HEADER SIGNALING PROTEIN 10-JUN-00 1F4V
TITLE CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS CHEY PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FLAGELLAR MOTOR SWITCH PROTEIN;
COMPND 7 CHAIN: D, E, F;
COMPND 8 FRAGMENT: N-TERMINUS;
COMPND 9 SYNONYM: FLIM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET21;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 10 ORGANISM_TAXID: 562
KEYWDS RESPONSE REGULATOR, PEPTIDE-PROTEIN COMPLEX, BACTERIAL SIGNAL
KEYWDS 2 TRANSDUCTION, BEF3, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Y.LEE,H.S.CHO,J.G.PELTON,D.YAN,R.K.HENDERSON,D.KING,L.S.HUANG,
AUTHOR 2 S.KUSTU,E.A.BERRY,D.E.WEMMER
REVDAT 7 07-FEB-24 1F4V 1 REMARK LINK
REVDAT 6 18-APR-18 1F4V 1 REMARK
REVDAT 5 13-JUL-11 1F4V 1 VERSN
REVDAT 4 24-FEB-09 1F4V 1 VERSN
REVDAT 3 01-APR-03 1F4V 1 JRNL
REVDAT 2 24-OCT-01 1F4V 1 CRYST1 REMARK
REVDAT 1 17-JAN-01 1F4V 0
JRNL AUTH S.Y.LEE,H.S.CHO,J.G.PELTON,D.YAN,R.K.HENDERSON,D.S.KING,
JRNL AUTH 2 L.HUANG,S.KUSTU,E.A.BERRY,D.E.WEMMER
JRNL TITL CRYSTAL STRUCTURE OF AN ACTIVATED RESPONSE REGULATOR BOUND
JRNL TITL 2 TO ITS TARGET.
JRNL REF NAT.STRUCT.BIOL. V. 8 52 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11135671
JRNL DOI 10.1038/83053
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.S.CHO,S.Y.LEE,D.YAN,X.PAN,J.S.PARKINSON,S.KUSTU,
REMARK 1 AUTH 2 D.E.WEMMER,J.G.PELTON
REMARK 1 TITL NMR STRUCTURE OF ACTIVATED CHEY
REMARK 1 REF J.MOL.BIOL. V. 297 543 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.3595
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.YAN,H.S.CHO,C.A.HASTINGS,M.M.IGO,S.Y.LEE,J.G.PELTON,
REMARK 1 AUTH 2 V.STEWART,D.E.WEMMER,S.KUSTU
REMARK 1 TITL BERYLLOFLUORIDE MIMICS PHOSPHORYLATION OF NTRC AND OTHER
REMARK 1 TITL 2 BACTERIAL RESPONSE REGULATORS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 96 14789 1999
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.96.26.14789
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.VOLZ,P.MATSUMURA
REMARK 1 TITL CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-A
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 266 15511 1991
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1216673.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 28623
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 SET) : 0.217
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1442
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4087
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 231
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.28000
REMARK 3 B12 (A**2) : 1.96000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.840
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.710 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.270 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.050 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : CONSTR
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : GOL_PAR
REMARK 3 PARAMETER FILE 3 : SO4_PAR
REMARK 3 PARAMETER FILE 4 : PARAM19.RCV
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F4V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011245.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-99; 06-JAN-00; NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100; 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y; Y
REMARK 200 RADIATION SOURCE : ALS; SSRL; SSRL; SSRL
REMARK 200 BEAMLINE : 5.0.2; BL1-5; BL1-5; BL1-5
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL; NULL; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2; 0.9799; 0.9796; 0.9253
REMARK 200 MONOCHROMATOR : NULL; NULL; NULL; NULL
REMARK 200 OPTICS : NULL; NULL; NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE; NULL;
REMARK 200 NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; FUJI; NULL; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28982
