HEADER OXIDOREDUCTASE 30-AUG-05 2C0C
TITLE STRUCTURE OF THE MGC45594 GENE PRODUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC BINDING ALCOHOL DEHYDROGENASE, DOMAIN CONTAINING 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DOMAIN, RESIDUES 33-371;
COMPND 5 SYNONYM: MGC45594 HYPOTHETICAL PROTEIN;
COMPND 6 ENGINEERED: 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS OXIDOREDUCTASE, QUINONE OXIDOREDUCTASE, MEDIUM-CHAIN
KEYWDS 2 DEHYDROGENASE/REDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BUNKOCZI,N.SHAFQAT,K.GUO,C.SMEE,C.ARROWSMITH,A.EDWARDS,J.WEIGELT,
AUTHOR 2 M.SUNDSTROM,O.GILEADI,F.VON DELFT,U.OPPERMANN
REVDAT 6 13-DEC-23 2C0C 1 REMARK
REVDAT 5 28-FEB-18 2C0C 1 SOURCE
REVDAT 4 24-JAN-18 2C0C 1 AUTHOR JRNL
REVDAT 3 24-FEB-09 2C0C 1 VERSN
REVDAT 2 06-FEB-07 2C0C 1 DBREF
REVDAT 1 12-SEP-05 2C0C 0
JRNL AUTH G.BUNKOCZI,N.SHAFQAT,K.GUO,C.SMEE,C.ARROWSMITH,A.EDWARDS,
JRNL AUTH 2 J.WEIGELT,M.SUNDSTROM,O.GILEADI,F.VON DELFT,U.OPPERMANN
JRNL TITL THE STRUCTURE OF MGC45594 GENE PRODUCT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 110704
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5848
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8020
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 434
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5163
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 674
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.70000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : -0.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.179
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5470 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5052 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7466 ; 1.764 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11777 ; 0.903 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 722 ; 6.264 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 190 ;38.982 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 890 ;12.835 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.935 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 866 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6062 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1040 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1039 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5046 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2727 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3328 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 364 ; 0.192 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.192 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 206 ; 0.267 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 148 ; 0.165 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3658 ; 3.605 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5640 ; 4.491 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2155 ; 5.618 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1813 ; 7.070 ;11.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2C0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1290025476.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0080
