HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 23-JAN-06 2FSU
TITLE CRYSTAL STRUCTURE OF THE PHNH PROTEIN FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN PHNH;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHNH
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS C-P LYASE, PHNH, PHOSPHONATE METABOLISM, STRUCTURAL GENOMICS,
KEYWDS 2 MONTREAL-KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE, BSGI,
KEYWDS 3 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.ADAMS,Y.LUO,D.L.ZECHEL,Z.JIA,MONTREAL-KINGSTON BACTERIAL
AUTHOR 2 STRUCTURAL GENOMICS INITIATIVE (BSGI)
REVDAT 7 24-JUL-19 2FSU 1 REMARK LINK
REVDAT 6 13-JUL-11 2FSU 1 VERSN
REVDAT 5 09-JUN-09 2FSU 1 REVDAT
REVDAT 4 24-FEB-09 2FSU 1 VERSN
REVDAT 3 20-JAN-09 2FSU 1 JRNL
REVDAT 2 01-MAY-07 2FSU 1 KEYWDS AUTHOR REMARK MASTER
REVDAT 2 2 1 HEADER
REVDAT 1 27-MAR-07 2FSU 0
JRNL AUTH M.A.ADAMS,Y.LUO,B.HOVE-JENSEN,S.M.HE,L.M.VAN STAALDUINEN,
JRNL AUTH 2 D.L.ZECHEL,Z.JIA
JRNL TITL CRYSTAL STRUCTURE OF PHNH: AN ESSENTIAL COMPONENT OF
JRNL TITL 2 CARBON-PHOSPHORUS LYASE IN ESCHERICHIA COLI.
JRNL REF J.BACTERIOL. V. 190 1072 2008
JRNL REFN ISSN 0021-9193
JRNL PMID 17993513
JRNL DOI 10.1128/JB.01274-07
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 18698
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 977
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1213
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1274
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 184
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.04000
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): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.994
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
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): 1315 ; 0.029 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1797 ; 2.308 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 171 ; 6.211 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;33.721 ;24.808
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 216 ;13.451 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;14.545 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 223 ; 0.194 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 977 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 700 ; 0.269 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 931 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 146 ; 0.194 ; 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): 70 ; 0.313 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.269 ; 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): 861 ; 1.645 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1387 ; 2.706 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 464 ; 4.537 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 409 ; 7.342 ; 4.500
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: NULL
REMARK 4
REMARK 4 2FSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036269.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979029, 0.978681, 0.925256
REMARK 200 MONOCHROMATOR : MONOCHROMATOR: SI(111) CHANNEL
REMARK 200 CUT MONOCHROMATOR.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24912
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 42.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 35.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM ACETATE, PEG 4000, SODIUM
REMARK 280 CITRATE PH 3.5 WITH PROTEIN IN HEPES BUFFER, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 37.94500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.94500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 26.51000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.70900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.51000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.70900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.94500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.51000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.70900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 37.94500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.51000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.70900
REMARK 290 SMTRY3 8 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 37.94500
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 671 LIES ON A SPECIAL POSITION.
