HEADER OXIDOREDUCTASE 30-DEC-99 1DQA
TITLE COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG,
TITLE 2 COA, AND NADP+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (HMG-COA REDUCTASE);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC PORTION;
COMPND 5 EC: 1.1.1.34;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS OXIDOREDUCTASE, CHOLESTEROL BIOSYNTHESIS, HMG-COA, NADPH
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.ISTVAN,M.PALNITKAR,S.K.BUCHANAN,J.DEISENHOFER
REVDAT 4 07-FEB-24 1DQA 1 REMARK SEQADV
REVDAT 3 14-MAR-18 1DQA 1 SEQADV
REVDAT 2 24-FEB-09 1DQA 1 VERSN
REVDAT 1 08-MAR-00 1DQA 0
JRNL AUTH E.S.ISTVAN,M.PALNITKAR,S.K.BUCHANAN,J.DEISENHOFER
JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC PORTION OF HUMAN HMG-COA
JRNL TITL 2 REDUCTASE: INSIGHTS INTO REGULATION OF ACTIVITY AND
JRNL TITL 3 CATALYSIS.
JRNL REF EMBO J. V. 19 819 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10698924
JRNL DOI 10.1093/EMBOJ/19.5.819
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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 : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 109701
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2186
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 17197
REMARK 3 BIN R VALUE (WORKING SET) : 0.1620
REMARK 3 BIN FREE R VALUE : 0.2050
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 371
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 428
REMARK 3 SOLVENT ATOMS : 471
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.61000
REMARK 3 B22 (A**2) : 0.77000
REMARK 3 B33 (A**2) : 1.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.80000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.06
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.460
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.540 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.620 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 25.26
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 : PROTEIN.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : CIS.PARAM
REMARK 3 PARAMETER FILE 4 : LIG.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : LIG.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.083
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109778
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 44.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.19300
REMARK 200 R SYM FOR SHELL (I) : 0.19300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 86.31500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 38160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 422
REMARK 465 ALA A 423
REMARK 465 MET A 424
REMARK 465 ALA A 425
REMARK 465 SER A 426
REMARK 465 SER A 427
REMARK 465 VAL A 428
REMARK 465 LEU A 429
REMARK 465 VAL A 430
REMARK 465 THR A 431
REMARK 465 GLN A 432
REMARK 465 GLU A 433
REMARK 465 PRO A 434
REMARK 465 GLU A 435
REMARK 465 ILE A 436
REMARK 465 GLU A 437
REMARK 465 LEU A 438
REMARK 465 PRO A 439
REMARK 465 ARG A 440
REMARK 465 GLU A 441
REMARK 465 PRO A 442
REMARK 465 ARG A 443
REMARK 465 PRO A 444
REMARK 465 ASN A 445
REMARK 465 GLU A 446
REMARK 465 GLU A 447
REMARK 465 CYS A 448
REMARK 465 LEU A 449
REMARK 465 GLN A 450
REMARK 465 ILE A 451
REMARK 465 LEU A 452
REMARK 465 GLY A 453
REMARK 465 ASN A 454
REMARK 465 ALA A 455
REMARK 465 GLU A 456
REMARK 465 LYS A 457
REMARK 465 GLY A 458
REMARK 465 ALA A 459
REMARK 465 LYS A 460
REMARK 465 PHE A 461
REMARK 465 ARG A 871
REMARK 465 SER A 872
REMARK 465 LYS A 873
REMARK 465 ILE A 874
REMARK 465 ASN A 875
REMARK 465 LEU A 876
REMARK 465 GLN A 877
REMARK 465 ASP A 878
REMARK 465 LEU A 879
REMARK 465 GLN A 880
REMARK 465 GLY A 881
REMARK 465 ALA A 882
REMARK 465 CYS A 883
