HEADER TRANSFERASE 10-JAN-06 2FN6
TITLE HELICOBACTER PYLORI PSEC, AMINOTRANSFERASE INVOLVED IN THE
TITLE 2 BIOSYNTHESIS OF PSEUDOAMINIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_TAXID: 85962;
SOURCE 4 STRAIN: 26695;
SOURCE 5 GENE: HP0366;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS AMINOTRANSFERASE, PSEUDOAMINIC ACID BIOSYNTHESIS, FLAGELLAR
KEYWDS 2 MODIFICATION, STRUCTURAL GENOMICS, MONTREAL-KINGSTON BACTERIAL
KEYWDS 3 STRUCTURAL GENOMICS INITIATIVE, BSGI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CYGLER,V.V.LUNIN,A.MATTE,MONTREAL-KINGSTON BACTERIAL STRUCTURAL
AUTHOR 2 GENOMICS INITIATIVE (BSGI)
REVDAT 5 30-AUG-23 2FN6 1 REMARK
REVDAT 4 13-JUL-11 2FN6 1 VERSN
REVDAT 3 24-FEB-09 2FN6 1 VERSN
REVDAT 2 11-APR-06 2FN6 1 JRNL
REVDAT 1 24-JAN-06 2FN6 0
JRNL AUTH I.C.SCHOENHOFEN,V.V.LUNIN,J.P.JULIEN,Y.LI,E.AJAMIAN,A.MATTE,
JRNL AUTH 2 M.CYGLER,J.R.BRISSON,A.AUBRY,S.M.LOGAN,S.BHATIA,
JRNL AUTH 3 W.W.WAKARCHUK,N.M.YOUNG
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF PSEC, AN
JRNL TITL 2 AMINOTRANSFERASE INVOLVED IN THE BIOSYNTHESIS OF PSEUDAMINIC
JRNL TITL 3 ACID, AN ESSENTIAL FLAGELLAR MODIFICATION IN HELICOBACTER
JRNL TITL 4 PYLORI
JRNL REF J.BIOL.CHEM. V. 281 8907 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16421095
JRNL DOI 10.1074/JBC.M512987200
REMARK 2
REMARK 2 RESOLUTION. 2.48 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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 33236
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1754
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) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2410
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5895
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : -0.71000
REMARK 3 B33 (A**2) : 1.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.430
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.291
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.219
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.854
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6066 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8185 ; 1.264 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 745 ; 5.912 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 271 ;38.985 ;24.686
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1103 ;17.410 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.979 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 916 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4500 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2749 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4134 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 236 ; 0.120 ; 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): 16 ; 0.182 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.045 ; 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): 3796 ; 1.677 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5988 ; 2.933 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2486 ; 3.192 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2197 ; 4.959 ;10.000
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 2FN6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35038
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.483
