278 -23.87 -149.34
REMARK 500 THR A 298 -154.03 -136.61
REMARK 500 LYS A 317 -106.27 -102.84
REMARK 500 MET A 332 124.24 -170.90
REMARK 500 ILE A 333 112.51 -33.87
REMARK 500 SER A 367 43.01 -72.68
REMARK 500 ILE A 368 -28.72 -156.58
REMARK 500 GLU A 373 49.66 -147.71
REMARK 500 SER A 374 13.03 -68.42
REMARK 500 GLN A 438 -83.76 -60.84
REMARK 500 VAL A 450 -72.58 -30.42
REMARK 500 PHE A 513 -143.46 -89.77
REMARK 500 ASN A 518 -76.28 174.31
REMARK 500 ARG B 90 -15.40 -157.61
REMARK 500 PHE B 92 -14.98 -46.33
REMARK 500 PRO B 116 -61.45 -24.81
REMARK 500 ASN B 119 69.41 -119.70
REMARK 500 GLU B 205 17.18 -63.24
REMARK 500 PRO B 209 82.90 -58.70
REMARK 500 MET B 221 49.82 -144.80
REMARK 500 LEU B 235 -52.22 -135.14
REMARK 500 LYS B 239 -70.36 -56.42
REMARK 500 ASN B 320 -25.86 51.03
REMARK 500 THR B 369 -75.95 -109.15
REMARK 500 SER B 371 171.47 -49.71
REMARK 500 PRO B 379 -151.94 -61.17
REMARK 500 ALA B 380 109.73 178.79
REMARK 500 LEU B 392 94.07 175.19
REMARK 500 TYR B 393 30.65 93.62
REMARK 500 LEU B 394 56.46 -64.21
REMARK 500 GLN B 395 83.07 -49.01
REMARK 500 THR B 430 148.80 -172.55
REMARK 500 LYS C 12 -72.65 -73.37
REMARK 500 LEU C 19 -72.78 -106.29
REMARK 500 ASN C 37 115.09 -165.04
REMARK 500 ALA C 38 34.13 -70.62
REMARK 500 SER C 79 2.54 -67.83
REMARK 500 LYS C 83 -155.92 -63.45
REMARK 500
REMARK 500 THIS ENTRY HAS 144 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 B 443 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 199 SG
REMARK 620 2 CYS B 202 SG 114.5
REMARK 620 3 CYS B 343 SG 108.6 111.3
REMARK 620 4 CYS B 346 SG 111.9 94.3 115.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 443 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 199 SG
REMARK 620 2 CYS D 202 SG 100.5
REMARK 620 3 CYS D 343 SG 96.6 112.1
REMARK 620 4 CYS D 346 SG 118.1 114.5 113.3
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 B 443
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 443
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R4N RELATED DB: PDB
REMARK 900 RELATED ID: 1R4M RELATED DB: PDB
REMARK 900 RELATED ID: 1TT5 RELATED DB: PDB
REMARK 900 RELATED ID: 1Y8X RELATED DB: PDB
DBREF 1YOV A 1 534 UNP Q13564 ULA1_HUMAN 1 534
DBREF 1YOV C 1 534 UNP Q13564 ULA1_HUMAN 1 534
DBREF 1YOV B 1 442 UNP Q8TBC4 UBA3_HUMAN 22 463
DBREF 1YOV D 1 442 UNP Q8TBC4 UBA3_HUMAN 22 463
SEQADV 1YOV MET A -2 UNP Q13564 CLONING ARTIFACT
SEQADV 1YOV LYS A -1 UNP Q13564 CLONING ARTIFACT