REMARK 465 THR A 884
REMARK 465 LYS A 885
REMARK 465 LYS A 886
REMARK 465 THR A 887
REMARK 465 ALA A 888
REMARK 465 GLY B 422
REMARK 465 ALA B 423
REMARK 465 MET B 424
REMARK 465 ALA B 425
REMARK 465 SER B 426
REMARK 465 SER B 427
REMARK 465 VAL B 428
REMARK 465 LEU B 429
REMARK 465 VAL B 430
REMARK 465 THR B 431
REMARK 465 GLN B 432
REMARK 465 GLU B 433
REMARK 465 PRO B 434
REMARK 465 GLU B 435
REMARK 465 ILE B 436
REMARK 465 GLU B 437
REMARK 465 LEU B 438
REMARK 465 PRO B 439
REMARK 465 ARG B 440
REMARK 465 GLU B 441
REMARK 465 PRO B 442
REMARK 465 ARG B 443
REMARK 465 PRO B 444
REMARK 465 ASN B 445
REMARK 465 GLU B 446
REMARK 465 GLU B 447
REMARK 465 CYS B 448
REMARK 465 LEU B 449
REMARK 465 GLN B 450
REMARK 465 ILE B 451
REMARK 465 LEU B 452
REMARK 465 GLY B 453
REMARK 465 ASN B 454
REMARK 465 ALA B 455
REMARK 465 GLU B 456
REMARK 465 LYS B 457
REMARK 465 GLY B 458
REMARK 465 ALA B 459
REMARK 465 LYS B 460
REMARK 465 PHE B 461
REMARK 465 MET B 867
REMARK 465 ILE B 868
REMARK 465 HIS B 869
REMARK 465 ASN B 870
REMARK 465 ARG B 871
REMARK 465 SER B 872
REMARK 465 LYS B 873
REMARK 465 ILE B 874
REMARK 465 ASN B 875
REMARK 465 LEU B 876
REMARK 465 GLN B 877
REMARK 465 ASP B 878
REMARK 465 LEU B 879
REMARK 465 GLN B 880
REMARK 465 GLY B 881
REMARK 465 ALA B 882
REMARK 465 CYS B 883
REMARK 465 THR B 884
REMARK 465 LYS B 885
REMARK 465 LYS B 886
REMARK 465 THR B 887
REMARK 465 ALA B 888
REMARK 465 GLY C 422
REMARK 465 ALA C 423
REMARK 465 MET C 424
REMARK 465 ALA C 425
REMARK 465 SER C 426
REMARK 465 SER C 427
REMARK 465 VAL C 428
REMARK 465 LEU C 429
REMARK 465 VAL C 430
REMARK 465 THR C 431
REMARK 465 GLN C 432
REMARK 465 GLU C 433
REMARK 465 PRO C 434
REMARK 465 GLU C 435
REMARK 465 ILE C 436
REMARK 465 GLU C 437
REMARK 465 LEU C 438
REMARK 465 PRO C 439
REMARK 465 ARG C 440
REMARK 465 GLU C 441
REMARK 465 PRO C 442
REMARK 465 ARG C 443
REMARK 465 PRO C 444
REMARK 465 ASN C 445
REMARK 465 GLU C 446
REMARK 465 GLU C 447
REMARK 465 CYS C 448
REMARK 465 LEU C 449
REMARK 465 GLN C 450
REMARK 465 ILE C 451
REMARK 465 LEU C 452
REMARK 465 GLY C 453
REMARK 465 ASN C 454
REMARK 465 ALA C 455
REMARK 465 GLU C 456
REMARK 465 LYS C 457
REMARK 465 GLY C 458
REMARK 465 ALA C 459
REMARK 465 LYS C 460
REMARK 465 PHE C 461
REMARK 465 LEU C 462
REMARK 465 SER C 463
REMARK 465 ASP C 464
REMARK 465 ALA C 465
REMARK 465 GLU C 466
REMARK 465 ILE C 467
REMARK 465 SER C 872
REMARK 465 LYS C 873
REMARK 465 ILE C 874
REMARK 465 ASN C 875
REMARK 465 LEU C 876
REMARK 465 GLN C 877
REMARK 465 ASP C 878
REMARK 465 LEU C 879
REMARK 465 GLN C 880
REMARK 465 GLY C 881
REMARK 465 ALA C 882
REMARK 465 CYS C 883
REMARK 465 THR C 884
REMARK 465 LYS C 885
REMARK 465 LYS C 886
REMARK 465 THR C 887
REMARK 465 ALA C 888
REMARK 465 GLY D 422
REMARK 465 ALA D 423
REMARK 465 MET D 424
REMARK 465 ALA D 425
REMARK 465 SER D 426
REMARK 465 SER D 427
REMARK 465 VAL D 428
REMARK 465 LEU D 429
REMARK 465 VAL D 430
REMARK 465 THR D 431
REMARK 465 GLN D 432
REMARK 465 GLU D 433
REMARK 465 PRO D 434
REMARK 465 GLU D 435
REMARK 465 ILE D 436
REMARK 465 GLU D 437
REMARK 465 LEU D 438
REMARK 465 PRO D 439
REMARK 465 ARG D 440
REMARK 465 GLU D 441
REMARK 465 PRO D 442
REMARK 465 ARG D 443
REMARK 465 PRO D 444
REMARK 465 ASN D 445
REMARK 465 GLU D 446
REMARK 465 GLU D 447
REMARK 465 CYS D 448
REMARK 465 LEU D 449
REMARK 465 GLN D 450
REMARK 465 ILE D 451
REMARK 465 LEU D 452
REMARK 465 GLY D 453
REMARK 465 ASN D 454
REMARK 465 ALA D 455
REMARK 465 GLU D 456
REMARK 465 LYS D 457
REMARK 465 GLY D 458
REMARK 465 ALA D 459
REMARK 465 LYS D 460
REMARK 465 PHE D 461
REMARK 465 LEU D 462
REMARK 465 SER D 463
REMARK 465 ASP D 464
REMARK 465 ALA D 465
REMARK 465 GLU D 466
REMARK 465 ILE D 467
REMARK 465 ILE D 468
