HEADER HYDROLASE 17-JAN-12 4DCC
TITLE CRYSTAL STRUCTURE OF HAD FAMILY ENZYME BT-2542 FROM BACTEROIDES
TITLE 2 THETAIOTAOMICRON (TARGET EFI-501088)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HALOACID DEHALOGENASE-LIKE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 818;
SOURCE 4 GENE: BT_2542;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS HYDROLASE, MAGNESIUM BINDING SITE, ENZYME FUNCTION INITIATIVE,
KEYWDS 2 STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,R.TORO,R.BHOSLE,B.HILLERICH,R.D.SEIDEL,E.WASHINGTON,
AUTHOR 2 A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,W.D.ZENCHECK,H.J.IMKER,
AUTHOR 3 J.A.GERLT,K.N.ALLEN,D.DUNAWAY-MARIANO,S.C.ALMO,ENZYME FUNCTION
AUTHOR 4 INITIATIVE (EFI)
REVDAT 3 13-SEP-23 4DCC 1 REMARK SEQADV LINK
REVDAT 2 24-JAN-18 4DCC 1 AUTHOR
REVDAT 1 22-FEB-12 4DCC 0
JRNL AUTH Y.PATSKOVSKY,R.TORO,R.BHOSLE,B.HILLERICH,R.D.SEIDEL,
JRNL AUTH 2 E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,
JRNL AUTH 3 W.D.ZENCHECK,H.J.IMKER,K.N.ALLEN,D.DUNAWAY-MARIANO,
JRNL AUTH 4 J.A.GERLT,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF PROTEIN BT-2542 FROM BACTEROIDES
JRNL TITL 2 THETAIOTAOMICRON (TARGET EFI-501088)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 29399
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT : 962
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2115
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1656
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.70000
REMARK 3 B22 (A**2) : 3.15000
REMARK 3 B33 (A**2) : -2.44000
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): 0.088
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.164
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1755 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2365 ; 1.304 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 211 ; 5.380 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;37.288 ;24.651
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 329 ;13.704 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;11.440 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 252 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1323 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1042 ; 3.279 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1680 ; 4.845 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 713 ; 6.909 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 682 ;10.339 ; 7.000
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 : 1.40
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 4DCC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30924
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 70.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.90000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2I6X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM ACETATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 25.12600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.63500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.71200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.63500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.12600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.71200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.12600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.71200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 65.63500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.71200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.12600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.63500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 551 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 MET A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 SER A 3
REMARK 465 LYS A 207
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 4 CG CD CE NZ
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 ASN A 36 CG OD1 ND2
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 THR A 43 OG1 CG2
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 36 46.35 -96.12
REMARK 500 HIS A 44 -0.87 84.86
REMARK 500 MET A 74 55.13 -93.33
REMARK 500 VAL A 89 -78.84 -105.71
REMARK 500 ARG A 130 -128.04 55.21
REMARK 500 ARG A 130 -125.06 50.32
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 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 12 OD2
REMARK 620 2 GLY A 14 O 97.5
REMARK 620 3 ASP A 176 OD1 113.6 90.0
REMARK 620 4 HOH A 521 O 80.8 174.2 85.6
REMARK 620 5 HOH A 567 O 166.3 79.8 80.0 103.2
REMARK 620 6 HOH A 598 O 114.0 93.6 131.2 92.2 53.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 135 O
REMARK 620 2 PHE A 138 O 91.6
REMARK 620 3 HOH A 516 O 86.6 171.0
REMARK 620 4 HOH A 517 O 162.5 92.7 86.5
REMARK 620 5 HOH A 563 O 108.9 117.5 71.4 84.0
REMARK 620 6 HOH A 563 O 141.0 94.7 92.3 55.4 36.0
