HEADER SIGNALING PROTEIN 04-DEC-08 3FFW
TITLE CRYSTAL STRUCTURE OF CHEY TRIPLE MUTANT F14Q, N59K, E89Y COMPLEXED
TITLE 2 WITH BEF3- AND MN2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS PROTEIN CHEY;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: B1882, CHEY, JW1871;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: KO641RECA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS RESPONSE REGULATOR, RECEIVER DOMAIN, BEF3, TWO-COMPONENT SIGNAL
KEYWDS 2 TRANSDUCTION, CHEMOTAXIS, FLAGELLAR ROTATION, MAGNESIUM, METAL-
KEYWDS 3 BINDING, PHOSPHOPROTEIN, TWO-COMPONENT REGULATORY SYSTEM, SIGNALING
KEYWDS 4 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PAZY,E.J.COLLINS,R.B.BOURRET
REVDAT 5 21-FEB-24 3FFW 1 REMARK
REVDAT 4 20-OCT-21 3FFW 1 REMARK SEQADV LINK
REVDAT 3 01-NOV-17 3FFW 1 REMARK
REVDAT 2 13-JUL-11 3FFW 1 VERSN
REVDAT 1 22-SEP-09 3FFW 0
JRNL AUTH Y.PAZY,A.C.WOLLISH,S.A.THOMAS,P.J.MILLER,E.J.COLLINS,
JRNL AUTH 2 R.B.BOURRET,R.E.SILVERSMITH
JRNL TITL MATCHING BIOCHEMICAL REACTION KINETICS TO THE TIMESCALES OF
JRNL TITL 2 LIFE: STRUCTURAL DETERMINANTS THAT INFLUENCE THE
JRNL TITL 3 AUTODEPHOSPHORYLATION RATE OF RESPONSE REGULATOR PROTEINS.
JRNL REF J.MOL.BIOL. V. 392 1205 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19646451
JRNL DOI 10.1016/J.JMB.2009.07.064
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 31360
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1593
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) : 2164
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 388
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : -0.65000
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): 0.116
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.594
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2073 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1400 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2791 ; 1.470 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3454 ; 0.979 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 266 ; 5.732 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;40.968 ;26.047
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 392 ;13.383 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ; 6.318 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 314 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2294 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 376 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 403 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1515 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1010 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1068 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 286 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.017 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.129 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 42 ; 0.274 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.252 ; 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): 1709 ; 1.002 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 536 ; 0.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2080 ; 1.168 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 891 ; 2.281 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 711 ; 3.191 ; 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 : 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 3FFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050540.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.4
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