REMARK 465 GLN D 469
REMARK 465 LEU D 470
REMARK 465 VAL D 471
REMARK 465 ASN D 472
REMARK 465 ALA D 473
REMARK 465 LYS D 474
REMARK 465 HIS D 475
REMARK 465 ILE D 476
REMARK 465 LYS D 873
REMARK 465 ILE D 874
REMARK 465 ASN D 875
REMARK 465 LEU D 876
REMARK 465 GLN D 877
REMARK 465 ASP D 878
REMARK 465 LEU D 879
REMARK 465 GLN D 880
REMARK 465 GLY D 881
REMARK 465 ALA D 882
REMARK 465 CYS D 883
REMARK 465 THR D 884
REMARK 465 LYS D 885
REMARK 465 LYS D 886
REMARK 465 THR D 887
REMARK 465 ALA D 888
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 ARG B 495 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 495 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 PRO B 786 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG C 590 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG C 590 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG D 495 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG D 568 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG D 590 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU D 596 CA - CB - CG ANGL. DEV. = -13.8 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 HIS A 475 52.34 17.61
REMARK 500 TYR A 514 -23.33 -153.27
REMARK 500 ALA A 525 -38.97 -148.24
REMARK 500 CYS A 561 -24.90 84.27
REMARK 500 SER A 651 32.13 -150.41
REMARK 500 LYS A 735 -62.08 -106.28
REMARK 500 LEU A 737 -68.00 -105.65
REMARK 500 TYR A 749 56.74 -97.01
REMARK 500 HIS A 752 43.05 -155.25
REMARK 500 SER A 799 56.91 -140.35
REMARK 500 LEU B 484 -38.07 -174.75
REMARK 500 THR B 487 108.23 -179.17
REMARK 500 TYR B 514 -23.58 -155.51
REMARK 500 ALA B 525 -41.96 -143.49
REMARK 500 CYS B 527 148.32 -173.40
REMARK 500 CYS B 561 -16.34 84.47
REMARK 500 SER B 651 32.75 -153.81
REMARK 500 LYS B 735 -60.28 -101.05
REMARK 500 LEU B 737 -69.00 -103.60
REMARK 500 TYR B 749 58.94 -95.16
REMARK 500 HIS B 752 44.32 -154.20
REMARK 500 SER B 799 57.08 -140.59
REMARK 500 ASN B 830 90.25 -164.00
REMARK 500 LYS B 864 -3.72 -51.70
REMARK 500 SER B 865 -54.96 -122.45
REMARK 500 TYR C 514 -18.41 -154.97
REMARK 500 ALA C 525 -39.34 -140.62
REMARK 500 CYS C 561 -26.03 90.11
REMARK 500 SER C 651 32.04 -150.89
REMARK 500 LYS C 735 -62.03 -101.89
REMARK 500 LEU C 737 -66.52 -105.77
REMARK 500 TYR C 749 58.52 -92.53
REMARK 500 HIS C 752 42.12 -151.93
REMARK 500 ASN C 830 79.19 -160.25
REMARK 500 GLU D 486 -79.68 -74.61
REMARK 500 TYR D 514 -25.35 -156.82
REMARK 500 ASN D 518 71.68 -69.96
REMARK 500 ALA D 525 -33.87 -136.44
REMARK 500 CYS D 527 149.10 -171.51
REMARK 500 CYS D 561 -26.30 86.62
REMARK 500 SER D 651 34.66 -152.26
REMARK 500 THR D 723 -159.56 -154.23
REMARK 500 LYS D 735 -60.93 -101.12
REMARK 500 LEU D 737 -66.08 -106.35
REMARK 500 TYR D 749 53.06 -94.44
REMARK 500 HIS D 752 43.82 -154.25
REMARK 500 SER D 799 54.25 -140.12
REMARK 500 ASN D 830 82.29 -152.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 749 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA C 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAH C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 4
DBREF 1DQA A 422 888 UNP P04035 HMDH_HUMAN 422 888
DBREF 1DQA B 422 888 UNP P04035 HMDH_HUMAN 422 888
DBREF 1DQA C 422 888 UNP P04035 HMDH_HUMAN 422 888
DBREF 1DQA D 422 888 UNP P04035 HMDH_HUMAN 422 888
SEQADV 1DQA ILE A 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 1DQA ILE B 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 1DQA ILE C 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQADV 1DQA ILE D 485 UNP P04035 MET 485 ENGINEERED MUTATION
