HEADER OXIDOREDUCTASE 11-NOV-13 4NJO
TITLE CRYSTAL STRUCTURE OF COFACTOR(NAD+) BOUND 3-PHOSPHOGLYCERATE
TITLE 2 DEHYDROGENASE IN ENTAMOEBA HISTOLYTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: D-PHOSPHOGLYCERATE DEHYDROGENASE;
COMPND 5 EC: 1.1.1.95;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA;
SOURCE 3 ORGANISM_TAXID: 5759;
SOURCE 4 STRAIN: HM1:IMSS;
SOURCE 5 GENE: EHPGDH, EHI_060860;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS ROSSMANN FOLD, DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.K.SINGH,S.GOURINATH
REVDAT 4 20-MAR-24 4NJO 1 REMARK SEQADV
REVDAT 3 22-NOV-17 4NJO 1 REMARK
REVDAT 2 17-JUN-15 4NJO 1 JRNL
REVDAT 1 08-OCT-14 4NJO 0
JRNL AUTH R.K.SINGH,I.RAJ,R.PUJARI,S.GOURINATH
JRNL TITL CRYSTAL STRUCTURES AND KINETICS OF TYPE III
JRNL TITL 2 3-PHOSPHOGLYCERATE DEHYDROGENASE REVEAL CATALYSIS BY LYSINE.
JRNL REF FEBS J. V. 281 5498 2014
JRNL REFN ISSN 1742-464X
JRNL PMID 25294608
JRNL DOI 10.1111/FEBS.13091
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 23444
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1257
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) : 2.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1604
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4724
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.64000
REMARK 3 B22 (A**2) : 4.36000
REMARK 3 B33 (A**2) : -1.64000
REMARK 3 B12 (A**2) : -2.25000
REMARK 3 B13 (A**2) : 2.03000
REMARK 3 B23 (A**2) : -1.84000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.532
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.259
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.187
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.397
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4846 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6483 ; 0.918 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 602 ; 5.010 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 204 ;34.878 ;25.196
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 978 ;14.784 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;12.310 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 730 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3477 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1031 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2415 ; 0.934 ; 4.414
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2415 ; 1.322 ; 4.457
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3014 ; 1.621 ; 6.614
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2431 ; 1.056 ; 4.608
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4NJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : CU-NI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 52.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
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) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 100MM TRIS PH 7.0-8.0