SEQADV 1YOV LEU A 0 UNP Q13564 CLONING ARTIFACT
SEQADV 1YOV MET C -2 UNP Q13564 CLONING ARTIFACT
SEQADV 1YOV LYS C -1 UNP Q13564 CLONING ARTIFACT
SEQADV 1YOV LEU C 0 UNP Q13564 CLONING ARTIFACT
SEQADV 1YOV GLY B -1 UNP Q8TBC4 CLONING ARTIFACT
SEQADV 1YOV SER B 0 UNP Q8TBC4 CLONING ARTIFACT
SEQADV 1YOV GLY D -1 UNP Q8TBC4 CLONING ARTIFACT
SEQADV 1YOV SER D 0 UNP Q8TBC4 CLONING ARTIFACT
SEQRES 1 A 537 MET LYS LEU MET ALA GLN LEU GLY LYS LEU LEU LYS GLU
SEQRES 2 A 537 GLN LYS TYR ASP ARG GLN LEU ARG LEU TRP GLY ASP HIS
SEQRES 3 A 537 GLY GLN GLU ALA LEU GLU SER ALA HIS VAL CYS LEU ILE
SEQRES 4 A 537 ASN ALA THR ALA THR GLY THR GLU ILE LEU LYS ASN LEU
SEQRES 5 A 537 VAL LEU PRO GLY ILE GLY SER PHE THR ILE ILE ASP GLY
SEQRES 6 A 537 ASN GLN VAL SER GLY GLU ASP ALA GLY ASN ASN PHE PHE
SEQRES 7 A 537 LEU GLN ARG SER SER ILE GLY LYS ASN ARG ALA GLU ALA
SEQRES 8 A 537 ALA MET GLU PHE LEU GLN GLU LEU ASN SER ASP VAL SER
SEQRES 9 A 537 GLY SER PHE VAL GLU GLU SER PRO GLU ASN LEU LEU ASP
SEQRES 10 A 537 ASN ASP PRO SER PHE PHE CYS ARG PHE THR VAL VAL VAL
SEQRES 11 A 537 ALA THR GLN LEU PRO GLU SER THR SER LEU ARG LEU ALA
SEQRES 12 A 537 ASP VAL LEU TRP ASN SER GLN ILE PRO LEU LEU ILE CYS
SEQRES 13 A 537 ARG THR TYR GLY LEU VAL GLY TYR MET ARG ILE ILE ILE
SEQRES 14 A 537 LYS GLU HIS PRO VAL ILE GLU SER HIS PRO ASP ASN ALA
SEQRES 15 A 537 LEU GLU ASP LEU ARG LEU ASP LYS PRO PHE PRO GLU LEU
SEQRES 16 A 537 ARG GLU HIS PHE GLN SER TYR ASP LEU ASP HIS MET GLU
SEQRES 17 A 537 LYS LYS ASP HIS SER HIS THR PRO TRP ILE VAL ILE ILE
SEQRES 18 A 537 ALA LYS TYR LEU ALA GLN TRP TYR SER GLU THR ASN GLY
SEQRES 19 A 537 ARG ILE PRO LYS THR TYR LYS GLU LYS GLU ASP PHE ARG
SEQRES 20 A 537 ASP LEU ILE ARG GLN GLY ILE LEU LYS ASN GLU ASN GLY
SEQRES 21 A 537 ALA PRO GLU ASP GLU GLU ASN PHE GLU GLU ALA ILE LYS
SEQRES 22 A 537 ASN VAL ASN THR ALA LEU ASN THR THR GLN ILE PRO SER
SEQRES 23 A 537 SER ILE GLU ASP ILE PHE ASN ASP ASP ARG CYS ILE ASN
SEQRES 24 A 537 ILE THR LYS GLN THR PRO SER PHE TRP ILE LEU ALA ARG
SEQRES 25 A 537 ALA LEU LYS GLU PHE VAL ALA LYS GLU GLY GLN GLY ASN
SEQRES 26 A 537 LEU PRO VAL ARG GLY THR ILE PRO ASP MET ILE ALA ASP
SEQRES 27 A 537 SER GLY LYS TYR ILE LYS LEU GLN ASN VAL TYR ARG GLU
SEQRES 28 A 537 LYS ALA LYS LYS ASP ALA ALA ALA VAL GLY ASN HIS VAL
SEQRES 29 A 537 ALA LYS LEU LEU GLN SER ILE GLY GLN ALA PRO GLU SER
SEQRES 30 A 537 ILE SER GLU LYS GLU LEU LYS LEU LEU CYS SER ASN SER
