HEADER HYDROLASE 20-JAN-06 2FS2
TITLE STRUCTURE OF THE E. COLI PAAI PROTEIN FROM THE PHYENYLACETIC ACID
TITLE 2 DEGRADATION OPERON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLACETIC ACID DEGRADATION PROTEIN PAAI;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PAAI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: TOPO-ADAPTED C-TERM HEXAHISTIDINE TAG
KEYWDS T820, PHENYLACETIC ACID, DEGRADATION, OPERON, STRUCTURAL GENOMICS,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, NYSGXRC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KNIEWEL,J.A.BUGLINO,V.SOLORZANO,J.WU,C.D.LIMA,S.K.BURLEY,NEW YORK
AUTHOR 2 SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 5 03-FEB-21 2FS2 1 AUTHOR REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2FS2 1 REMARK
REVDAT 3 24-FEB-09 2FS2 1 VERSN
REVDAT 2 02-MAY-06 2FS2 1 JRNL
REVDAT 1 07-FEB-06 2FS2 0
JRNL AUTH F.SONG,Z.ZHUANG,L.FINCI,D.DUNAWAY-MARIANO,R.KNIEWEL,
JRNL AUTH 2 J.A.BUGLINO,V.SOLORZANO,J.WU,C.D.LIMA
JRNL TITL STRUCTURE, FUNCTION, AND MECHANISM OF THE PHENYLACETATE
JRNL TITL 2 PATHWAY HOT DOG-FOLD THIOESTERASE PAAI
JRNL REF J.BIOL.CHEM. V. 281 11028 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16464851
JRNL DOI 10.1074/JBC.M513896200
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.1
REMARK 3 NUMBER OF REFLECTIONS : 19072
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 981
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 920
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE SET COUNT : 51
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2014
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 79
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.06000
REMARK 3 B22 (A**2) : 1.06000
REMARK 3 B33 (A**2) : -1.59000
REMARK 3 B12 (A**2) : 0.53000
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): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.145
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2062 ; 0.031 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2790 ; 2.329 ; 1.916
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 268 ; 7.143 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.167 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1560 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 866 ; 0.247 ; 0.200
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): 109 ; 0.200 ; 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): 36 ; 0.213 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.221 ; 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): 1328 ; 1.608 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2102 ; 3.087 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 734 ; 5.506 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 688 ; 8.814 ; 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 : 1.40
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 2FS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000036242.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40460
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.46200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE 2.03, RESOLVE 2.02
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE NUMBER OF UNIQUE REFLECTIONS FOR THE DATA COLLECTION
REMARK 200 INCLUDES FRIEDEL PAIRS USED TO PHASE THE STRUCTURE.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 4000, 0.1M BIS-TRIS, 20% MPD,
REMARK 280 0.2M LITHIUM SULFATE, PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.05600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 78.11200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 78.11200
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.05600
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 300 REMARK: TETRAMER BY TRANSLATING THE DIMER BY
REMARK 300
REMARK 300 1 0 0
REMARK 300 0 -1 0
REMARK 300 0 0 -1
REMARK 300 TRANS 0, 121.0, 195.3
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 120.97855
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 195.28000