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116573
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 46.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.890
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.18
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.270
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1QOR
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): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE PH=9.1 24% PEG 10K, PH
REMARK 280 9.10
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 41.06850
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 VAL B 11
REMARK 465 ASP B 12
REMARK 465 LEU B 13
REMARK 465 GLY B 14
REMARK 465 THR B 15
REMARK 465 GLU B 16
REMARK 465 ASN B 17
REMARK 465 LEU B 18
REMARK 465 TYR B 19
REMARK 465 PHE B 20
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 LYS A 82 CD CE NZ
REMARK 470 LYS A 188 CE NZ
REMARK 470 LYS A 205 CD CE NZ
REMARK 470 LYS A 351 CE NZ
REMARK 470 ARG B 44 CZ NH1 NH2
REMARK 470 ASP B 45 CG OD1 OD2
REMARK 470 LYS B 166 NZ
REMARK 470 LYS B 188 NZ
REMARK 470 LYS B 205 CE NZ
REMARK 470 LYS B 225 CD CE NZ
REMARK 470 GLN B 226 CG CD OE1 NE2
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 HOH B 2127 O HOH B 2243 2.14
REMARK 500 O HOH A 2084 O HOH A 2087 2.16
REMARK 500 O HOH B 2035 O HOH B 2044 2.17
REMARK 500 O HOH B 2021 O HOH B 2022 2.18
REMARK 500 O HOH B 2005 O HOH B 2006 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 195 CB CYS B 195 SG -0.132
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 ARG B 256 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET B 307 CG - SD - CE ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG B 342 NE - CZ - NH1 ANGL. DEV. = 3.0 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 ASP A 45 59.97 -140.55
REMARK 500 ASP A 78 84.73 -160.01
REMARK 500 LYS A 188 30.75 73.40
REMARK 500 ARG A 211 82.08 -151.23
REMARK 500 PHE A 262 70.79 -154.80
REMARK 500 ASP B 78 89.96 -154.61
REMARK 500 PRO B 79 1.30 -62.80
REMARK 500 SER B 103 129.41 -38.02
REMARK 500 PHE B 262 65.35 -157.30
REMARK 500 CYS B 321 79.69 -113.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2013 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH B2085 DISTANCE = 6.74 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B1363
DBREF 2C0C A 1 23 PDB 2C0C 2C0C 1 23
DBREF 2C0C A 24 362 UNP Q8N4Q0 Q8N4Q0_HUMAN 33 371
DBREF 2C0C B 1 23 PDB 2C0C 2C0C 1 23
DBREF 2C0C B 24 362 UNP Q8N4Q0 Q8N4Q0_HUMAN 33 371