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 24.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.31800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, GLYCEROL, TRIS, PH
REMARK 280 8.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500009 -0.866009 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866041 -0.499991 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 231.62200
REMARK 290 SMTRY1 3 -0.499991 0.866009 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866041 -0.500009 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 115.81100
REMARK 290 SMTRY1 4 -0.500009 0.865999 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866041 0.500009 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 115.81100
REMARK 290 SMTRY1 6 -0.499991 -0.866020 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866041 0.499991 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 231.62200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 1610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: 3
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: 1490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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 GLY C 128
REMARK 465 MET C 129
REMARK 465 MET E 1
REMARK 465 GLY E 2
REMARK 465 MET F 1
REMARK 465 GLY F 2
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 O HOH A 311 O HOH A 418 1.92
REMARK 500 O HOH A 318 O HOH A 436 2.01
REMARK 500 O ASP C 57 O HOH C 304 2.02
REMARK 500 O ASP A 57 O HOH A 312 2.06
REMARK 500 O HOH A 309 O HOH A 437 2.08
REMARK 500 O HOH A 368 O HOH A 385 2.13
REMARK 500 O HOH A 378 O HOH D 21 2.14
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 B 387 O HOH D 28 6765 2.14
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 TRP A 58 -64.90 -103.88
REMARK 500 ASN A 62 -48.44 68.72
REMARK 500 MET A 63 117.80 -167.27
REMARK 500 ALA A 90 13.29 -140.13
REMARK 500 TRP B 58 -70.22 -104.87
REMARK 500 ASN B 62 -30.06 68.23
REMARK 500 MET B 63 112.99 -173.04
REMARK 500 SER B 79 -37.07 -27.46
REMARK 500 ASP C 3 113.74 -36.36
REMARK 500 LYS C 4 -10.84 88.98
REMARK 500 LEU C 9 71.96 -156.39
REMARK 500 GLU C 34 -159.75 -92.08
REMARK 500 ALA C 36 142.09 -175.83
REMARK 500 TRP C 58 -70.22 -101.65
REMARK 500 ASN C 59 97.45 -68.07
REMARK 500 ASN C 62 -29.99 71.69
REMARK 500 MET C 63 113.17 -175.92
REMARK 500 PRO C 82 107.84 -56.78
REMARK 500 LYS C 126 -1.53 -58.12
REMARK 500 SER E 4 -169.19 -108.04
REMARK 500 SER F 4 81.01 62.88
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 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD2
REMARK 620 2 ASP A 13 OD1 45.1
REMARK 620 3 ASP A 57 OD2 123.4 83.5
REMARK 620 4 ASN A 59 O 78.1 88.2 78.6
REMARK 620 5 BEF A 130 F1 155.3 153.3 69.8 85.3
REMARK 620 6 HOH A 416 O 114.5 88.5 78.4 157.0 87.6
REMARK 620 7 HOH A 428 O 69.5 112.6 162.1 93.6 93.7 108.7
REMARK 620 N 1 2 3 4 5 6
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 112.5
REMARK 620 3 BEF A 130 F2 107.2 109.0
REMARK 620 4 BEF A 130 F3 110.4 108.2 109.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 13 OD1
REMARK 620 2 ASP B 57 OD2 82.0
REMARK 620 3 ASN B 59 O 79.9 69.4
REMARK 620 4 BEF B 130 F1 149.5 72.9 75.4
REMARK 620 5 HOH B 324 O 99.8 94.3 163.6 98.9
REMARK 620 6 HOH B 331 O 100.3 148.5 80.0 92.7 115.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF B 130 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 57 OD1
REMARK 620 2 BEF B 130 F1 113.9
REMARK 620 3 BEF B 130 F2 107.4 107.3
REMARK 620 4 BEF B 130 F3 109.5 108.4 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 13 OD2
REMARK 620 2 ASP C 13 OD1 49.7
REMARK 620 3 ASN C 59 O 83.0 61.1
REMARK 620 4 BEF C 130 F1 151.6 104.1 72.7
REMARK 620 5 HOH C 310 O 105.5 76.3 114.7 72.8