SEQRES 31 A 537 ALA PHE LEU ARG VAL VAL ARG CYS ARG SER LEU ALA GLU
SEQRES 32 A 537 GLU TYR GLY LEU ASP THR ILE ASN LYS ASP GLU ILE ILE
SEQRES 33 A 537 SER SER MET ASP ASN PRO ASP ASN GLU ILE VAL LEU TYR
SEQRES 34 A 537 LEU MET LEU ARG ALA VAL ASP ARG PHE HIS LYS GLN GLN
SEQRES 35 A 537 GLY ARG TYR PRO GLY VAL SER ASN TYR GLN VAL GLU GLU
SEQRES 36 A 537 ASP ILE GLY LYS LEU LYS SER CYS LEU THR GLY PHE LEU
SEQRES 37 A 537 GLN GLU TYR GLY LEU SER VAL MET VAL LYS ASP ASP TYR
SEQRES 38 A 537 VAL HIS GLU PHE CYS ARG TYR GLY ALA ALA GLU PRO HIS
SEQRES 39 A 537 THR ILE ALA ALA PHE LEU GLY GLY ALA ALA ALA GLN GLU
SEQRES 40 A 537 VAL ILE LYS ILE ILE THR LYS GLN PHE VAL ILE PHE ASN
SEQRES 41 A 537 ASN THR TYR ILE TYR SER GLY MET SER GLN THR SER ALA
SEQRES 42 A 537 THR PHE GLN LEU
SEQRES 1 B 444 GLY SER MET ALA VAL ASP GLY GLY CYS GLY ASP THR GLY
SEQRES 2 B 444 ASP TRP GLU GLY ARG TRP ASN HIS VAL LYS LYS PHE LEU
SEQRES 3 B 444 GLU ARG SER GLY PRO PHE THR HIS PRO ASP PHE GLU PRO
SEQRES 4 B 444 SER THR GLU SER LEU GLN PHE LEU LEU ASP THR CYS LYS
SEQRES 5 B 444 VAL LEU VAL ILE GLY ALA GLY GLY LEU GLY CYS GLU LEU
SEQRES 6 B 444 LEU LYS ASN LEU ALA LEU SER GLY PHE ARG GLN ILE HIS
SEQRES 7 B 444 VAL ILE ASP MET ASP THR ILE ASP VAL SER ASN LEU ASN
SEQRES 8 B 444 ARG GLN PHE LEU PHE ARG PRO LYS ASP ILE GLY ARG PRO
SEQRES 9 B 444 LYS ALA GLU VAL ALA ALA GLU PHE LEU ASN ASP ARG VAL
SEQRES 10 B 444 PRO ASN CYS ASN VAL VAL PRO HIS PHE ASN LYS ILE GLN
SEQRES 11 B 444 ASP PHE ASN ASP THR PHE TYR ARG GLN PHE HIS ILE ILE
SEQRES 12 B 444 VAL CYS GLY LEU ASP SER ILE ILE ALA ARG ARG TRP ILE
SEQRES 13 B 444 ASN GLY MET LEU ILE SER LEU LEU ASN TYR GLU ASP GLY
SEQRES 14 B 444 VAL LEU ASP PRO SER SER ILE VAL PRO LEU ILE ASP GLY
SEQRES 15 B 444 GLY THR GLU GLY PHE LYS GLY ASN ALA ARG VAL ILE LEU
SEQRES 16 B 444 PRO GLY MET THR ALA CYS ILE GLU CYS THR LEU GLU LEU
SEQRES 17 B 444 TYR PRO PRO GLN VAL ASN PHE PRO MET CYS THR ILE ALA
SEQRES 18 B 444 SER MET PRO ARG LEU PRO GLU HIS CYS ILE GLU TYR VAL
SEQRES 19 B 444 ARG MET LEU GLN TRP PRO LYS GLU GLN PRO PHE GLY GLU
SEQRES 20 B 444 GLY VAL PRO LEU ASP GLY ASP ASP PRO GLU HIS ILE GLN
SEQRES 21 B 444 TRP ILE PHE GLN LYS SER LEU GLU ARG ALA SER GLN TYR
SEQRES 22 B 444 ASN ILE ARG GLY VAL THR TYR ARG LEU THR GLN GLY VAL
SEQRES 23 B 444 VAL LYS ARG ILE ILE PRO ALA VAL ALA SER THR ASN ALA
SEQRES 24 B 444 VAL ILE ALA ALA VAL CYS ALA THR GLU VAL PHE LYS ILE