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 MSE A -15
REMARK 465 ARG A -14
REMARK 465 GLY A -13
REMARK 465 SER A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 GLY A -5
REMARK 465 SER A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 MSE A -1
REMARK 465 GLY A 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 LEU A 3
REMARK 465 GLU A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 PHE A 7
REMARK 465 MSE A 8
REMARK 465 LEU A 9
REMARK 465 PRO A 10
REMARK 465 VAL A 11
REMARK 465 THR A 111
REMARK 465 GLY A 112
REMARK 465 THR A 113
REMARK 465 ALA A 114
REMARK 465 VAL A 115
REMARK 465 ALA A 116
REMARK 465 PRO A 117
REMARK 465 GLU A 118
REMARK 465 ALA A 119
REMARK 465 ALA A 141
REMARK 465 GLY A 142
REMARK 465 ILE A 143
REMARK 465 ALA A 144
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 GLN A 12 CG CD OE1 NE2
REMARK 470 LYS A 38 CB CG CD CE NZ
REMARK 470 ARG A 39 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 134 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 145 CG CD OE1 OE2
REMARK 470 PRO A 167 CG CD
REMARK 470 PHE A 168 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 169 CG CD
REMARK 470 LEU A 170 CG CD1 CD2
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 N GLY A 120 O HOH A 508 2.03
REMARK 500 OE1 GLU A 192 O HOH A 686 2.04
REMARK 500 O ACT A 502 O HOH A 674 2.05
REMARK 500 CD GLU A 192 O HOH A 686 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU A 99 O HOH A 655 3655 1.99
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 TRP A 63 CG TRP A 63 CD1 0.099
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 LEU A 34 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 78 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 PRO A 169 N - CA - CB ANGL. DEV. = 8.9 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 57 -158.74 -148.24
REMARK 500 ASN A 82 17.64 51.39
REMARK 500 ASP A 98 -164.31 -104.27
REMARK 500 ALA A 150 55.30 -149.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 509 O
REMARK 620 2 HOH A 509 O 93.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 503 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 540 O
REMARK 620 2 HOH A 668 O 115.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PHNH_ECOLI RELATED DB: TARGETDB
DBREF 2FSU A 1 194 UNP P16686 PHNH_ECOLI 1 194
SEQADV 2FSU MSE A -15 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU ARG A -14 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU GLY A -13 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU SER A -12 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU HIS A -11 UNP P16686 EXPRESSION TAG
SEQADV 2FSU HIS A -10 UNP P16686 EXPRESSION TAG
SEQADV 2FSU HIS A -9 UNP P16686 EXPRESSION TAG
SEQADV 2FSU HIS A -8 UNP P16686 EXPRESSION TAG
SEQADV 2FSU HIS A -7 UNP P16686 EXPRESSION TAG
SEQADV 2FSU HIS A -6 UNP P16686 EXPRESSION TAG
SEQADV 2FSU GLY A -5 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU SER A -4 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU GLY A -3 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU SER A -2 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU MSE A -1 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU GLY A 0 UNP P16686 CLONING ARTIFACT
SEQADV 2FSU MSE A 1 UNP P16686 MET 1 MODIFIED RESIDUE
SEQADV 2FSU MSE A 8 UNP P16686 MET 8 MODIFIED RESIDUE
SEQADV 2FSU MSE A 25 UNP P16686 MET 25 MODIFIED RESIDUE
SEQADV 2FSU MSE A 135 UNP P16686 MET 135 MODIFIED RESIDUE
SEQADV 2FSU MSE A 148 UNP P16686 MET 148 MODIFIED RESIDUE