REMARK 200 RESOLUTION RANGE LOW (A) : 77.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1MDO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXING 1.5 MICROL OF PROTEIN IN BUFFER
REMARK 280 WITH 1.5 MICROL OF RESERVOIR SOLUTION CONTAINING 0.2 M AMMONIUM
REMARK 280 ACETATE, 0.1 M TRISODIUM CITRATE PH 5.6, 30% PEG 4000., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 43.84550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.71200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.84550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.71200
REMARK 290 SMTRY3 4 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: 6000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 MET A 1
REMARK 465 ILE A 374
REMARK 465 GLU A 375
REMARK 465 MET B 1
REMARK 465 LYS B 373
REMARK 465 ILE B 374
REMARK 465 GLU B 375
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 GLU A 39 CD OE1 OE2
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 ASP A 216 CG OD1 OD2
REMARK 470 GLU A 370 CG CD OE1 OE2
REMARK 470 LYS A 373 CG CD CE NZ
REMARK 470 GLU B 370 CG CD OE1 OE2
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 ASN A 119 -152.62 -144.77
REMARK 500 ASN A 119 -152.62 -135.48
REMARK 500 ALA A 131 -1.92 69.28
REMARK 500 GLN A 164 62.66 38.32
REMARK 500 ASN A 165 22.54 45.92
REMARK 500 ALA A 188 -67.06 72.81
REMARK 500 LYS A 215 -119.18 -149.28
REMARK 500 ASP A 216 -34.60 -39.64
REMARK 500 PHE A 217 -31.70 108.82
REMARK 500 HIS A 227 -166.14 -119.94
REMARK 500 LYS A 298 -71.17 -35.29
REMARK 500 ASN A 330 59.08 39.96
REMARK 500 PHE A 372 -125.69 -100.17
REMARK 500 ARG B 74 74.50 -103.39
REMARK 500 ALA B 113 25.49 -62.20
REMARK 500 ASN B 119 -146.33 -121.08
REMARK 500 ALA B 181 -38.61 -33.01
REMARK 500 ALA B 188 -63.39 73.06
REMARK 500 LYS B 215 -85.90 -97.68
REMARK 500 ASP B 216 -164.59 -109.82
REMARK 500 HIS B 227 -164.02 -116.70
REMARK 500 ASP B 266 18.53 52.15
REMARK 500 LYS B 293 -6.40 -56.46
REMARK 500 ASN B 330 -2.37 56.59
REMARK 500 THR B 331 124.12 -9.85
REMARK 500 PRO B 333 144.05 -33.15
REMARK 500 SER B 371 23.91 -70.04
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 PO4 A 376
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 376
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HEP0366_HELPY RELATED DB: TARGETDB
DBREF 2FN6 A 1 375 GB 2313467 AAD07433 1 375
DBREF 2FN6 B 1 375 GB 2313467 AAD07433 1 375
SEQRES 1 A 375 MET LYS GLU PHE ALA TYR SER GLU PRO CYS LEU ASP LYS
SEQRES 2 A 375 GLU ASP LYS LYS ALA VAL LEU GLU VAL LEU ASN SER LYS
SEQRES 3 A 375 GLN LEU THR GLN GLY LYS ARG SER LEU LEU PHE GLU GLU
SEQRES 4 A 375 ALA LEU CYS GLU PHE LEU GLY VAL LYS HIS ALA LEU VAL
SEQRES 5 A 375 PHE ASN SER ALA THR SER ALA LEU LEU THR LEU TYR ARG
SEQRES 6 A 375 ASN PHE SER GLU PHE SER ALA ASP ARG ASN GLU ILE ILE
SEQRES 7 A 375 THR THR PRO ILE SER PHE VAL ALA THR ALA ASN MET LEU
SEQRES 8 A 375 LEU GLU SER GLY TYR THR PRO VAL PHE ALA GLY ILE LYS
SEQRES 9 A 375 ASN ASP GLY ASN ILE ASP GLU LEU ALA LEU GLU LYS LEU
SEQRES 10 A 375 ILE ASN GLU ARG THR LYS ALA ILE VAL SER VAL ASP TYR
SEQRES 11 A 375 ALA GLY LYS SER VAL GLU VAL GLU SER VAL GLN LYS LEU
SEQRES 12 A 375 CYS LYS LYS HIS SER LEU SER PHE LEU SER ASP SER SER
SEQRES 13 A 375 HIS ALA LEU GLY SER GLU TYR GLN ASN LYS LYS VAL GLY