SEQRES 1 A 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 A 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 A 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 A 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 A 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 A 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 A 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 A 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 A 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 A 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 A 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 A 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 A 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 A 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 A 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 A 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 A 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 A 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 A 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 A 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 A 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 A 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 A 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 A 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 A 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 A 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 A 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 A 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 A 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 A 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 A 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 A 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 A 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 A 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 A 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 A 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
SEQRES 1 B 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 B 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 B 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 B 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 B 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 B 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 B 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 B 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 B 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 B 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 B 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 B 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 B 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 B 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 B 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 B 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 B 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 B 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 B 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 B 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 B 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 B 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 B 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 B 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 B 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 B 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 B 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 B 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 B 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 B 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 B 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 B 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 B 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 B 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 B 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 B 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
SEQRES 1 C 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 C 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 C 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 C 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 C 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 C 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 C 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 C 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 C 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 C 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 C 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 C 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 C 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 C 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 C 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 C 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 C 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 C 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 C 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 C 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 C 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 C 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 C 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 C 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 C 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 C 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 C 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 C 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 C 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 C 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 C 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 C 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 C 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 C 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 C 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 C 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
SEQRES 1 D 467 GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO
SEQRES 2 D 467 GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU
SEQRES 3 D 467 CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS
SEQRES 4 D 467 PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA
SEQRES 5 D 467 LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU
SEQRES 6 D 467 THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU
SEQRES 7 D 467 SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU
SEQRES 8 D 467 PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA
SEQRES 9 D 467 CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL
SEQRES 10 D 467 GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE
SEQRES 11 D 467 GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA
SEQRES 12 D 467 SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY
SEQRES 13 D 467 GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG
SEQRES 14 D 467 GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA
SEQRES 15 D 467 GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA
SEQRES 16 D 467 VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA
SEQRES 17 D 467 ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN
SEQRES 18 D 467 LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET
SEQRES 19 D 467 GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU
SEQRES 20 D 467 SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU
SEQRES 21 D 467 ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA
SEQRES 22 D 467 ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL
SEQRES 23 D 467 CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL
SEQRES 24 D 467 LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE
SEQRES 25 D 467 ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE
SEQRES 26 D 467 GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA
SEQRES 27 D 467 ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL
SEQRES 28 D 467 GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY
SEQRES 29 D 467 PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO
SEQRES 30 D 467 SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU
SEQRES 31 D 467 LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN
SEQRES 32 D 467 GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN
SEQRES 33 D 467 LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU
SEQRES 34 D 467 LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL
SEQRES 35 D 467 LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU
SEQRES 36 D 467 GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA
HET COA A 101 48
HET MAH A 201 11
HET NAP A 1 48
HET COA B 102 48
HET MAH B 202 11
HET NAP B 2 48
HET COA C 103 48
HET NAP C 3 48
HET MAH C 204 11
HET COA D 104 48
HET MAH D 203 11
HET NAP D 4 48
HETNAM COA COENZYME A
HETNAM MAH 3-HYDROXY-3-METHYL-GLUTARIC ACID
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 5 COA 4(C21 H36 N7 O16 P3 S)
FORMUL 6 MAH 4(C6 H10 O5)
FORMUL 7 NAP 4(C21 H28 N7 O17 P3)
FORMUL 17 HOH *471(H2 O)
HELIX 1 1 SER A 463 LYS A 474 1 12
HELIX 2 2 PRO A 477 TYR A 479 5 3
HELIX 3 3 LYS A 480 ILE A 485 1 6
HELIX 4 4 THR A 487 LYS A 501 1 15
HELIX 5 5 SER A 507 LEU A 512 5 6
HELIX 6 6 ASN A 518 MET A 523 1 6
HELIX 7 7 CYS A 561 GLY A 576 1 16
HELIX 8 8 ARG A 598 GLU A 610 1 13
HELIX 9 9 THR A 611 SER A 624 1 14
HELIX 10 10 GLY A 656 PHE A 675 1 20
HELIX 11 11 ALA A 694 GLY A 701 1 8
HELIX 12 12 PRO A 713 VAL A 720 1 8
HELIX 13 13 THR A 724 LEU A 737 1 14
HELIX 14 14 LEU A 737 ALA A 743 1 7
HELIX 15 15 HIS A 752 CYS A 764 1 13
HELIX 16 16 ASP A 767 ALA A 769 5 3
HELIX 17 17 GLN A 770 SER A 775 1 6
HELIX 18 18 GLY A 806 ASN A 810 5 5
HELIX 19 19 LEU A 811 GLY A 822 1 12
HELIX 20 20 GLY A 832 GLY A 860 1 29
HELIX 21 21 HIS A 861 ASN A 870 1 10
HELIX 22 22 SER B 463 ALA B 473 1 11
HELIX 23 23 PRO B 477 LEU B 481 5 5
HELIX 24 24 THR B 487 LYS B 501 1 15
HELIX 25 25 GLU B 505 LEU B 512 5 8
HELIX 26 26 ASN B 518 MET B 523 1 6
HELIX 27 27 CYS B 561 GLY B 576 1 16
HELIX 28 28 ARG B 598 GLU B 610 1 13
HELIX 29 29 THR B 611 SER B 624 1 14
HELIX 30 30 GLY B 656 PHE B 675 1 20
HELIX 31 31 ALA B 694 GLY B 701 1 8
HELIX 32 32 PRO B 713 VAL B 720 1 8
HELIX 33 33 THR B 724 LEU B 737 1 14
HELIX 34 34 LEU B 737 ALA B 743 1 7
HELIX 35 35 HIS B 752 CYS B 764 1 13
HELIX 36 36 ASP B 767 ALA B 769 5 3
HELIX 37 37 GLN B 770 SER B 775 1 6
HELIX 38 38 GLY B 806 ASN B 810 5 5
HELIX 39 39 LEU B 811 LEU B 821 1 11
HELIX 40 40 GLY B 832 GLY B 860 1 29
HELIX 41 41 ILE C 468 HIS C 475 1 8
HELIX 42 42 PRO C 477 TYR C 479 5 3
HELIX 43 43 LYS C 480 ILE C 485 1 6
HELIX 44 44 THR C 487 LEU C 503 1 17
HELIX 45 45 GLU C 505 LEU C 512 5 8
HELIX 46 46 ASN C 518 MET C 523 1 6
HELIX 47 47 CYS C 561 GLY C 576 1 16
HELIX 48 48 ARG C 598 GLU C 610 1 13
HELIX 49 49 THR C 611 SER C 624 1 14
HELIX 50 50 GLY C 656 PHE C 675 1 20
HELIX 51 51 ALA C 694 GLY C 701 1 8
HELIX 52 52 PRO C 713 VAL C 720 1 8
HELIX 53 53 THR C 724 LEU C 737 1 14
HELIX 54 54 LEU C 737 ALA C 743 1 7
HELIX 55 55 HIS C 752 CYS C 764 1 13
HELIX 56 56 ASP C 767 ALA C 769 5 3
HELIX 57 57 GLN C 770 SER C 775 1 6
HELIX 58 58 GLY C 806 ASN C 810 5 5
HELIX 59 59 LEU C 811 LEU C 821 1 11
HELIX 60 60 GLY C 832 GLY C 860 1 29
HELIX 61 61 HIS C 861 ASN C 870 1 10
HELIX 62 62 PRO D 477 TYR D 479 5 3
HELIX 63 63 LYS D 480 ILE D 485 1 6