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 : 31409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 27.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4540
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.33300
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS BUFFER, AMMONIUM SULFATE,
REMARK 280 GLYCEROL, BECL2, NAF, MNCL2, PH 8.4, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 26.74550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.78400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.77150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.78400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.74550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.77150
REMARK 290 SMTRY3 4 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ND2 ASN B 94 O HOH B 338 1.99
REMARK 500 O4 SO4 A 1 O HOH A 350 2.17
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 O HOH A 253 O HOH A 273 3554 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 ASP A 12 143.35 -170.14
REMARK 500 TRP A 58 -68.63 -104.71
REMARK 500 ASN A 62 -56.23 75.48
REMARK 500 MET A 78 26.33 -144.06
REMARK 500 TRP B 58 -66.12 -106.81
REMARK 500 ASN B 62 -56.23 78.41
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 MN A 202 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 ASP A 57 OD2 83.9
REMARK 620 3 LYS A 59 O 88.2 87.0
REMARK 620 4 BEF A 130 F1 165.3 81.4 92.4
REMARK 620 5 HOH A 257 O 84.7 83.8 168.9 92.3
REMARK 620 6 HOH A 347 O 98.8 177.1 92.1 95.9 97.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF A 130 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 BEF A 130 F1 110.8
REMARK 620 3 BEF A 130 F2 107.6 110.2
REMARK 620 4 BEF A 130 F3 110.1 108.8 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 202 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 13 OD1
REMARK 620 2 ASP B 57 OD2 85.9
REMARK 620 3 LYS B 59 O 88.6 85.6
REMARK 620 4 BEF B 131 F1 165.1 79.3 91.3
REMARK 620 5 HOH B 280 O 87.9 86.3 171.4 90.0
REMARK 620 6 HOH B 346 O 98.5 174.9 91.7 96.4 96.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF B 131 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 57 OD1
REMARK 620 2 BEF B 131 F1 112.1
REMARK 620 3 BEF B 131 F2 106.9 110.2
REMARK 620 4 BEF B 131 F3 109.6 108.9 109.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF B 131
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F7N RELATED DB: PDB
REMARK 900 RELATED ID: 3FFT RELATED DB: PDB
REMARK 900 RELATED ID: 3FFX RELATED DB: PDB
DBREF 3FFW A 2 129 UNP P0AE67 CHEY_ECOLI 2 129
DBREF 3FFW B 2 129 UNP P0AE67 CHEY_ECOLI 2 129
SEQADV 3FFW GLN A 14 UNP P0AE67 PHE 14 ENGINEERED MUTATION
SEQADV 3FFW LYS A 59 UNP P0AE67 ASN 59 ENGINEERED MUTATION
SEQADV 3FFW TYR A 89 UNP P0AE67 GLU 89 ENGINEERED MUTATION
SEQADV 3FFW GLN B 14 UNP P0AE67 PHE 14 ENGINEERED MUTATION
SEQADV 3FFW LYS B 59 UNP P0AE67 ASN 59 ENGINEERED MUTATION
SEQADV 3FFW TYR B 89 UNP P0AE67 GLU 89 ENGINEERED MUTATION
SEQRES 1 A 128 ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP GLN
SEQRES 2 A 128 SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS GLU
SEQRES 3 A 128 LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY VAL
SEQRES 4 A 128 ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY PHE
SEQRES 5 A 128 VAL ILE SER ASP TRP LYS MET PRO ASN MET ASP GLY LEU
SEQRES 6 A 128 GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET SER
SEQRES 7 A 128 ALA LEU PRO VAL LEU MET VAL THR ALA TYR ALA LYS LYS
SEQRES 8 A 128 GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER GLY
SEQRES 9 A 128 TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU GLU
SEQRES 10 A 128 LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET
SEQRES 1 B 128 ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP GLN
SEQRES 2 B 128 SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS GLU
SEQRES 3 B 128 LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY VAL
SEQRES 4 B 128 ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY PHE
SEQRES 5 B 128 VAL ILE SER ASP TRP LYS MET PRO ASN MET ASP GLY LEU
SEQRES 6 B 128 GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET SER
SEQRES 7 B 128 ALA LEU PRO VAL LEU MET VAL THR ALA TYR ALA LYS LYS
SEQRES 8 B 128 GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER GLY
SEQRES 9 B 128 TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU GLU
SEQRES 10 B 128 LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET
HET MN A 202 1
HET BEF A 130 4
HET GOL A 501 6
HET SO4 A 1 5
HET GOL B 502 6
HET GOL B 503 6
HET SO4 B 130 5
HET MN B 202 1
HET BEF B 131 4
HETNAM MN MANGANESE (II) ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MN 2(MN 2+)
FORMUL 4 BEF 2(BE F3 1-)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 12 HOH *388(H2 O)
HELIX 1 1 GLN A 14 LEU A 28 1 15
HELIX 2 2 ASP A 38 ALA A 48 1 11
HELIX 3 3 ASP A 64 ASP A 75 1 12
HELIX 4 4 LYS A 91 ALA A 101 1 11
HELIX 5 5 THR A 112 GLY A 128 1 17
HELIX 6 6 GLN B 14 LEU B 28 1 15
HELIX 7 7 ASP B 38 ALA B 48 1 11
HELIX 8 8 ASP B 64 ASP B 75 1 12
HELIX 9 9 LYS B 91 ALA B 101 1 11
HELIX 10 10 THR B 112 LEU B 127 1 16
SHEET 1 A 5 VAL A 33 ALA A 36 0
SHEET 2 A 5 PHE A 8 VAL A 11 1 N VAL A 10 O GLU A 34
SHEET 3 A 5 PHE A 53 SER A 56 1 O ILE A 55 N VAL A 11
SHEET 4 A 5 VAL A 83 THR A 87 1 O LEU A 84 N SER A 56
SHEET 5 A 5 GLY A 105 VAL A 108 1 O VAL A 107 N MET A 85
SHEET 1 B 5 VAL B 33 ALA B 36 0
SHEET 2 B 5 PHE B 8 VAL B 11 1 N VAL B 10 O GLU B 34
SHEET 3 B 5 PHE B 53 SER B 56 1 O ILE B 55 N VAL B 11
SHEET 4 B 5 VAL B 83 THR B 87 1 O LEU B 84 N SER B 56
SHEET 5 B 5 GLY B 105 VAL B 108 1 O VAL B 107 N THR B 87
LINK OD1 ASP A 13 MN MN A 202 1555 1555 2.15
LINK OD1 ASP A 57 BE BEF A 130 1555 1555 1.50
LINK OD2 ASP A 57 MN MN A 202 1555 1555 2.08
LINK O LYS A 59 MN MN A 202 1555 1555 2.20
LINK F1 BEF A 130 MN MN A 202 1555 1555 2.01
LINK MN MN A 202 O HOH A 257 1555 1555 2.28
LINK MN MN A 202 O HOH A 347 1555 1555 2.04
LINK OD1 ASP B 13 MN MN B 202 1555 1555 2.21
LINK OD1 ASP B 57 BE BEF B 131 1555 1555 1.50
LINK OD2 ASP B 57 MN MN B 202 1555 1555 2.13
LINK O LYS B 59 MN MN B 202 1555 1555 2.24
LINK F1 BEF B 131 MN MN B 202 1555 1555 2.02
LINK MN MN B 202 O HOH B 280 1555 1555 2.33
LINK MN MN B 202 O HOH B 346 1555 1555 2.11
CISPEP 1 LYS A 109 PRO A 110 0 -3.69
CISPEP 2 LYS B 109 PRO B 110 0 -5.87
SITE 1 AC1 6 ASP A 13 ASP A 57 LYS A 59 BEF A 130
SITE 2 AC1 6 HOH A 257 HOH A 347
SITE 1 AC2 11 ASP A 57 TRP A 58 LYS A 59 THR A 87
SITE 2 AC2 11 ALA A 88 LYS A 109 HOH A 164 MN A 202
SITE 3 AC2 11 HOH A 252 HOH A 257 HOH A 347
SITE 1 AC3 5 ARG A 19 LYS A 70 HOH A 292 HOH A 316
SITE 2 AC3 5 LYS B 126
SITE 1 AC4 4 LYS A 91 LYS A 92 HOH A 315 HOH A 350
SITE 1 AC5 5 ARG B 19 LYS B 70 HOH B 171 HOH B 205
SITE 2 AC5 5 HOH B 271
SITE 1 AC6 5 LYS B 7 ASN B 32 GLY B 50 HOH B 181
SITE 2 AC6 5 HOH B 378
SITE 1 AC7 6 LYS A 92 LYS B 91 LYS B 92 GLU B 93
SITE 2 AC7 6 HOH B 194 HOH B 197
SITE 1 AC8 6 ASP B 13 ASP B 57 LYS B 59 BEF B 131
SITE 2 AC8 6 HOH B 280 HOH B 346
SITE 1 AC9 11 ASP B 57 TRP B 58 LYS B 59 THR B 87
SITE 2 AC9 11 ALA B 88 LYS B 109 MN B 202 HOH B 246
SITE 3 AC9 11 HOH B 280 HOH B 341 HOH B 346
CRYST1 53.491 53.543 161.568 90.00 90.00 90.00 P 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 0.018695 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006189 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