REMARK 620 7 HOH A 590 O 91.4 81.0 90.2 72.5 151.1 127.6
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EFI-501088 RELATED DB: TARGETTRACK
DBREF 4DCC A 1 207 UNP Q8A4Q5 Q8A4Q5_BACTN 1 207
SEQADV 4DCC MET A -21 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC HIS A -20 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC HIS A -19 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC HIS A -18 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC HIS A -17 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC HIS A -16 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC HIS A -15 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC SER A -14 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC SER A -13 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC GLY A -12 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC VAL A -11 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC ASP A -10 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC LEU A -9 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC GLY A -8 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC THR A -7 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC GLU A -6 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC ASN A -5 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC LEU A -4 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC TYR A -3 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC PHE A -2 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC GLN A -1 UNP Q8A4Q5 EXPRESSION TAG
SEQADV 4DCC SER A 0 UNP Q8A4Q5 EXPRESSION TAG
SEQRES 1 A 229 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 229 GLY THR GLU ASN LEU TYR PHE GLN SER MET LYS SER LYS
SEQRES 3 A 229 GLY ILE LYS ASN LEU LEU ILE ASP LEU GLY GLY VAL LEU
SEQRES 4 A 229 ILE ASN LEU ASP ARG GLU ARG CYS ILE GLU ASN PHE LYS
SEQRES 5 A 229 LYS ILE GLY PHE GLN ASN ILE GLU GLU LYS PHE CYS THR
SEQRES 6 A 229 HIS GLN LEU ASP GLY ILE PHE LEU GLN GLN GLU LYS GLY
SEQRES 7 A 229 LEU ILE THR PRO ALA GLU PHE ARG ASP GLY ILE ARG GLU
SEQRES 8 A 229 MET MET GLY LYS MET VAL SER ASP LYS GLN ILE ASP ALA
SEQRES 9 A 229 ALA TRP ASN SER PHE LEU VAL ASP ILE PRO THR TYR LYS
SEQRES 10 A 229 LEU ASP LEU LEU LEU LYS LEU ARG GLU LYS TYR VAL VAL
SEQRES 11 A 229 TYR LEU LEU SER ASN THR ASN ASP ILE HIS TRP LYS TRP
SEQRES 12 A 229 VAL CYS LYS ASN ALA PHE PRO TYR ARG THR PHE LYS VAL
SEQRES 13 A 229 GLU ASP TYR PHE GLU LYS THR TYR LEU SER TYR GLU MET
SEQRES 14 A 229 LYS MET ALA LYS PRO GLU PRO GLU ILE PHE LYS ALA VAL
SEQRES 15 A 229 THR GLU ASP ALA GLY ILE ASP PRO LYS GLU THR PHE PHE
SEQRES 16 A 229 ILE ASP ASP SER GLU ILE ASN CYS LYS VAL ALA GLN GLU
SEQRES 17 A 229 LEU GLY ILE SER THR TYR THR PRO LYS ALA GLY GLU ASP
SEQRES 18 A 229 TRP SER HIS LEU PHE ARG LYS LYS
HET CL A 301 1
HET NA A 302 1
HET NA A 303 1
HET UNL A 304 8
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM UNL UNKNOWN LIGAND
FORMUL 2 CL CL 1-
FORMUL 3 NA 2(NA 1+)
FORMUL 6 HOH *203(H2 O)
HELIX 1 1 ASP A 21 GLY A 33 1 13
HELIX 2 2 ASN A 36 HIS A 44 1 9
HELIX 3 3 HIS A 44 LYS A 55 1 12
HELIX 4 4 THR A 59 GLY A 72 1 14
HELIX 5 5 SER A 76 SER A 86 1 11
HELIX 6 6 PRO A 92 ARG A 103 1 12
HELIX 7 7 ASN A 115 ALA A 126 1 12
HELIX 8 8 LYS A 133 PHE A 138 1 6
HELIX 9 9 SER A 144 LYS A 148 1 5
HELIX 10 10 GLU A 153 GLY A 165 1 13
HELIX 11 11 ASP A 167 LYS A 169 5 3
HELIX 12 12 SER A 177 LEU A 187 1 11
HELIX 13 13 ASP A 199 ARG A 205 5 7
SHEET 1 A 5 LYS A 140 LEU A 143 0
SHEET 2 A 5 VAL A 107 SER A 112 1 N LEU A 110 O TYR A 142
SHEET 3 A 5 ASN A 8 ILE A 11 1 N LEU A 9 O TYR A 109
SHEET 4 A 5 THR A 171 ILE A 174 1 O PHE A 172 N LEU A 10
SHEET 5 A 5 SER A 190 TYR A 192 1 O SER A 190 N PHE A 173
LINK OD2 ASP A 12 NA NA A 302 1555 1555 2.16
LINK O GLY A 14 NA NA A 302 1555 1555 2.36
LINK O GLU A 135 NA NA A 303 1555 1555 2.22
LINK O PHE A 138 NA NA A 303 1555 1555 2.38
LINK OD1 ASP A 176 NA NA A 302 1555 1555 2.22
LINK NA NA A 302 O HOH A 521 1555 1555 2.31
LINK NA NA A 302 O HOH A 567 1555 1555 2.85
LINK NA NA A 302 O HOH A 598 1555 1555 2.46
LINK NA NA A 303 O HOH A 516 1555 1555 2.45
LINK NA NA A 303 O HOH A 517 1555 1555 2.55
LINK NA NA A 303 O BHOH A 563 1555 1555 2.42
LINK NA NA A 303 O AHOH A 563 1555 1555 2.87
LINK NA NA A 303 O HOH A 590 1555 1555 2.83
CISPEP 1 LYS A 151 PRO A 152 0 8.25
SITE 1 AC1 6 ASP A 12 LEU A 13 GLY A 14 SER A 112
SITE 2 AC1 6 ASN A 113 HOH A 583
SITE 1 AC2 6 ASP A 12 GLY A 14 ASP A 176 HOH A 521
SITE 2 AC2 6 HOH A 567 HOH A 598
SITE 1 AC3 6 GLU A 135 PHE A 138 HOH A 516 HOH A 517
SITE 2 AC3 6 HOH A 563 HOH A 590
CRYST1 50.252 75.424 131.270 90.00 90.00 90.00 I 21 21 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 0.019900 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013258 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007618 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