SEQRES 1 A 362 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 362 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET GLN LYS
SEQRES 3 A 362 LEU VAL VAL THR ARG LEU SER PRO ASN PHE ARG GLU ALA
SEQRES 4 A 362 VAL THR LEU SER ARG ASP CYS PRO VAL PRO LEU PRO GLY
SEQRES 5 A 362 ASP GLY ASP LEU LEU VAL ARG ASN ARG PHE VAL GLY VAL
SEQRES 6 A 362 ASN ALA SER ASP ILE ASN TYR SER ALA GLY ARG TYR ASP
SEQRES 7 A 362 PRO SER VAL LYS PRO PRO PHE ASP ILE GLY PHE GLU GLY
SEQRES 8 A 362 ILE GLY GLU VAL VAL ALA LEU GLY LEU SER ALA SER ALA
SEQRES 9 A 362 ARG TYR THR VAL GLY GLN ALA VAL ALA TYR MET ALA PRO
SEQRES 10 A 362 GLY SER PHE ALA GLU TYR THR VAL VAL PRO ALA SER ILE
SEQRES 11 A 362 ALA THR PRO VAL PRO SER VAL LYS PRO GLU TYR LEU THR
SEQRES 12 A 362 LEU LEU VAL SER GLY THR THR ALA TYR ILE SER LEU LYS
SEQRES 13 A 362 GLU LEU GLY GLY LEU SER GLU GLY LYS LYS VAL LEU VAL
SEQRES 14 A 362 THR ALA ALA ALA GLY GLY THR GLY GLN PHE ALA MET GLN
SEQRES 15 A 362 LEU SER LYS LYS ALA LYS CYS HIS VAL ILE GLY THR CYS
SEQRES 16 A 362 SER SER ASP GLU LYS SER ALA PHE LEU LYS SER LEU GLY
SEQRES 17 A 362 CYS ASP ARG PRO ILE ASN TYR LYS THR GLU PRO VAL GLY
SEQRES 18 A 362 THR VAL LEU LYS GLN GLU TYR PRO GLU GLY VAL ASP VAL
SEQRES 19 A 362 VAL TYR GLU SER VAL GLY GLY ALA MET PHE ASP LEU ALA
SEQRES 20 A 362 VAL ASP ALA LEU ALA THR LYS GLY ARG LEU ILE VAL ILE
SEQRES 21 A 362 GLY PHE ILE SER GLY TYR GLN THR PRO THR GLY LEU SER
SEQRES 22 A 362 PRO VAL LYS ALA GLY THR LEU PRO ALA LYS LEU LEU LYS
SEQRES 23 A 362 LYS SER ALA SER VAL GLN GLY PHE PHE LEU ASN HIS TYR
SEQRES 24 A 362 LEU SER LYS TYR GLN ALA ALA MET SER HIS LEU LEU GLU
SEQRES 25 A 362 MET CYS VAL SER GLY ASP LEU VAL CYS GLU VAL ASP LEU
SEQRES 26 A 362 GLY ASP LEU SER PRO GLU GLY ARG PHE THR GLY LEU GLU
SEQRES 27 A 362 SER ILE PHE ARG ALA VAL ASN TYR MET TYR MET GLY LYS
SEQRES 28 A 362 ASN THR GLY LYS ILE VAL VAL GLU LEU PRO HIS
SEQRES 1 B 362 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 362 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET GLN LYS
SEQRES 3 B 362 LEU VAL VAL THR ARG LEU SER PRO ASN PHE ARG GLU ALA
SEQRES 4 B 362 VAL THR LEU SER ARG ASP CYS PRO VAL PRO LEU PRO GLY
SEQRES 5 B 362 ASP GLY ASP LEU LEU VAL ARG ASN ARG PHE VAL GLY VAL
SEQRES 6 B 362 ASN ALA SER ASP ILE ASN TYR SER ALA GLY ARG TYR ASP
SEQRES 7 B 362 PRO SER VAL LYS PRO PRO PHE ASP ILE GLY PHE GLU GLY
SEQRES 8 B 362 ILE GLY GLU VAL VAL ALA LEU GLY LEU SER ALA SER ALA
SEQRES 9 B 362 ARG TYR THR VAL GLY GLN ALA VAL ALA TYR MET ALA PRO
SEQRES 10 B 362 GLY SER PHE ALA GLU TYR THR VAL VAL PRO ALA SER ILE
SEQRES 11 B 362 ALA THR PRO VAL PRO SER VAL LYS PRO GLU TYR LEU THR
SEQRES 12 B 362 LEU LEU VAL SER GLY THR THR ALA TYR ILE SER LEU LYS
SEQRES 13 B 362 GLU LEU GLY GLY LEU SER GLU GLY LYS LYS VAL LEU VAL
SEQRES 14 B 362 THR ALA ALA ALA GLY GLY THR GLY GLN PHE ALA MET GLN