REMARK 280 300MM SODIUM FORMATE, 5% GLYCEROL , VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 289K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 GLU A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 GLU B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 HIS B 304
REMARK 465 HIS B 305
REMARK 465 HIS B 306
REMARK 465 HIS B 307
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 NH2 ARG A 119 O GLY B 105 2.17
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 LYS A 39 52.20 -69.76
REMARK 500 GLU A 40 -25.60 -140.55
REMARK 500 ARG A 55 -125.80 -99.24
REMARK 500 ASP A 132 -3.37 75.91
REMARK 500 CYS A 140 70.03 -113.19
REMARK 500 ASP A 162 100.74 -169.60
REMARK 500 ALA A 216 -91.89 -100.61
REMARK 500 PHE A 253 45.21 -99.14
REMARK 500 ARG B 55 -122.70 -101.39
REMARK 500 ASP B 162 107.68 -163.23
REMARK 500 PRO B 207 -179.80 -66.67
REMARK 500 ALA B 216 -89.28 -91.89
REMARK 500 ARG B 256 12.27 -147.19
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 NAD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NJM RELATED DB: PDB
DBREF 4NJO A 1 299 UNP Q76KF5 Q76KF5_ENTHI 1 299
DBREF 4NJO B 1 299 UNP Q76KF5 Q76KF5_ENTHI 1 299
SEQADV 4NJO ALA A -1 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO SER A 0 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO LEU A 300 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO GLU A 301 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS A 302 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS A 303 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS A 304 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS A 305 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS A 306 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS A 307 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO ALA B -1 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO SER B 0 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO LEU B 300 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO GLU B 301 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS B 302 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS B 303 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS B 304 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS B 305 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS B 306 UNP Q76KF5 EXPRESSION TAG
SEQADV 4NJO HIS B 307 UNP Q76KF5 EXPRESSION TAG
SEQRES 1 A 309 ALA SER MET LYS ILE VAL VAL ILE THR GLU LYS PRO PHE
SEQRES 2 A 309 ALA GLU ASN ALA VAL LYS GLY ILE ARG GLU ILE LEU GLU
SEQRES 3 A 309 LYS ALA GLY HIS GLU VAL VAL MET ILE GLU LYS TYR LYS
SEQRES 4 A 309 LYS LYS GLU ASP VAL ILE GLU ARG ILE LYS ASP ALA ASP
SEQRES 5 A 309 GLY VAL ILE VAL ARG SER ASP LYS ILE ASP GLU GLU ILE
SEQRES 6 A 309 ILE LYS ALA GLY GLU LYS VAL LYS ILE ILE VAL ARG ALA
SEQRES 7 A 309 GLY ALA GLY TYR ASP ASN ILE ASP ILE GLU ALA CYS ASN
SEQRES 8 A 309 GLN GLY LYS ILE VAL VAL MET ASN THR PRO GLY GLN ASN
SEQRES 9 A 309 ARG ASN GLY VAL ALA GLU LEU CYS ILE GLY MET MET ILE
SEQRES 10 A 309 PHE GLY PHE ARG LYS GLY PHE LYS GLU GLY LYS GLY ARG