SEQRES 25 B 444 ALA THR SER ALA TYR ILE PRO LEU ASN ASN TYR LEU VAL
SEQRES 26 B 444 PHE ASN ASP VAL ASP GLY LEU TYR THR TYR THR PHE GLU
SEQRES 27 B 444 ALA GLU ARG LYS GLU ASN CYS PRO ALA CYS SER GLN LEU
SEQRES 28 B 444 PRO GLN ASN ILE GLN PHE SER PRO SER ALA LYS LEU GLN
SEQRES 29 B 444 GLU VAL LEU ASP TYR LEU THR ASN SER ALA SER LEU GLN
SEQRES 30 B 444 MET LYS SER PRO ALA ILE THR ALA THR LEU GLU GLY LYS
SEQRES 31 B 444 ASN ARG THR LEU TYR LEU GLN SER VAL THR SER ILE GLU
SEQRES 32 B 444 GLU ARG THR ARG PRO ASN LEU SER LYS THR LEU LYS GLU
SEQRES 33 B 444 LEU GLY LEU VAL ASP GLY GLN GLU LEU ALA VAL ALA ASP
SEQRES 34 B 444 VAL THR THR PRO GLN THR VAL LEU PHE LYS LEU HIS PHE
SEQRES 35 B 444 THR SER
SEQRES 1 C 537 MET LYS LEU MET ALA GLN LEU GLY LYS LEU LEU LYS GLU
SEQRES 2 C 537 GLN LYS TYR ASP ARG GLN LEU ARG LEU TRP GLY ASP HIS
SEQRES 3 C 537 GLY GLN GLU ALA LEU GLU SER ALA HIS VAL CYS LEU ILE
SEQRES 4 C 537 ASN ALA THR ALA THR GLY THR GLU ILE LEU LYS ASN LEU
SEQRES 5 C 537 VAL LEU PRO GLY ILE GLY SER PHE THR ILE ILE ASP GLY
SEQRES 6 C 537 ASN GLN VAL SER GLY GLU ASP ALA GLY ASN ASN PHE PHE
SEQRES 7 C 537 LEU GLN ARG SER SER ILE GLY LYS ASN ARG ALA GLU ALA
SEQRES 8 C 537 ALA MET GLU PHE LEU GLN GLU LEU ASN SER ASP VAL SER
SEQRES 9 C 537 GLY SER PHE VAL GLU GLU SER PRO GLU ASN LEU LEU ASP
SEQRES 10 C 537 ASN ASP PRO SER PHE PHE CYS ARG PHE THR VAL VAL VAL
SEQRES 11 C 537 ALA THR GLN LEU PRO GLU SER THR SER LEU ARG LEU ALA
SEQRES 12 C 537 ASP VAL LEU TRP ASN SER GLN ILE PRO LEU LEU ILE CYS
SEQRES 13 C 537 ARG THR TYR GLY LEU VAL GLY TYR MET ARG ILE ILE ILE
SEQRES 14 C 537 LYS GLU HIS PRO VAL ILE GLU SER HIS PRO ASP ASN ALA
SEQRES 15 C 537 LEU GLU ASP LEU ARG LEU ASP LYS PRO PHE PRO GLU LEU
SEQRES 16 C 537 ARG GLU HIS PHE GLN SER TYR ASP LEU ASP HIS MET GLU
SEQRES 17 C 537 LYS LYS ASP HIS SER HIS THR PRO TRP ILE VAL ILE ILE
SEQRES 18 C 537 ALA LYS TYR LEU ALA GLN TRP TYR SER GLU THR ASN GLY
SEQRES 19 C 537 ARG ILE PRO LYS THR TYR LYS GLU LYS GLU ASP PHE ARG
SEQRES 20 C 537 ASP LEU ILE ARG GLN GLY ILE LEU LYS ASN GLU ASN GLY
SEQRES 21 C 537 ALA PRO GLU ASP GLU GLU ASN PHE GLU GLU ALA ILE LYS
SEQRES 22 C 537 ASN VAL ASN THR ALA LEU ASN THR THR GLN ILE PRO SER
SEQRES 23 C 537 SER ILE GLU ASP ILE PHE ASN ASP ASP ARG CYS ILE ASN
SEQRES 24 C 537 ILE THR LYS GLN THR PRO SER PHE TRP ILE LEU ALA ARG
SEQRES 25 C 537 ALA LEU LYS GLU PHE VAL ALA LYS GLU GLY GLN GLY ASN