SEQRES 15 B 362 LEU SER LYS LYS ALA LYS CYS HIS VAL ILE GLY THR CYS
SEQRES 16 B 362 SER SER ASP GLU LYS SER ALA PHE LEU LYS SER LEU GLY
SEQRES 17 B 362 CYS ASP ARG PRO ILE ASN TYR LYS THR GLU PRO VAL GLY
SEQRES 18 B 362 THR VAL LEU LYS GLN GLU TYR PRO GLU GLY VAL ASP VAL
SEQRES 19 B 362 VAL TYR GLU SER VAL GLY GLY ALA MET PHE ASP LEU ALA
SEQRES 20 B 362 VAL ASP ALA LEU ALA THR LYS GLY ARG LEU ILE VAL ILE
SEQRES 21 B 362 GLY PHE ILE SER GLY TYR GLN THR PRO THR GLY LEU SER
SEQRES 22 B 362 PRO VAL LYS ALA GLY THR LEU PRO ALA LYS LEU LEU LYS
SEQRES 23 B 362 LYS SER ALA SER VAL GLN GLY PHE PHE LEU ASN HIS TYR
SEQRES 24 B 362 LEU SER LYS TYR GLN ALA ALA MET SER HIS LEU LEU GLU
SEQRES 25 B 362 MET CYS VAL SER GLY ASP LEU VAL CYS GLU VAL ASP LEU
SEQRES 26 B 362 GLY ASP LEU SER PRO GLU GLY ARG PHE THR GLY LEU GLU
SEQRES 27 B 362 SER ILE PHE ARG ALA VAL ASN TYR MET TYR MET GLY LYS
SEQRES 28 B 362 ASN THR GLY LYS ILE VAL VAL GLU LEU PRO HIS
HET NAP A1363 48
HET NAP B1363 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 5 HOH *674(H2 O)
HELIX 1 1 GLY A 14 GLN A 21 1 8
HELIX 2 2 ASN A 35 ALA A 39 1 5
HELIX 3 3 SER A 68 ALA A 74 1 7
HELIX 4 4 SER A 101 ARG A 105 5 5
HELIX 5 5 SER A 129 ALA A 131 5 3
HELIX 6 6 LYS A 138 THR A 143 1 6
HELIX 7 7 VAL A 146 GLY A 159 1 14
HELIX 8 8 THR A 176 ALA A 187 1 12
HELIX 9 9 SER A 197 LEU A 207 1 11
HELIX 10 10 PRO A 219 TYR A 228 1 10
HELIX 11 11 GLY A 241 ALA A 250 1 10
HELIX 12 12 PHE A 262 TYR A 266 5 5
HELIX 13 13 THR A 279 SER A 288 1 10
HELIX 14 14 PHE A 295 TYR A 299 5 5
HELIX 15 15 TYR A 299 SER A 301 5 3
HELIX 16 16 LYS A 302 SER A 316 1 15
HELIX 17 17 GLU A 338 MET A 349 1 12
HELIX 18 18 ASN B 35 ALA B 39 1 5
HELIX 19 19 SER B 68 ALA B 74 1 7
HELIX 20 20 SER B 129 ALA B 131 5 3
HELIX 21 21 LYS B 138 THR B 143 1 6
HELIX 22 22 VAL B 146 GLY B 159 1 14
HELIX 23 23 THR B 176 ALA B 187 1 12
HELIX 24 24 SER B 197 LEU B 207 1 11
HELIX 25 25 PRO B 219 TYR B 228 1 10
HELIX 26 26 GLY B 240 ALA B 250 1 11
HELIX 27 27 PHE B 262 TYR B 266 5 5
HELIX 28 28 THR B 279 SER B 288 1 10
HELIX 29 29 PHE B 295 TYR B 299 5 5
HELIX 30 30 TYR B 299 SER B 301 5 3
HELIX 31 31 LYS B 302 SER B 316 1 15
HELIX 32 32 GLU B 338 MET B 349 1 12
SHEET 1 AA 3 VAL A 40 PRO A 47 0
SHEET 2 AA 3 MET A 23 VAL A 29 -1 O MET A 24 N CYS A 46
SHEET 3 AA 3 PHE A 85 ASP A 86 -1 O PHE A 85 N VAL A 29
SHEET 1 AB 5 TYR A 123 PRO A 127 0
SHEET 2 AB 5 ASP A 55 GLY A 64 -1 O LEU A 56 N VAL A 126
SHEET 3 AB 5 GLU A 90 LEU A 98 -1 O GLU A 90 N GLY A 64
SHEET 4 AB 5 ALA A 111 MET A 115 -1 O VAL A 112 N GLY A 93
SHEET 5 AB 5 THR A 132 PRO A 133 -1 O THR A 132 N ALA A 113
SHEET 1 AC 4 TYR A 123 PRO A 127 0
SHEET 2 AC 4 ASP A 55 GLY A 64 -1 O LEU A 56 N VAL A 126
SHEET 3 AC 4 LYS A 355 GLU A 359 -1 O VAL A 358 N VAL A 63
SHEET 4 AC 4 VAL A 323 ASP A 324 1 O ASP A 324 N VAL A 357