SEQRES 11 A 309 GLU LEU LYS ASP LYS THR LEU GLY ILE CYS GLY CYS GLY
SEQRES 12 A 309 TYR VAL GLY LYS ARG VAL LYS GLU ILE ALA GLU GLY ILE
SEQRES 13 A 309 GLY MET LYS ILE LYS VAL TYR ASP PRO PHE ILE THR THR
SEQRES 14 A 309 GLU ASN GLN VAL LYS LYS ILE GLU GLU LEU PHE GLU GLU
SEQRES 15 A 309 CYS GLN VAL ILE SER LEU HIS LEU PRO LEU THR LYS GLU
SEQRES 16 A 309 THR LYS GLY LYS ILE GLY TYR GLU LEU ILE LYS LYS LEU
SEQRES 17 A 309 PRO TYR GLY GLY MET ILE CYS ASN THR ALA ARG LYS GLU
SEQRES 18 A 309 ILE ILE ASP GLU GLU GLY LEU ILE ARG ILE MET ARG GLU
SEQRES 19 A 309 ARG GLU ASP LEU ILE TYR ILE THR ASP VAL ALA PRO THR
SEQRES 20 A 309 SER LYS VAL PHE ASN ASN GLU PHE LYS GLY ARG PHE PHE
SEQRES 21 A 309 ALA THR PRO ILE LYS ILE GLY ALA GLU THR GLU GLU SER
SEQRES 22 A 309 ASN ILE ASN ALA GLY MET ALA ALA ALA SER GLN ILE CYS
SEQRES 23 A 309 ASP PHE PHE THR ASN GLY THR VAL LYS PHE GLN VAL ASN
SEQRES 24 A 309 LYS PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 309 ALA SER MET LYS ILE VAL VAL ILE THR GLU LYS PRO PHE
SEQRES 2 B 309 ALA GLU ASN ALA VAL LYS GLY ILE ARG GLU ILE LEU GLU
SEQRES 3 B 309 LYS ALA GLY HIS GLU VAL VAL MET ILE GLU LYS TYR LYS
SEQRES 4 B 309 LYS LYS GLU ASP VAL ILE GLU ARG ILE LYS ASP ALA ASP
SEQRES 5 B 309 GLY VAL ILE VAL ARG SER ASP LYS ILE ASP GLU GLU ILE
SEQRES 6 B 309 ILE LYS ALA GLY GLU LYS VAL LYS ILE ILE VAL ARG ALA
SEQRES 7 B 309 GLY ALA GLY TYR ASP ASN ILE ASP ILE GLU ALA CYS ASN
SEQRES 8 B 309 GLN GLY LYS ILE VAL VAL MET ASN THR PRO GLY GLN ASN
SEQRES 9 B 309 ARG ASN GLY VAL ALA GLU LEU CYS ILE GLY MET MET ILE
SEQRES 10 B 309 PHE GLY PHE ARG LYS GLY PHE LYS GLU GLY LYS GLY ARG
SEQRES 11 B 309 GLU LEU LYS ASP LYS THR LEU GLY ILE CYS GLY CYS GLY
SEQRES 12 B 309 TYR VAL GLY LYS ARG VAL LYS GLU ILE ALA GLU GLY ILE
SEQRES 13 B 309 GLY MET LYS ILE LYS VAL TYR ASP PRO PHE ILE THR THR
SEQRES 14 B 309 GLU ASN GLN VAL LYS LYS ILE GLU GLU LEU PHE GLU GLU
SEQRES 15 B 309 CYS GLN VAL ILE SER LEU HIS LEU PRO LEU THR LYS GLU
SEQRES 16 B 309 THR LYS GLY LYS ILE GLY TYR GLU LEU ILE LYS LYS LEU
SEQRES 17 B 309 PRO TYR GLY GLY MET ILE CYS ASN THR ALA ARG LYS GLU
SEQRES 18 B 309 ILE ILE ASP GLU GLU GLY LEU ILE ARG ILE MET ARG GLU
SEQRES 19 B 309 ARG GLU ASP LEU ILE TYR ILE THR ASP VAL ALA PRO THR
SEQRES 20 B 309 SER LYS VAL PHE ASN ASN GLU PHE LYS GLY ARG PHE PHE
SEQRES 21 B 309 ALA THR PRO ILE LYS ILE GLY ALA GLU THR GLU GLU SER
SEQRES 22 B 309 ASN ILE ASN ALA GLY MET ALA ALA ALA SER GLN ILE CYS
SEQRES 23 B 309 ASP PHE PHE THR ASN GLY THR VAL LYS PHE GLN VAL ASN
SEQRES 24 B 309 LYS PHE LEU GLU HIS HIS HIS HIS HIS HIS
HET NAD A 401 44
HET FMT A 402 3
HET FMT B 401 3
HET TRS B 402 8
HET GOL B 403 6
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM FMT FORMIC ACID
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETSYN TRS TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAD C21 H27 N7 O14 P2
FORMUL 4 FMT 2(C H2 O2)
FORMUL 6 TRS C4 H12 N O3 1+
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *148(H2 O)
HELIX 1 1 ALA A 12 ALA A 26 1 15