SEQRES 26 C 537 LEU PRO VAL ARG GLY THR ILE PRO ASP MET ILE ALA ASP
SEQRES 27 C 537 SER GLY LYS TYR ILE LYS LEU GLN ASN VAL TYR ARG GLU
SEQRES 28 C 537 LYS ALA LYS LYS ASP ALA ALA ALA VAL GLY ASN HIS VAL
SEQRES 29 C 537 ALA LYS LEU LEU GLN SER ILE GLY GLN ALA PRO GLU SER
SEQRES 30 C 537 ILE SER GLU LYS GLU LEU LYS LEU LEU CYS SER ASN SER
SEQRES 31 C 537 ALA PHE LEU ARG VAL VAL ARG CYS ARG SER LEU ALA GLU
SEQRES 32 C 537 GLU TYR GLY LEU ASP THR ILE ASN LYS ASP GLU ILE ILE
SEQRES 33 C 537 SER SER MET ASP ASN PRO ASP ASN GLU ILE VAL LEU TYR
SEQRES 34 C 537 LEU MET LEU ARG ALA VAL ASP ARG PHE HIS LYS GLN GLN
SEQRES 35 C 537 GLY ARG TYR PRO GLY VAL SER ASN TYR GLN VAL GLU GLU
SEQRES 36 C 537 ASP ILE GLY LYS LEU LYS SER CYS LEU THR GLY PHE LEU
SEQRES 37 C 537 GLN GLU TYR GLY LEU SER VAL MET VAL LYS ASP ASP TYR
SEQRES 38 C 537 VAL HIS GLU PHE CYS ARG TYR GLY ALA ALA GLU PRO HIS
SEQRES 39 C 537 THR ILE ALA ALA PHE LEU GLY GLY ALA ALA ALA GLN GLU
SEQRES 40 C 537 VAL ILE LYS ILE ILE THR LYS GLN PHE VAL ILE PHE ASN
SEQRES 41 C 537 ASN THR TYR ILE TYR SER GLY MET SER GLN THR SER ALA
SEQRES 42 C 537 THR PHE GLN LEU
SEQRES 1 D 444 GLY SER MET ALA VAL ASP GLY GLY CYS GLY ASP THR GLY
SEQRES 2 D 444 ASP TRP GLU GLY ARG TRP ASN HIS VAL LYS LYS PHE LEU
SEQRES 3 D 444 GLU ARG SER GLY PRO PHE THR HIS PRO ASP PHE GLU PRO
SEQRES 4 D 444 SER THR GLU SER LEU GLN PHE LEU LEU ASP THR CYS LYS
SEQRES 5 D 444 VAL LEU VAL ILE GLY ALA GLY GLY LEU GLY CYS GLU LEU
SEQRES 6 D 444 LEU LYS ASN LEU ALA LEU SER GLY PHE ARG GLN ILE HIS
SEQRES 7 D 444 VAL ILE ASP MET ASP THR ILE ASP VAL SER ASN LEU ASN
SEQRES 8 D 444 ARG GLN PHE LEU PHE ARG PRO LYS ASP ILE GLY ARG PRO
SEQRES 9 D 444 LYS ALA GLU VAL ALA ALA GLU PHE LEU ASN ASP ARG VAL
SEQRES 10 D 444 PRO ASN CYS ASN VAL VAL PRO HIS PHE ASN LYS ILE GLN
SEQRES 11 D 444 ASP PHE ASN ASP THR PHE TYR ARG GLN PHE HIS ILE ILE
SEQRES 12 D 444 VAL CYS GLY LEU ASP SER ILE ILE ALA ARG ARG TRP ILE
SEQRES 13 D 444 ASN GLY MET LEU ILE SER LEU LEU ASN TYR GLU ASP GLY
SEQRES 14 D 444 VAL LEU ASP PRO SER SER ILE VAL PRO LEU ILE ASP GLY
SEQRES 15 D 444 GLY THR GLU GLY PHE LYS GLY ASN ALA ARG VAL ILE LEU
SEQRES 16 D 444 PRO GLY MET THR ALA CYS ILE GLU CYS THR LEU GLU LEU
SEQRES 17 D 444 TYR PRO PRO GLN VAL ASN PHE PRO MET CYS THR ILE ALA
SEQRES 18 D 444 SER MET PRO ARG LEU PRO GLU HIS CYS ILE GLU TYR VAL
SEQRES 19 D 444 ARG MET LEU GLN TRP PRO LYS GLU GLN PRO PHE GLY GLU
SEQRES 20 D 444 GLY VAL PRO LEU ASP GLY ASP ASP PRO GLU HIS ILE GLN