SEQRES 14 A 375 GLY PHE ALA LEU ALA SER VAL PHE SER PHE HIS ALA ILE
SEQRES 15 A 375 LYS PRO ILE THR THR ALA GLU GLY GLY ALA VAL VAL THR
SEQRES 16 A 375 ASN ASP SER GLU LEU HIS GLU LYS MET LYS LEU PHE ARG
SEQRES 17 A 375 SER HIS GLY MET LEU LYS LYS ASP PHE PHE GLU GLY GLU
SEQRES 18 A 375 VAL LYS SER ILE GLY HIS ASN PHE ARG LEU ASN GLU ILE
SEQRES 19 A 375 GLN SER ALA LEU GLY LEU SER GLN LEU LYS LYS ALA PRO
SEQRES 20 A 375 PHE LEU MET GLN LYS ARG GLU GLU ALA ALA LEU THR TYR
SEQRES 21 A 375 ASP ARG ILE PHE LYS ASP ASN PRO TYR PHE THR PRO LEU
SEQRES 22 A 375 HIS PRO LEU LEU LYS ASP LYS SER SER ASN HIS LEU TYR
SEQRES 23 A 375 PRO ILE LEU MET HIS GLN LYS PHE PHE THR CYS LYS LYS
SEQRES 24 A 375 LEU ILE LEU GLU SER LEU HIS LYS ARG GLY ILE LEU ALA
SEQRES 25 A 375 GLN VAL HIS TYR LYS PRO ILE TYR GLN TYR GLN LEU TYR
SEQRES 26 A 375 GLN GLN LEU PHE ASN THR ALA PRO LEU LYS SER ALA GLU
SEQRES 27 A 375 ASP PHE TYR HIS ALA GLU ILE SER LEU PRO CYS HIS ALA
SEQRES 28 A 375 ASN LEU ASN LEU GLU SER VAL GLN ASN ILE ALA HIS SER
SEQRES 29 A 375 VAL LEU LYS THR PHE GLU SER PHE LYS ILE GLU
SEQRES 1 B 375 MET LYS GLU PHE ALA TYR SER GLU PRO CYS LEU ASP LYS
SEQRES 2 B 375 GLU ASP LYS LYS ALA VAL LEU GLU VAL LEU ASN SER LYS
SEQRES 3 B 375 GLN LEU THR GLN GLY LYS ARG SER LEU LEU PHE GLU GLU
SEQRES 4 B 375 ALA LEU CYS GLU PHE LEU GLY VAL LYS HIS ALA LEU VAL
SEQRES 5 B 375 PHE ASN SER ALA THR SER ALA LEU LEU THR LEU TYR ARG
SEQRES 6 B 375 ASN PHE SER GLU PHE SER ALA ASP ARG ASN GLU ILE ILE
SEQRES 7 B 375 THR THR PRO ILE SER PHE VAL ALA THR ALA ASN MET LEU
SEQRES 8 B 375 LEU GLU SER GLY TYR THR PRO VAL PHE ALA GLY ILE LYS
SEQRES 9 B 375 ASN ASP GLY ASN ILE ASP GLU LEU ALA LEU GLU LYS LEU
SEQRES 10 B 375 ILE ASN GLU ARG THR LYS ALA ILE VAL SER VAL ASP TYR
SEQRES 11 B 375 ALA GLY LYS SER VAL GLU VAL GLU SER VAL GLN LYS LEU
SEQRES 12 B 375 CYS LYS LYS HIS SER LEU SER PHE LEU SER ASP SER SER
SEQRES 13 B 375 HIS ALA LEU GLY SER GLU TYR GLN ASN LYS LYS VAL GLY
SEQRES 14 B 375 GLY PHE ALA LEU ALA SER VAL PHE SER PHE HIS ALA ILE
SEQRES 15 B 375 LYS PRO ILE THR THR ALA GLU GLY GLY ALA VAL VAL THR
SEQRES 16 B 375 ASN ASP SER GLU LEU HIS GLU LYS MET LYS LEU PHE ARG
SEQRES 17 B 375 SER HIS GLY MET LEU LYS LYS ASP PHE PHE GLU GLY GLU
SEQRES 18 B 375 VAL LYS SER ILE GLY HIS ASN PHE ARG LEU ASN GLU ILE
SEQRES 19 B 375 GLN SER ALA LEU GLY LEU SER GLN LEU LYS LYS ALA PRO
SEQRES 20 B 375 PHE LEU MET GLN LYS ARG GLU GLU ALA ALA LEU THR TYR
SEQRES 21 B 375 ASP ARG ILE PHE LYS ASP ASN PRO TYR PHE THR PRO LEU
SEQRES 22 B 375 HIS PRO LEU LEU LYS ASP LYS SER SER ASN HIS LEU TYR
SEQRES 23 B 375 PRO ILE LEU MET HIS GLN LYS PHE PHE THR CYS LYS LYS
SEQRES 24 B 375 LEU ILE LEU GLU SER LEU HIS LYS ARG GLY ILE LEU ALA
SEQRES 25 B 375 GLN VAL HIS TYR LYS PRO ILE TYR GLN TYR GLN LEU TYR
SEQRES 26 B 375 GLN GLN LEU PHE ASN THR ALA PRO LEU LYS SER ALA GLU
SEQRES 27 B 375 ASP PHE TYR HIS ALA GLU ILE SER LEU PRO CYS HIS ALA
SEQRES 28 B 375 ASN LEU ASN LEU GLU SER VAL GLN ASN ILE ALA HIS SER
SEQRES 29 B 375 VAL LEU LYS THR PHE GLU SER PHE LYS ILE GLU
HET PO4 A 376 5
HET PO4 B 376 5
HETNAM PO4 PHOSPHATE ION
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *119(H2 O)
HELIX 1 1 ASP A 12 SER A 25 1 14
HELIX 2 2 GLY A 31 GLY A 46 1 16