SEQRES 1 A 210 MSE ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLY
SEQRES 2 A 210 SER MSE GLY MSE THR LEU GLU THR ALA PHE MSE LEU PRO
SEQRES 3 A 210 VAL GLN ASP ALA GLN HIS SER PHE ARG ARG LEU LEU LYS
SEQRES 4 A 210 ALA MSE SER GLU PRO GLY VAL ILE VAL ALA LEU HIS GLN
SEQRES 5 A 210 LEU LYS ARG GLY TRP GLN PRO LEU ASN ILE ALA THR THR
SEQRES 6 A 210 SER VAL LEU LEU THR LEU ALA ASP ASN ASP THR PRO VAL
SEQRES 7 A 210 TRP LEU SER THR PRO LEU ASN ASN ASP ILE VAL ASN GLN
SEQRES 8 A 210 SER LEU ARG PHE HIS THR ASN ALA PRO LEU VAL SER GLN
SEQRES 9 A 210 PRO GLU GLN ALA THR PHE ALA VAL THR ASP GLU ALA ILE
SEQRES 10 A 210 SER SER GLU GLN LEU ASN ALA LEU SER THR GLY THR ALA
SEQRES 11 A 210 VAL ALA PRO GLU ALA GLY ALA THR LEU ILE LEU GLN VAL
SEQRES 12 A 210 ALA SER LEU SER GLY GLY ARG MSE LEU ARG LEU THR GLY
SEQRES 13 A 210 ALA GLY ILE ALA GLU GLU ARG MSE ILE ALA PRO GLN LEU
SEQRES 14 A 210 PRO GLU CYS ILE LEU HIS GLU LEU THR GLU ARG PRO HIS
SEQRES 15 A 210 PRO PHE PRO LEU GLY ILE ASP LEU ILE LEU THR CYS GLY
SEQRES 16 A 210 GLU ARG LEU LEU ALA ILE PRO ARG THR THR HIS VAL GLU
SEQRES 17 A 210 VAL CYS
MODRES 2FSU MSE A 25 MET SELENOMETHIONINE
MODRES 2FSU MSE A 135 MET SELENOMETHIONINE
MODRES 2FSU MSE A 148 MET SELENOMETHIONINE
HET MSE A 25 16
HET MSE A 135 13
HET MSE A 148 8
HET NA A 501 1
HET ACT A 502 4
HET NA A 503 1
HET NA A 504 1
HET NA A 505 1
HETNAM MSE SELENOMETHIONINE
HETNAM NA SODIUM ION
HETNAM ACT ACETATE ION
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 NA 4(NA 1+)
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 7 HOH *184(H2 O)
HELIX 1 1 ASP A 13 GLU A 27 1 15
HELIX 2 2 ASN A 45 SER A 50 1 6
HELIX 3 3 VAL A 51 ALA A 56 1 6
HELIX 4 4 THR A 66 ASN A 69 5 4
HELIX 5 5 ASN A 70 ASN A 82 1 13
HELIX 6 6 GLN A 88 ALA A 92 5 5
HELIX 7 7 SER A 102 LEU A 109 1 8
HELIX 8 8 PRO A 154 ARG A 164 1 11
SHEET 1 A 6 VAL A 32 ALA A 33 0
SHEET 2 A 6 ARG A 181 ILE A 185 -1 O LEU A 182 N VAL A 32
SHEET 3 A 6 ASP A 173 CYS A 178 -1 N LEU A 174 O ILE A 185
SHEET 4 A 6 THR A 122 GLN A 126 1 N LEU A 123 O ILE A 175
SHEET 5 A 6 PHE A 94 THR A 97 1 N ALA A 95 O ILE A 124
SHEET 6 A 6 VAL A 62 LEU A 64 1 N TRP A 63 O VAL A 96
SHEET 1 B 3 ARG A 147 ILE A 149 0
SHEET 2 B 3 LEU A 136 THR A 139 -1 N LEU A 136 O ILE A 149
SHEET 3 B 3 HIS A 190 VAL A 193 -1 O HIS A 190 N THR A 139
LINK NA NA A 501 O HOH A 509 1555 1555 2.86
LINK NA NA A 503 O HOH A 540 1555 1555 2.68
LINK NA NA A 503 O HOH A 668 1555 1555 2.62
LINK NA NA A 504 O HOH A 584 1555 1555 2.64
LINK C ALA A 24 N AMSE A 25 1555 1555 1.32
LINK C ALA A 24 N BMSE A 25 1555 1555 1.29
LINK C AMSE A 25 N SER A 26 1555 1555 1.35
LINK C BMSE A 25 N SER A 26 1555 1555 1.33
LINK C ARG A 134 N MSE A 135 1555 1555 1.34
LINK C MSE A 135 N LEU A 136 1555 1555 1.34
LINK C ARG A 147 N MSE A 148 1555 1555 1.32
LINK C MSE A 148 N ILE A 149 1555 1555 1.38
LINK NA NA A 501 O HOH A 509 1555 3655 2.59
CISPEP 1 GLN A 42 PRO A 43 0 10.85
CISPEP 2 PHE A 168 PRO A 169 0 1.37
SITE 1 AC1 2 LEU A 153 HOH A 509
SITE 1 AC2 8 PRO A 89 GLU A 90 ALA A 92 ALA A 108
SITE 2 AC2 8 LEU A 109 SER A 110 HOH A 627 HOH A 674
SITE 1 AC3 3 PHE A 94 HOH A 540 HOH A 668
SITE 1 AC4 2 HOH A 584 HOH A 631
SITE 1 AC5 1 MSE A 25
CRYST1 53.020 87.418 75.890 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018861 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011439 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013177 0.00000
(ATOM LINES ARE NOT SHOWN.)
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