SEQRES 21 D 444 TRP ILE PHE GLN LYS SER LEU GLU ARG ALA SER GLN TYR
SEQRES 22 D 444 ASN ILE ARG GLY VAL THR TYR ARG LEU THR GLN GLY VAL
SEQRES 23 D 444 VAL LYS ARG ILE ILE PRO ALA VAL ALA SER THR ASN ALA
SEQRES 24 D 444 VAL ILE ALA ALA VAL CYS ALA THR GLU VAL PHE LYS ILE
SEQRES 25 D 444 ALA THR SER ALA TYR ILE PRO LEU ASN ASN TYR LEU VAL
SEQRES 26 D 444 PHE ASN ASP VAL ASP GLY LEU TYR THR TYR THR PHE GLU
SEQRES 27 D 444 ALA GLU ARG LYS GLU ASN CYS PRO ALA CYS SER GLN LEU
SEQRES 28 D 444 PRO GLN ASN ILE GLN PHE SER PRO SER ALA LYS LEU GLN
SEQRES 29 D 444 GLU VAL LEU ASP TYR LEU THR ASN SER ALA SER LEU GLN
SEQRES 30 D 444 MET LYS SER PRO ALA ILE THR ALA THR LEU GLU GLY LYS
SEQRES 31 D 444 ASN ARG THR LEU TYR LEU GLN SER VAL THR SER ILE GLU
SEQRES 32 D 444 GLU ARG THR ARG PRO ASN LEU SER LYS THR LEU LYS GLU
SEQRES 33 D 444 LEU GLY LEU VAL ASP GLY GLN GLU LEU ALA VAL ALA ASP
SEQRES 34 D 444 VAL THR THR PRO GLN THR VAL LEU PHE LYS LEU HIS PHE
SEQRES 35 D 444 THR SER
HET ZN B 443 1
HET ZN D 443 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *150(H2 O)
HELIX 1 1 LYS A 6 TYR A 13 1 8
HELIX 2 2 TYR A 13 ALA A 31 1 19
HELIX 3 3 THR A 39 LEU A 51 1 13
HELIX 4 4 SER A 66 ASN A 73 1 8
HELIX 5 5 GLN A 77 ILE A 81 5 5
HELIX 6 6 ASN A 84 GLU A 95 1 12
HELIX 7 7 SER A 108 ASN A 115 1 8
HELIX 8 8 ASP A 116 PHE A 123 5 8
HELIX 9 9 PRO A 132 GLN A 147 1 16
HELIX 10 10 PHE A 189 SER A 198 1 10
HELIX 11 11 GLU A 205 SER A 210 1 6
HELIX 12 12 PRO A 213 THR A 229 1 17
HELIX 13 13 LYS A 238 GLN A 249 1 12
HELIX 14 14 GLU A 262 LEU A 276 1 15
HELIX 15 15 PRO A 282 ASN A 290 1 9
HELIX 16 16 ASP A 291 ASN A 296 1 6
HELIX 17 17 PRO A 302 LYS A 317 1 16
HELIX 18 18 ASP A 335 SER A 367 1 33
HELIX 19 19 SER A 376 ASN A 386 1 11
HELIX 20 20 SER A 397 GLY A 403 1 7
HELIX 21 21 ASN A 408 MET A 416 1 9
HELIX 22 22 GLU A 422 GLN A 439 1 18
HELIX 23 23 GLN A 449 TYR A 468 1 20
HELIX 24 24 LYS A 475 TYR A 485 1 11
HELIX 25 25 PRO A 490 LYS A 511 1 22
HELIX 26 26 TRP B 17 ARG B 26 1 10
HELIX 27 27 GLU B 40 CYS B 49 1 10
HELIX 28 28 LEU B 59 LEU B 69 1 11
HELIX 29 29 ASP B 84 ARG B 90 5 7
HELIX 30 30 ARG B 95 ILE B 99 5 5
HELIX 31 31 PRO B 102 VAL B 115 1 14
HELIX 32 32 LYS B 126 PHE B 130 5 5
HELIX 33 33 ASN B 131 ARG B 136 1 6
HELIX 34 34 SER B 147 LEU B 161 1 15
HELIX 35 35 PRO B 171 ILE B 174 5 4
HELIX 36 36 CYS B 199 TYR B 207 5 9
HELIX 37 37 PRO B 214 MET B 221 1 8