HELIX 3 3 SER A 55 PHE A 67 1 13
HELIX 4 4 VAL A 85 SER A 94 1 10
HELIX 5 5 ASP A 110 ILE A 118 5 9
HELIX 6 6 TYR A 130 LYS A 133 5 4
HELIX 7 7 GLU A 136 HIS A 147 1 12
HELIX 8 8 ASP A 197 ARG A 208 1 12
HELIX 9 9 ASN A 232 LYS A 244 1 13
HELIX 10 10 LYS A 245 LYS A 265 1 21
HELIX 11 11 HIS A 274 LEU A 277 5 4
HELIX 12 12 GLN A 292 THR A 296 5 5
HELIX 13 13 CYS A 297 ARG A 308 1 12
HELIX 14 14 PRO A 318 GLN A 321 5 4
HELIX 15 15 TYR A 322 PHE A 329 1 8
HELIX 16 16 LEU A 334 ALA A 343 1 10
HELIX 17 17 ASN A 354 SER A 371 1 18
HELIX 18 18 ASP B 12 ASN B 24 1 13
HELIX 19 19 GLY B 31 GLY B 46 1 16
HELIX 20 20 SER B 55 PHE B 67 1 13
HELIX 21 21 VAL B 85 SER B 94 1 10
HELIX 22 22 TYR B 130 LYS B 133 5 4
HELIX 23 23 GLU B 136 HIS B 147 1 12
HELIX 24 24 ASP B 197 SER B 209 1 13
HELIX 25 25 ASN B 232 LYS B 244 1 13
HELIX 26 26 LYS B 245 LYS B 265 1 21
HELIX 27 27 HIS B 274 LEU B 277 5 4
HELIX 28 28 GLN B 292 THR B 296 5 5
HELIX 29 29 CYS B 297 ARG B 308 1 12
HELIX 30 30 PRO B 318 GLN B 321 5 4
HELIX 31 31 TYR B 322 ASN B 330 1 9
HELIX 32 32 LEU B 334 ALA B 343 1 10
HELIX 33 33 ASN B 354 SER B 371 1 18
SHEET 1 A 2 PHE A 4 ALA A 5 0
SHEET 2 A 2 ILE A 310 LEU A 311 1 O LEU A 311 N PHE A 4
SHEET 1 B 7 HIS A 49 PHE A 53 0
SHEET 2 B 7 GLY A 191 THR A 195 -1 O GLY A 191 N PHE A 53
SHEET 3 B 7 ALA A 174 SER A 178 -1 N SER A 175 O VAL A 194
SHEET 4 B 7 SER A 150 ASP A 154 1 N SER A 153 O VAL A 176
SHEET 5 B 7 THR A 122 VAL A 128 1 N SER A 127 O ASP A 154
SHEET 6 B 7 GLU A 76 THR A 79 1 N ILE A 78 O VAL A 126
SHEET 7 B 7 THR A 97 PHE A 100 1 O VAL A 99 N ILE A 77
SHEET 1 C 2 GLU A 162 TYR A 163 0
SHEET 2 C 2 LYS A 166 LYS A 167 -1 O LYS A 166 N TYR A 163
SHEET 1 D 2 MET A 212 LYS A 214 0
SHEET 2 D 2 GLY A 220 VAL A 222 -1 O GLU A 221 N LEU A 213
SHEET 1 E 3 PHE A 270 PRO A 272 0
SHEET 2 E 3 TYR A 286 MET A 290 -1 O LEU A 289 N THR A 271
SHEET 3 E 3 GLU A 344 LEU A 347 -1 O ILE A 345 N ILE A 288
SHEET 1 F 2 PHE B 4 ALA B 5 0
SHEET 2 F 2 ILE B 310 LEU B 311 1 O LEU B 311 N PHE B 4
SHEET 1 G 7 HIS B 49 PHE B 53 0
SHEET 2 G 7 GLY B 191 THR B 195 -1 O GLY B 191 N PHE B 53
SHEET 3 G 7 ALA B 174 SER B 178 -1 N SER B 175 O VAL B 194
SHEET 4 G 7 SER B 150 ASP B 154 1 N SER B 153 O VAL B 176
SHEET 5 G 7 THR B 122 VAL B 128 1 N SER B 127 O ASP B 154
SHEET 6 G 7 GLU B 76 THR B 79 1 N GLU B 76 O LYS B 123
SHEET 7 G 7 THR B 97 PHE B 100 1 O THR B 97 N ILE B 77
SHEET 1 H 2 GLU B 162 TYR B 163 0
SHEET 2 H 2 LYS B 166 LYS B 167 -1 O LYS B 166 N TYR B 163
SHEET 1 I 2 MET B 212 LYS B 214 0
SHEET 2 I 2 GLY B 220 VAL B 222 -1 O GLU B 221 N LEU B 213
SHEET 1 J 3 PHE B 270 PRO B 272 0
SHEET 2 J 3 TYR B 286 MET B 290 -1 O LEU B 289 N THR B 271
SHEET 3 J 3 GLU B 344 LEU B 347 -1 O LEU B 347 N TYR B 286
CISPEP 1 HIS A 315 TYR A 316 0 -1.83
CISPEP 2 HIS B 315 TYR B 316 0 2.28
SITE 1 AC1 6 SER A 55 ALA A 56 THR A 57 SER A 178
SITE 2 AC1 6 HOH A 418 ASN B 228
SITE 1 AC2 5 ASN A 228 SER B 55 ALA B 56 THR B 57
SITE 2 AC2 5 SER B 178
CRYST1 87.691 155.424 71.482 90.00 90.00 90.00 P 21 21 2 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 0.011404 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006434 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013990 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