SHEET 1 AD12 ARG A 211 ASN A 214 0
SHEET 2 AD12 HIS A 190 CYS A 195 1 O GLY A 193 N ILE A 213
SHEET 3 AD12 LYS A 166 VAL A 169 1 O VAL A 167 N ILE A 192
SHEET 4 AD12 VAL A 232 GLU A 237 1 N ASP A 233 O LYS A 166
SHEET 5 AD12 LEU A 251 VAL A 259 1 N ALA A 252 O VAL A 232
SHEET 6 AD12 SER A 290 GLY A 293 1 O SER A 290 N LEU A 257
SHEET 7 AD12 SER B 290 GLY B 293 -1 O VAL B 291 N VAL A 291
SHEET 8 AD12 LEU B 251 VAL B 259 1 O GLY B 255 N SER B 290
SHEET 9 AD12 VAL B 232 GLU B 237 1 O VAL B 232 N ALA B 252
SHEET 10 AD12 LYS B 166 VAL B 169 1 O LYS B 166 N VAL B 234
SHEET 11 AD12 HIS B 190 CYS B 195 1 O HIS B 190 N VAL B 167
SHEET 12 AD12 ARG B 211 ASN B 214 1 O ARG B 211 N GLY B 193
SHEET 1 BA 3 VAL B 40 PRO B 47 0
SHEET 2 BA 3 MET B 23 VAL B 29 -1 O MET B 24 N CYS B 46
SHEET 3 BA 3 PHE B 85 ASP B 86 -1 O PHE B 85 N VAL B 29
SHEET 1 BB 5 TYR B 123 PRO B 127 0
SHEET 2 BB 5 ASP B 55 GLY B 64 -1 O LEU B 56 N VAL B 126
SHEET 3 BB 5 GLU B 90 LEU B 98 -1 O GLU B 90 N GLY B 64
SHEET 4 BB 5 ALA B 111 MET B 115 -1 O VAL B 112 N GLY B 93
SHEET 5 BB 5 THR B 132 PRO B 133 -1 O THR B 132 N ALA B 113
SHEET 1 BC 4 TYR B 123 PRO B 127 0
SHEET 2 BC 4 ASP B 55 GLY B 64 -1 O LEU B 56 N VAL B 126
SHEET 3 BC 4 LYS B 355 GLU B 359 -1 O VAL B 358 N VAL B 63
SHEET 4 BC 4 VAL B 323 ASP B 324 1 O ASP B 324 N VAL B 357
CISPEP 1 PRO A 83 PRO A 84 0 -0.30
CISPEP 2 PRO B 83 PRO B 84 0 4.48
SITE 1 AC1 36 ASN A 66 ALA A 67 THR A 150 ALA A 171
SITE 2 AC1 36 GLY A 174 GLY A 175 THR A 176 CYS A 195
SITE 3 AC1 36 SER A 196 LYS A 200 TYR A 215 SER A 238
SITE 4 AC1 36 ILE A 260 GLY A 261 PHE A 262 ILE A 263
SITE 5 AC1 36 SER A 264 TYR A 266 PHE A 294 LEU A 296
SITE 6 AC1 36 MET A 347 ASN A 352 HOH A2073 HOH A2075
SITE 7 AC1 36 HOH A2174 HOH A2188 HOH A2195 HOH A2254
SITE 8 AC1 36 HOH A2258 HOH A2348 HOH A2349 HOH A2350
SITE 9 AC1 36 HOH A2351 HOH A2352 HOH A2353 HOH A2354
SITE 1 AC2 38 ASN B 66 ALA B 67 THR B 150 ALA B 171
SITE 2 AC2 38 GLY B 174 GLY B 175 THR B 176 CYS B 195
SITE 3 AC2 38 SER B 196 LYS B 200 TYR B 215 SER B 238
SITE 4 AC2 38 VAL B 239 ILE B 260 GLY B 261 PHE B 262
SITE 5 AC2 38 ILE B 263 SER B 264 TYR B 266 PHE B 294
SITE 6 AC2 38 LEU B 296 MET B 347 TYR B 348 ASN B 352
SITE 7 AC2 38 HOH B2074 HOH B2075 HOH B2155 HOH B2226
SITE 8 AC2 38 HOH B2309 HOH B2312 HOH B2313 HOH B2314
SITE 9 AC2 38 HOH B2315 HOH B2316 HOH B2317 HOH B2318
SITE 10 AC2 38 HOH B2319 HOH B2320
CRYST1 61.164 82.137 73.905 90.00 112.54 90.00 P 1 21 1 4
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 0.016349 0.000000 0.006786 0.00000
SCALE2 0.000000 0.012175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014650 0.00000
MTRIX1 1 -0.967500 0.202630 0.151250 73.81544 1
MTRIX2 1 0.228520 0.444700 0.866040 19.17183 1
MTRIX3 1 0.108230 0.872460 -0.476550 -49.96343 1
(ATOM LINES ARE NOT SHOWN.)
END