HELIX 38 38 LEU B 224 LEU B 235 1 12
HELIX 39 39 LEU B 235 GLU B 240 1 6
HELIX 40 40 ASP B 253 TYR B 271 1 19
HELIX 41 41 THR B 277 LYS B 286 1 10
HELIX 42 42 VAL B 292 SER B 313 1 22
HELIX 43 43 GLU B 363 LEU B 368 1 6
HELIX 44 44 GLU B 401 ARG B 405 5 5
HELIX 45 45 TYR C 13 ALA C 31 1 19
HELIX 46 46 THR C 39 LEU C 51 1 13
HELIX 47 47 SER C 66 ASN C 73 1 8
HELIX 48 48 ASN C 84 ASN C 97 1 14
HELIX 49 49 SER C 108 ASP C 116 1 9
HELIX 50 50 PRO C 117 PHE C 123 5 7
HELIX 51 51 PRO C 132 SER C 146 1 15
HELIX 52 52 PHE C 189 GLN C 197 1 9
HELIX 53 53 ASP C 200 MET C 204 5 5
HELIX 54 54 GLU C 205 SER C 210 1 6
HELIX 55 55 PRO C 213 TYR C 226 1 14
HELIX 56 56 THR C 236 GLN C 249 1 14
HELIX 57 57 GLU C 262 LEU C 276 1 15
HELIX 58 58 PRO C 282 ASN C 290 1 9
HELIX 59 59 ASP C 291 ASN C 296 1 6
HELIX 60 60 PRO C 302 LYS C 317 1 16
HELIX 61 61 ASP C 335 GLY C 369 1 35
HELIX 62 62 GLU C 377 CYS C 384 1 8
HELIX 63 63 ASN C 386 LEU C 390 5 5
HELIX 64 64 SER C 397 GLY C 403 1 7
HELIX 65 65 ASN C 408 MET C 416 1 9
HELIX 66 66 GLU C 422 GLY C 440 1 19
HELIX 67 67 GLN C 449 GLY C 469 1 21
HELIX 68 68 ASP C 476 TYR C 485 1 10
HELIX 69 69 PRO C 490 LYS C 511 1 22
HELIX 70 70 LEU D 42 ASP D 47 1 6
HELIX 71 71 GLY D 57 LEU D 69 1 13
HELIX 72 72 ASP D 84 LEU D 88 5 5
HELIX 73 73 PRO D 102 VAL D 115 1 14
HELIX 74 74 LYS D 126 PHE D 130 5 5
HELIX 75 75 PHE D 134 PHE D 138 5 5
HELIX 76 76 SER D 147 LEU D 161 1 15
HELIX 77 77 PRO D 171 ILE D 174 5 4
HELIX 78 78 ILE D 200 LEU D 204 5 5
HELIX 79 79 PRO D 214 SER D 220 1 7
HELIX 80 80 LEU D 224 ARG D 233 1 10
HELIX 81 81 GLN D 236 GLN D 241 1 6
HELIX 82 82 HIS D 256 LEU D 265 1 10
HELIX 83 83 GLU D 266 TYR D 271 1 6
HELIX 84 84 THR D 277 LYS D 286 1 10
HELIX 85 85 VAL D 292 SER D 313 1 22
HELIX 86 86 GLU D 363 SER D 371 1 9
SHEET 1 A 8 PHE A 104 VAL A 105 0
SHEET 2 A 8 SER A 56 ILE A 60 1 N ILE A 59 O VAL A 105
SHEET 3 A 8 HIS A 32 LEU A 35 1 N LEU A 35 O THR A 58
SHEET 4 A 8 VAL A 125 THR A 129 1 O VAL A 127 N CYS A 34
SHEET 5 A 8 LEU A 150 TYR A 156 1 O CYS A 153 N ALA A 128
SHEET 6 A 8 VAL A 159 ILE A 165 -1 O ARG A 163 N ILE A 152
SHEET 7 A 8 THR A 519 SER A 523 -1 O TYR A 520 N MET A 162
SHEET 8 A 8 THR A 528 PHE A 532 -1 O PHE A 532 N THR A 519
SHEET 1 B 2 HIS A 169 VAL A 171 0
SHEET 2 B 2 ARG A 391 VAL A 393 -1 O VAL A 393 N HIS A 169
SHEET 1 C 8 VAL B 121 HIS B 123 0
SHEET 2 C 8 ILE B 75 ILE B 78 1 N ILE B 75 O VAL B 121
SHEET 3 C 8 VAL B 51 ILE B 54 1 N VAL B 53 O HIS B 76