HELIX 2 2 GLU A 40 ILE A 46 1 7
HELIX 3 3 ASP A 60 GLY A 67 1 8
HELIX 4 4 ASP A 84 GLY A 91 1 8
HELIX 5 5 ASN A 102 ARG A 119 1 18
HELIX 6 6 LYS A 120 LYS A 123 5 4
HELIX 7 7 GLY A 141 GLY A 155 1 15
HELIX 8 8 LYS A 173 CYS A 181 1 9
HELIX 9 9 GLY A 199 LYS A 204 1 6
HELIX 10 10 ARG A 217 ILE A 221 5 5
HELIX 11 11 ASP A 222 ARG A 233 1 12
HELIX 12 12 LYS A 247 PHE A 253 1 7
HELIX 13 13 THR A 268 GLY A 290 1 23
HELIX 14 14 ALA B 12 ALA B 26 1 15
HELIX 15 15 LYS B 39 LYS B 47 1 9
HELIX 16 16 ASP B 60 GLY B 67 1 8
HELIX 17 17 ASP B 84 GLY B 91 1 8
HELIX 18 18 ASN B 102 ARG B 119 1 18
HELIX 19 19 LYS B 120 LYS B 123 5 4
HELIX 20 20 GLY B 141 GLY B 155 1 15
HELIX 21 21 LYS B 173 CYS B 181 1 9
HELIX 22 22 GLY B 199 LYS B 204 1 6
HELIX 23 23 ARG B 217 ILE B 221 5 5
HELIX 24 24 ASP B 222 ARG B 233 1 12
HELIX 25 25 LYS B 247 PHE B 253 1 7
HELIX 26 26 THR B 268 GLY B 290 1 23
SHEET 1 A 5 GLU A 29 GLU A 34 0
SHEET 2 A 5 LYS A 2 THR A 7 1 N ILE A 3 O GLU A 29
SHEET 3 A 5 GLY A 51 VAL A 54 1 O ILE A 53 N ILE A 6
SHEET 4 A 5 ILE A 72 ARG A 75 1 O VAL A 74 N VAL A 52
SHEET 5 A 5 VAL A 94 MET A 96 1 O MET A 96 N ARG A 75
SHEET 1 B 6 LYS A 157 TYR A 161 0
SHEET 2 B 6 THR A 134 CYS A 138 1 N LEU A 135 O LYS A 157
SHEET 3 B 6 VAL A 183 LEU A 186 1 O VAL A 183 N GLY A 136
SHEET 4 B 6 MET A 211 ASN A 214 1 O CYS A 213 N ILE A 184
SHEET 5 B 6 ILE A 237 THR A 240 1 O ILE A 239 N ASN A 214
SHEET 6 B 6 PHE A 257 ALA A 259 1 O PHE A 258 N THR A 240
SHEET 1 C 5 GLU B 29 GLU B 34 0
SHEET 2 C 5 LYS B 2 THR B 7 1 N ILE B 3 O GLU B 29
SHEET 3 C 5 GLY B 51 VAL B 54 1 O ILE B 53 N ILE B 6
SHEET 4 C 5 ILE B 72 ARG B 75 1 O VAL B 74 N VAL B 52
SHEET 5 C 5 VAL B 94 MET B 96 1 O VAL B 94 N ILE B 73
SHEET 1 D 6 LYS B 157 TYR B 161 0
SHEET 2 D 6 THR B 134 CYS B 138 1 N LEU B 135 O LYS B 157
SHEET 3 D 6 VAL B 183 LEU B 186 1 O VAL B 183 N GLY B 136
SHEET 4 D 6 MET B 211 ASN B 214 1 O CYS B 213 N ILE B 184
SHEET 5 D 6 ILE B 237 THR B 240 1 O ILE B 239 N ILE B 212
SHEET 6 D 6 PHE B 257 ALA B 259 1 O PHE B 258 N THR B 240
SITE 1 AC1 25 ALA A 78 ASN A 102 VAL A 106 GLY A 139
SITE 2 AC1 25 GLY A 141 TYR A 142 VAL A 143 ASP A 162
SITE 3 AC1 25 PRO A 163 PHE A 164 HIS A 187 LEU A 188
SITE 4 AC1 25 PRO A 189 GLU A 193 THR A 194 THR A 215
SITE 5 AC1 25 ALA A 216 ARG A 217 ASP A 241 LYS A 263
SITE 6 AC1 25 GLY A 265 ALA A 266 FMT A 402 HOH A 507
SITE 7 AC1 25 HOH A 519
SITE 1 AC2 6 ARG A 75 ALA A 78 GLY A 79 ARG A 217
SITE 2 AC2 6 LYS A 263 NAD A 401
SITE 1 AC3 7 ARG B 75 GLY B 77 ALA B 78 GLY B 79
SITE 2 AC3 7 ASN B 102 ARG B 217 GOL B 403
SITE 1 AC4 5 GLY B 141 TYR B 142 VAL B 143 GLY B 144
SITE 2 AC4 5 HIS B 187
SITE 1 AC5 6 LYS B 9 ARG B 55 SER B 56 ARG B 75
SITE 2 AC5 6 ALA B 266 FMT B 401
CRYST1 49.378 56.857 57.259 66.71 66.22 77.36 P 1 2
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 0.020252 -0.004542 -0.007840 0.00000
SCALE2 0.000000 0.018025 -0.006603 0.00000
SCALE3 0.000000 0.000000 0.020325 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