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 169 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 171 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 ILE A 132
REMARK 465 GLY A 133
REMARK 465 GLY A 134
REMARK 465 THR A 135
REMARK 465 ILE A 136
REMARK 465 THR A 137
REMARK 465 GLY A 138
REMARK 465 GLU A 139
REMARK 465 ALA A 140
REMARK 465 GLU A 141
REMARK 465 GLY A 142
REMARK 465 GLY A 143
REMARK 465 SER A 144
REMARK 465 HIS A 145
REMARK 465 HIS A 146
REMARK 465 HIS A 147
REMARK 465 HIS A 148
REMARK 465 HIS A 149
REMARK 465 HIS A 150
REMARK 465 GLY B 138
REMARK 465 GLU B 139
REMARK 465 ALA B 140
REMARK 465 GLU B 141
REMARK 465 GLY B 142
REMARK 465 GLY B 143
REMARK 465 SER B 144
REMARK 465 HIS B 145
REMARK 465 HIS B 146
REMARK 465 HIS B 147
REMARK 465 HIS B 148
REMARK 465 HIS B 149
REMARK 465 HIS B 150
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 86 O1 SO4 A 152 2.10
REMARK 500 O HOH A 160 O HOH A 185 2.18
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 ARG A 126 CG ARG A 126 CD 0.164
REMARK 500 GLN B 71 CG GLN B 71 CD 0.145
REMARK 500 SER B 78 CB SER B 78 OG -0.083
REMARK 500 GLN B 99 CB GLN B 99 CG -0.167
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 ASP A 25 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP A 30 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 61 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 83 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 111 CB - CG - OD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP B 30 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 THR B 81 OG1 - CB - CG2 ANGL. DEV. = -15.3 DEGREES
REMARK 500 GLN B 99 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 ASP B 111 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG B 131 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
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 SO4 B 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 152
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PSU RELATED DB: PDB
REMARK 900 PREVIOUS REFINEMENT TO 2.2
REMARK 900 RELATED ID: NYSGXRC-1PSU RELATED DB: TARGETDB
DBREF 2FS2 A 2 140 UNP P76084 PAAI_ECOLI 2 140
DBREF 2FS2 B 2 140 UNP P76084 PAAI_ECOLI 2 140
SEQADV 2FS2 SER A 0 UNP P76084 CLONING ARTIFACT
SEQADV 2FS2 LEU A 1 UNP P76084 CLONING ARTIFACT
SEQADV 2FS2 MSE A 12 UNP P76084 MET 12 MODIFIED RESIDUE
SEQADV 2FS2 MSE A 29 UNP P76084 MET 29 MODIFIED RESIDUE
SEQADV 2FS2 MSE A 38 UNP P76084 MET 38 MODIFIED RESIDUE
SEQADV 2FS2 MSE A 44 UNP P76084 MET 44 MODIFIED RESIDUE
SEQADV 2FS2 GLU A 141 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 GLY A 142 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 GLY A 143 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 SER A 144 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS A 145 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS A 146 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS A 147 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS A 148 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS A 149 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS A 150 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 SER B 0 UNP P76084 CLONING ARTIFACT
SEQADV 2FS2 LEU B 1 UNP P76084 CLONING ARTIFACT
SEQADV 2FS2 MSE B 12 UNP P76084 MET 12 MODIFIED RESIDUE
SEQADV 2FS2 MSE B 29 UNP P76084 MET 29 MODIFIED RESIDUE
SEQADV 2FS2 MSE B 38 UNP P76084 MET 38 MODIFIED RESIDUE
SEQADV 2FS2 MSE B 44 UNP P76084 MET 44 MODIFIED RESIDUE
SEQADV 2FS2 GLU B 141 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 GLY B 142 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 GLY B 143 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 SER B 144 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS B 145 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS B 146 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS B 147 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS B 148 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS B 149 UNP P76084 EXPRESSION TAG
SEQADV 2FS2 HIS B 150 UNP P76084 EXPRESSION TAG
SEQRES 1 A 151 SER LEU SER HIS LYS ALA TRP GLN ASN ALA HIS ALA MSE