SHEET 4 C 8 ILE B 140 CYS B 143 1 O VAL B 142 N ILE B 54
SHEET 5 C 8 LEU B 177 GLU B 183 1 O ILE B 178 N CYS B 143
SHEET 6 C 8 LYS B 186 ILE B 192 -1 O LYS B 186 N GLU B 183
SHEET 7 C 8 TYR B 321 ASN B 325 -1 O LEU B 322 N ALA B 189
SHEET 8 C 8 TYR B 331 PHE B 335 -1 O TYR B 333 N VAL B 323
SHEET 1 D 2 TYR B 164 GLU B 165 0
SHEET 2 D 2 VAL B 168 LEU B 169 -1 O VAL B 168 N GLU B 165
SHEET 1 E 2 GLN B 351 ASN B 352 0
SHEET 2 E 2 PHE B 436 LYS B 437 1 O LYS B 437 N GLN B 351
SHEET 1 F 2 ILE B 381 THR B 382 0
SHEET 2 F 2 THR B 391 LEU B 392 -1 O LEU B 392 N ILE B 381
SHEET 1 G 8 SER C 101 SER C 103 0
SHEET 2 G 8 SER C 56 THR C 58 1 N PHE C 57 O SER C 103
SHEET 3 G 8 HIS C 32 LEU C 35 1 N VAL C 33 O SER C 56
SHEET 4 G 8 VAL C 126 THR C 129 1 O VAL C 127 N CYS C 34
SHEET 5 G 8 LEU C 150 TYR C 156 1 O CYS C 153 N ALA C 128
SHEET 6 G 8 VAL C 159 ILE C 165 -1 O ARG C 163 N ILE C 152
SHEET 7 G 8 TYR C 520 SER C 523 -1 O TYR C 522 N GLY C 160
SHEET 8 G 8 THR C 528 THR C 531 -1 O THR C 528 N SER C 523
SHEET 1 H 2 HIS C 169 VAL C 171 0
SHEET 2 H 2 ARG C 391 VAL C 393 -1 O VAL C 393 N HIS C 169
SHEET 1 I 8 ASN D 119 HIS D 123 0
SHEET 2 I 8 GLN D 74 ILE D 78 1 N ILE D 75 O VAL D 121
SHEET 3 I 8 VAL D 51 ILE D 54 1 N VAL D 53 O HIS D 76
SHEET 4 I 8 ILE D 140 CYS D 143 1 O VAL D 142 N ILE D 54
SHEET 5 I 8 LEU D 177 GLU D 183 1 O ILE D 178 N CYS D 143
SHEET 6 I 8 LYS D 186 ILE D 192 -1 O ILE D 192 N LEU D 177
SHEET 7 I 8 LEU D 322 ASN D 325 -1 O LEU D 322 N ALA D 189
SHEET 8 I 8 TYR D 331 THR D 334 -1 O TYR D 331 N ASN D 325
SHEET 1 J 2 TYR D 164 GLU D 165 0
SHEET 2 J 2 VAL D 168 LEU D 169 -1 O VAL D 168 N GLU D 165
SHEET 1 K 2 ALA D 380 ILE D 381 0
SHEET 2 K 2 TYR D 393 LEU D 394 -1 O TYR D 393 N ILE D 381
LINK SG CYS B 199 ZN ZN B 443 1555 1555 2.52
LINK SG CYS B 202 ZN ZN B 443 1555 1555 2.44
LINK SG CYS B 343 ZN ZN B 443 1555 1555 2.35
LINK SG CYS B 346 ZN ZN B 443 1555 1555 2.31
LINK SG CYS D 199 ZN ZN D 443 1555 1555 2.45
LINK SG CYS D 202 ZN ZN D 443 1555 1555 2.54
LINK SG CYS D 343 ZN ZN D 443 1555 1555 2.46
LINK SG CYS D 346 ZN ZN D 443 1555 1555 2.27
SITE 1 AC1 4 CYS B 199 CYS B 202 CYS B 343 CYS B 346
SITE 1 AC2 4 CYS D 199 CYS D 202 CYS D 343 CYS D 346
CRYST1 92.400 123.600 198.200 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010823 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005045 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