HELIX 64 64 THR D 487 LYS D 501 1 15
HELIX 65 65 GLU D 505 LEU D 512 5 8
HELIX 66 66 ASN D 518 MET D 523 1 6
HELIX 67 67 CYS D 561 GLY D 576 1 16
HELIX 68 68 ARG D 598 GLU D 610 1 13
HELIX 69 69 THR D 611 SER D 624 1 14
HELIX 70 70 GLY D 656 PHE D 675 1 20
HELIX 71 71 ALA D 694 GLY D 701 1 8
HELIX 72 72 PRO D 713 VAL D 720 1 8
HELIX 73 73 THR D 724 LEU D 737 1 14
HELIX 74 74 LEU D 737 ALA D 743 1 7
HELIX 75 75 HIS D 752 CYS D 764 1 13
HELIX 76 76 ASP D 767 ALA D 769 5 3
HELIX 77 77 GLN D 770 SER D 775 1 6
HELIX 78 78 GLY D 806 ASN D 810 5 5
HELIX 79 79 LEU D 811 LEU D 821 1 11
HELIX 80 80 GLY D 832 GLY D 860 1 29
HELIX 81 81 HIS D 861 ASN D 870 1 10
SHEET 1 A 4 LYS A 549 ALA A 556 0
SHEET 2 A 4 VAL A 530 LEU A 546 -1 N GLY A 539 O MET A 555
SHEET 3 A 4 VAL B 530 LEU B 546 -1 N ILE B 531 O VAL A 538
SHEET 4 A 4 LYS B 549 ALA B 556 -1 O LYS B 549 N LEU B 546
SHEET 1 B 7 ALA A 629 ALA A 639 0
SHEET 2 B 7 ASN A 642 SER A 651 -1 N ASN A 642 O ALA A 639
SHEET 3 B 7 SER A 580 ARG A 590 -1 O MET A 588 N SER A 649
SHEET 4 B 7 GLY A 703 ILE A 712 -1 N GLY A 703 O GLY A 587
SHEET 5 B 7 ASP A 790 ILE A 800 -1 O LEU A 791 N ILE A 712
SHEET 6 B 7 CYS A 777 SER A 784 -1 O ILE A 778 N THR A 796
SHEET 7 B 7 GLY A 748 TYR A 749 1 O TYR A 749 N THR A 779
SHEET 1 C 4 ALA A 629 ALA A 639 0
SHEET 2 C 4 ASN A 642 SER A 651 -1 N ASN A 642 O ALA A 639
SHEET 3 C 4 VAL A 593 ARG A 595 -1 O VAL A 594 N LEU A 643
SHEET 4 C 4 GLN A 679 ALA A 682 -1 N GLN A 679 O ARG A 595
SHEET 1 D 7 ALA B 629 ALA B 639 0
SHEET 2 D 7 ASN B 642 SER B 651 -1 N ASN B 642 O ALA B 639
SHEET 3 D 7 SER B 580 ARG B 590 -1 O MET B 588 N SER B 649
SHEET 4 D 7 GLY B 703 ILE B 712 -1 N GLY B 703 O GLY B 587
SHEET 5 D 7 ASP B 790 ILE B 800 -1 O LEU B 791 N ILE B 712
SHEET 6 D 7 CYS B 777 SER B 784 -1 O ILE B 778 N THR B 796
SHEET 7 D 7 GLY B 748 TYR B 749 1 O TYR B 749 N THR B 779
SHEET 1 E 4 ALA B 629 ALA B 639 0
SHEET 2 E 4 ASN B 642 SER B 651 -1 N ASN B 642 O ALA B 639
SHEET 3 E 4 VAL B 593 ARG B 595 -1 O VAL B 594 N LEU B 643
SHEET 4 E 4 GLN B 679 ALA B 682 -1 N GLN B 679 O ARG B 595
SHEET 1 F 4 LYS C 549 ALA C 556 0
SHEET 2 F 4 VAL C 530 LEU C 546 -1 N GLY C 539 O MET C 555
SHEET 3 F 4 VAL D 530 LEU D 546 -1 N ILE D 531 O VAL C 538
SHEET 4 F 4 LYS D 549 ALA D 556 -1 O LYS D 549 N LEU D 546
SHEET 1 G 7 ALA C 629 ALA C 639 0
SHEET 2 G 7 ASN C 642 SER C 651 -1 N ASN C 642 O ALA C 639
SHEET 3 G 7 SER C 580 ARG C 590 -1 O MET C 588 N SER C 649
SHEET 4 G 7 GLY C 703 ILE C 712 -1 O GLY C 703 N GLY C 587
SHEET 5 G 7 ASP C 790 ILE C 800 -1 O LEU C 791 N ILE C 712
SHEET 6 G 7 CYS C 777 SER C 784 -1 O ILE C 778 N THR C 796
SHEET 7 G 7 GLY C 748 TYR C 749 1 O TYR C 749 N THR C 779
SHEET 1 H 4 ALA C 629 ALA C 639 0
SHEET 2 H 4 ASN C 642 SER C 651 -1 N ASN C 642 O ALA C 639
SHEET 3 H 4 VAL C 593 ARG C 595 -1 O VAL C 594 N LEU C 643
SHEET 4 H 4 GLN C 679 ALA C 682 -1 N GLN C 679 O ARG C 595
SHEET 1 I 7 ALA D 629 ALA D 639 0
SHEET 2 I 7 ASN D 642 SER D 651 -1 O ASN D 642 N ALA D 639
SHEET 3 I 7 SER D 580 ARG D 590 -1 O MET D 588 N SER D 649
SHEET 4 I 7 GLY D 703 ILE D 712 -1 O GLY D 703 N GLY D 587
SHEET 5 I 7 ASP D 790 ILE D 800 -1 O LEU D 791 N ILE D 712
SHEET 6 I 7 CYS D 777 SER D 784 -1 N ILE D 778 O THR D 796
SHEET 7 I 7 GLY D 748 TYR D 749 1 O TYR D 749 N THR D 779
SHEET 1 J 4 ALA D 629 ALA D 639 0
SHEET 2 J 4 ASN D 642 SER D 651 -1 O ASN D 642 N ALA D 639
SHEET 3 J 4 VAL D 593 ARG D 595 -1 O VAL D 594 N LEU D 643
SHEET 4 J 4 GLN D 679 ALA D 682 -1 N GLN D 679 O ARG D 595
CISPEP 1 GLY A 542 PRO A 543 0 1.32
CISPEP 2 CYS A 688 THR A 689 0 -0.74
CISPEP 3 GLY B 542 PRO B 543 0 0.53
CISPEP 4 CYS B 688 THR B 689 0 -1.31
CISPEP 5 GLY C 542 PRO C 543 0 0.36
CISPEP 6 CYS C 688 THR C 689 0 -0.25
CISPEP 7 GLY D 542 PRO D 543 0 0.64