SEQRES 2 A 151 TYR GLU ASN ASP ALA CYS ALA LYS ALA LEU GLY ILE ASP
SEQRES 3 A 151 ILE ILE SER MSE ASP GLU GLY PHE ALA VAL VAL THR MSE
SEQRES 4 A 151 THR VAL THR ALA GLN MSE LEU ASN GLY HIS GLN SER CYS
SEQRES 5 A 151 HIS GLY GLY GLN LEU PHE SER LEU ALA ASP THR ALA PHE
SEQRES 6 A 151 ALA TYR ALA CYS ASN SER GLN GLY LEU ALA ALA VAL ALA
SEQRES 7 A 151 SER ALA CYS THR ILE ASP PHE LEU ARG PRO GLY PHE ALA
SEQRES 8 A 151 GLY ASP THR LEU THR ALA THR ALA GLN VAL ARG HIS GLN
SEQRES 9 A 151 GLY LYS GLN THR GLY VAL TYR ASP ILE GLU ILE VAL ASN
SEQRES 10 A 151 GLN GLN GLN LYS THR VAL ALA LEU PHE ARG GLY LYS SER
SEQRES 11 A 151 HIS ARG ILE GLY GLY THR ILE THR GLY GLU ALA GLU GLY
SEQRES 12 A 151 GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 151 SER LEU SER HIS LYS ALA TRP GLN ASN ALA HIS ALA MSE
SEQRES 2 B 151 TYR GLU ASN ASP ALA CYS ALA LYS ALA LEU GLY ILE ASP
SEQRES 3 B 151 ILE ILE SER MSE ASP GLU GLY PHE ALA VAL VAL THR MSE
SEQRES 4 B 151 THR VAL THR ALA GLN MSE LEU ASN GLY HIS GLN SER CYS
SEQRES 5 B 151 HIS GLY GLY GLN LEU PHE SER LEU ALA ASP THR ALA PHE
SEQRES 6 B 151 ALA TYR ALA CYS ASN SER GLN GLY LEU ALA ALA VAL ALA
SEQRES 7 B 151 SER ALA CYS THR ILE ASP PHE LEU ARG PRO GLY PHE ALA
SEQRES 8 B 151 GLY ASP THR LEU THR ALA THR ALA GLN VAL ARG HIS GLN
SEQRES 9 B 151 GLY LYS GLN THR GLY VAL TYR ASP ILE GLU ILE VAL ASN
SEQRES 10 B 151 GLN GLN GLN LYS THR VAL ALA LEU PHE ARG GLY LYS SER
SEQRES 11 B 151 HIS ARG ILE GLY GLY THR ILE THR GLY GLU ALA GLU GLY
SEQRES 12 B 151 GLY SER HIS HIS HIS HIS HIS HIS
MODRES 2FS2 MSE A 12 MET SELENOMETHIONINE
MODRES 2FS2 MSE A 29 MET SELENOMETHIONINE
MODRES 2FS2 MSE A 38 MET SELENOMETHIONINE
MODRES 2FS2 MSE A 44 MET SELENOMETHIONINE
MODRES 2FS2 MSE B 12 MET SELENOMETHIONINE
MODRES 2FS2 MSE B 29 MET SELENOMETHIONINE
MODRES 2FS2 MSE B 38 MET SELENOMETHIONINE
MODRES 2FS2 MSE B 44 MET SELENOMETHIONINE
HET MSE A 12 8
HET MSE A 29 8
HET MSE A 38 8
HET MSE A 44 8
HET MSE B 12 8
HET MSE B 29 8
HET MSE B 38 8
HET MSE B 44 8
HET SO4 A 151 5
HET SO4 A 152 5
HET SO4 B 151 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 HOH *79(H2 O)
HELIX 1 1 SER A 0 GLY A 23 1 24
HELIX 2 2 THR A 41 LEU A 45 5 5
HELIX 3 3 HIS A 52 SER A 70 1 19
HELIX 4 4 SER B 0 ASN B 15 1 16
HELIX 5 5 ASP B 16 LEU B 22 1 7
HELIX 6 6 THR B 41 LEU B 45 5 5
HELIX 7 7 HIS B 52 SER B 70 1 19
SHEET 1 A12 ASP A 25 ASP A 30 0
SHEET 2 A12 PHE A 33 THR A 39 -1 O THR A 37 N ASP A 25
SHEET 3 A12 THR A 93 GLN A 103 -1 O LEU A 94 N MSE A 38
SHEET 4 A12 THR A 107 VAL A 115 -1 O VAL A 109 N ARG A 101
SHEET 5 A12 THR A 121 HIS A 130 -1 O PHE A 125 N ILE A 112
SHEET 6 A12 VAL A 76 PHE A 84 -1 N VAL A 76 O HIS A 130
SHEET 7 A12 ALA B 75 PHE B 84 -1 O ILE B 82 N CYS A 80
SHEET 8 A12 THR B 121 ARG B 131 -1 O LYS B 128 N ALA B 79
SHEET 9 A12 THR B 107 VAL B 115 -1 N TYR B 110 O GLY B 127
SHEET 10 A12 THR B 93 GLN B 103 -1 N ARG B 101 O VAL B 109
SHEET 11 A12 PHE B 33 THR B 39 -1 N ALA B 34 O ALA B 98
SHEET 12 A12 ASP B 25 ASP B 30 -1 N ASP B 30 O PHE B 33
LINK C ALA A 11 N MSE A 12 1555 1555 1.33
LINK C MSE A 12 N TYR A 13 1555 1555 1.36
LINK C SER A 28 N MSE A 29 1555 1555 1.31
LINK C MSE A 29 N ASP A 30 1555 1555 1.32
LINK C THR A 37 N MSE A 38 1555 1555 1.32
LINK C MSE A 38 N THR A 39 1555 1555 1.34
LINK C GLN A 43 N MSE A 44 1555 1555 1.33
LINK C MSE A 44 N LEU A 45 1555 1555 1.33
LINK C ALA B 11 N MSE B 12 1555 1555 1.34
LINK C MSE B 12 N TYR B 13 1555 1555 1.33
LINK C SER B 28 N MSE B 29 1555 1555 1.32
LINK C MSE B 29 N ASP B 30 1555 1555 1.30
LINK C THR B 37 N MSE B 38 1555 1555 1.31
LINK C MSE B 38 N THR B 39 1555 1555 1.31
LINK C GLN B 43 N MSE B 44 1555 1555 1.31
LINK C MSE B 44 N LEU B 45 1555 1555 1.34
SITE 1 AC1 4 GLY B 104 LYS B 105 GLN B 106 THR B 107
SITE 1 AC2 4 GLY A 104 LYS A 105 GLN A 106 THR A 107
SITE 1 AC3 4 ARG A 86 LYS A 120 THR A 121 HIS B 102
CRYST1 69.847 69.847 117.168 90.00 90.00 120.00 P 31 2 1 12
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 0.014317 0.008266 0.000000 0.00000
SCALE2 0.000000 0.016532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008535 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