CISPEP 8 CYS D 688 THR D 689 0 -1.25
SITE 1 AC1 23 MAH A 201 GLU A 559 LEU A 562 ALA A 564
SITE 2 AC1 23 SER A 565 ASN A 567 ARG A 568 ARG A 571
SITE 3 AC1 23 VAL A 720 LYS A 722 HIS A 752 ASN A 755
SITE 4 AC1 23 SER A 852 LEU A 853 ALA A 856 LEU A 862
SITE 5 AC1 23 SER A 865 HIS A 866 HOH A2178 HOH A2284
SITE 6 AC1 23 HOH A2290 TYR B 479 GLU B 528
SITE 1 AC2 19 TYR A 479 GLU A 528 MAH B 202 GLU B 559
SITE 2 AC2 19 LEU B 562 ALA B 564 SER B 565 ASN B 567
SITE 3 AC2 19 ARG B 568 ARG B 571 VAL B 720 LYS B 722
SITE 4 AC2 19 HIS B 752 SER B 852 LEU B 853 SER B 865
SITE 5 AC2 19 HIS B 866 HOH B2211 HOH B2279
SITE 1 AC3 19 LEU C 562 ALA C 564 SER C 565 ASN C 567
SITE 2 AC3 19 ARG C 568 VAL C 720 LYS C 722 HIS C 752
SITE 3 AC3 19 SER C 852 LEU C 853 LEU C 862 SER C 865
SITE 4 AC3 19 HIS C 866 HOH C2247 HOH C2248 HOH C2416
SITE 5 AC3 19 MAH D 203 TYR D 479 GLU D 528
SITE 1 AC4 21 MAH C 204 PRO C 477 TYR C 479 GLU D 559
SITE 2 AC4 21 LEU D 562 ALA D 564 SER D 565 ASN D 567
SITE 3 AC4 21 ARG D 568 ARG D 571 VAL D 720 LYS D 722
SITE 4 AC4 21 HIS D 752 ASN D 755 SER D 852 LEU D 853
SITE 5 AC4 21 LEU D 862 SER D 865 HIS D 866 HOH D2265
SITE 6 AC4 21 HOH D2384
SITE 1 AC5 12 COA A 101 GLU A 559 LYS A 735 ALA A 751
SITE 2 AC5 12 ASN A 755 HOH A2062 NAP B 2 ARG B 590
SITE 3 AC5 12 SER B 684 ASP B 690 LYS B 691 LYS B 692
SITE 1 AC6 25 ARG A 590 SER A 626 ARG A 627 PHE A 628
SITE 2 AC6 25 SER A 651 GLY A 652 ASP A 653 ALA A 654
SITE 3 AC6 25 MET A 655 GLY A 656 MET A 657 ASN A 658
SITE 4 AC6 25 MET A 659 SER A 661 ASP A 690 LYS A 691
SITE 5 AC6 25 ASP A 767 GLY A 807 ALA A 826 HOH A2168
SITE 6 AC6 25 HOH A2272 MAH B 202 GLU B 559 HIS B 866
SITE 7 AC6 25 HOH B2155
SITE 1 AC7 13 NAP A 1 ARG A 590 SER A 684 ASP A 690
SITE 2 AC7 13 LYS A 691 LYS A 692 COA B 102 GLU B 559
SITE 3 AC7 13 LYS B 735 ALA B 751 ASN B 755 HIS B 866
SITE 4 AC7 13 HOH B2081
SITE 1 AC8 29 MAH A 201 GLU A 559 HIS A 866 ASN A 870
SITE 2 AC8 29 HOH A2288 ARG B 590 SER B 626 ARG B 627
SITE 3 AC8 29 PHE B 628 SER B 651 ASP B 653 ALA B 654
SITE 4 AC8 29 MET B 655 GLY B 656 MET B 657 ASN B 658
SITE 5 AC8 29 MET B 659 SER B 661 ASP B 690 LYS B 691
SITE 6 AC8 29 ASP B 767 VAL B 805 GLY B 806 GLY B 807
SITE 7 AC8 29 ALA B 826 HOH B2171 HOH B2266 HOH B2267
SITE 8 AC8 29 HOH B2268
SITE 1 AC9 12 COA C 103 GLU C 559 LYS C 735 ALA C 751
SITE 2 AC9 12 ASN C 755 NAP D 4 ARG D 590 SER D 684
SITE 3 AC9 12 ASP D 690 LYS D 691 LYS D 692 HOH D2001
SITE 1 BC1 32 MAH C 204 ARG C 590 SER C 626 ARG C 627
SITE 2 BC1 32 PHE C 628 SER C 651 GLY C 652 ASP C 653
SITE 3 BC1 32 ALA C 654 MET C 655 GLY C 656 MET C 657
SITE 4 BC1 32 ASN C 658 MET C 659 SER C 661 ASP C 690
SITE 5 BC1 32 LYS C 691 ASP C 767 GLY C 806 GLY C 807
SITE 6 BC1 32 ALA C 826 HOH C2111 HOH C2147 HOH C2166
SITE 7 BC1 32 HOH C2244 HOH C2273 HOH C2274 HOH C2452
SITE 8 BC1 32 GLU D 559 HIS D 866 ASN D 870 ARG D 871
SITE 1 BC2 12 NAP C 3 ARG C 590 SER C 684 ASP C 690
SITE 2 BC2 12 LYS C 691 LYS C 692 HOH C2005 COA D 104
SITE 3 BC2 12 GLU D 559 LYS D 735 ALA D 751 ASN D 755
SITE 1 BC3 32 GLU C 559 HIS C 866 ASN C 870 ARG C 871
SITE 2 BC3 32 HOH C2095 MAH D 203 ARG D 590 SER D 626
SITE 3 BC3 32 ARG D 627 PHE D 628 SER D 651 GLY D 652
SITE 4 BC3 32 ASP D 653 ALA D 654 MET D 655 GLY D 656
SITE 5 BC3 32 MET D 657 ASN D 658 MET D 659 SER D 661
SITE 6 BC3 32 ASP D 690 LYS D 691 ASP D 767 VAL D 805
SITE 7 BC3 32 GLY D 806 GLY D 807 ALA D 826 HOH D2264
SITE 8 BC3 32 HOH D2269 HOH D2270 HOH D2453 HOH D2471
CRYST1 73.918 172.630 73.991 90.00 117.50 90.00 P 1 21 1 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 0.013529 0.000000 0.007043 0.00000
SCALE2 0.000000 0.005793 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015237 0.00000
(ATOM LINES ARE NOT SHOWN.)
END