REMARK 620 6 HOH C 333 O 128.8 170.5 110.0 74.8 111.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF C 130 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 57 OD1
REMARK 620 2 BEF C 130 F1 111.3
REMARK 620 3 BEF C 130 F2 108.4 109.0
REMARK 620 4 BEF C 130 F3 109.5 108.9 109.7
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 MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF B 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF C 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DJM RELATED DB: PDB
REMARK 900 BEF3-ACTIVATED CHEY
REMARK 900 RELATED ID: 3CHY RELATED DB: PDB
REMARK 900 RELATED ID: 1FQW RELATED DB: PDB
DBREF 1F4V A 2 129 UNP P06143 CHEY_ECOLI 1 128
DBREF 1F4V B 2 129 UNP P06143 CHEY_ECOLI 1 128
DBREF 1F4V C 2 129 UNP P06143 CHEY_ECOLI 1 128
DBREF 1F4V D 1 16 UNP P06974 FLIM_ECOLI 1 16
DBREF 1F4V E 1 16 UNP P06974 FLIM_ECOLI 1 16
DBREF 1F4V F 1 16 UNP P06974 FLIM_ECOLI 1 16
SEQRES 1 A 128 ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP PHE
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 ASN 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 GLU 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 PHE
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 ASN 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 GLU 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
SEQRES 1 C 128 ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP PHE
SEQRES 2 C 128 SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS GLU
SEQRES 3 C 128 LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY VAL
SEQRES 4 C 128 ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY PHE
SEQRES 5 C 128 VAL ILE SER ASP TRP ASN MET PRO ASN MET ASP GLY LEU
SEQRES 6 C 128 GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET SER
SEQRES 7 C 128 ALA LEU PRO VAL LEU MET VAL THR ALA GLU ALA LYS LYS
SEQRES 8 C 128 GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER GLY
SEQRES 9 C 128 TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU GLU
SEQRES 10 C 128 LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET
SEQRES 1 D 16 MET GLY ASP SER ILE LEU SER GLN ALA GLU ILE ASP ALA
SEQRES 2 D 16 LEU LEU ASN
SEQRES 1 E 16 MET GLY ASP SER ILE LEU SER GLN ALA GLU ILE ASP ALA
SEQRES 2 E 16 LEU LEU ASN
SEQRES 1 F 16 MET GLY ASP SER ILE LEU SER GLN ALA GLU ILE ASP ALA
SEQRES 2 F 16 LEU LEU ASN
HET MG A 301 1
HET BEF A 130 4
HET GOL A 304 6
HET MG B 302 1
HET BEF B 130 4
HET GOL B 305 6
HET MG C 303 1
HET BEF C 130 4
HETNAM MG MAGNESIUM ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 MG 3(MG 2+)
FORMUL 8 BEF 3(BE F3 1-)
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 15 HOH *280(H2 O)
HELIX 1 1 PHE A 14 GLY A 29 1 16
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 MET A 129 1 18
HELIX 6 6 PHE B 14 GLY B 29 1 16
HELIX 7 7 ASP B 38 ALA B 48 1 11
HELIX 8 8 ASP B 64 ALA B 74 1 11
HELIX 9 9 LYS B 91 GLY B 102 1 12
HELIX 10 10 THR B 112 LEU B 127 1 16
HELIX 11 11 PHE C 14 GLY C 29 1 16
HELIX 12 12 ASP C 38 GLY C 49 1 12
HELIX 13 13 ASP C 64 ASP C 75 1 12
HELIX 14 14 LYS C 91 ALA C 101 1 11
HELIX 15 15 THR C 112 LYS C 126 1 15
HELIX 16 16 SER D 7 ASN D 16 1 10
HELIX 17 17 SER E 7 ASN E 16 1 10
HELIX 18 18 SER F 7 ASN F 16 1 10
SHEET 1 A 5 VAL A 33 ALA A 36 0
SHEET 2 A 5 PHE A 8 VAL A 11 1 O PHE A 8 N GLU A 34
SHEET 3 A 5 PHE A 53 SER A 56 1 O PHE A 53 N LEU A 9
SHEET 4 A 5 VAL A 83 THR A 87 1 N LEU A 84 O VAL A 54
SHEET 5 A 5 GLY A 105 VAL A 108 1 O GLY A 105 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 O PHE B 8 N GLU B 34
SHEET 3 B 5 PHE B 53 SER B 56 1 O PHE B 53 N LEU B 9
SHEET 4 B 5 VAL B 83 THR B 87 1 N LEU B 84 O VAL B 54
SHEET 5 B 5 GLY B 105 VAL B 108 1 O GLY B 105 N MET B 85
SHEET 1 C 2 PHE C 8 LEU C 9 0
SHEET 2 C 2 VAL C 33 GLU C 34 1 N GLU C 34 O PHE C 8
SHEET 1 D 3 VAL C 54 SER C 56 0
SHEET 2 D 3 VAL C 83 THR C 87 1 N LEU C 84 O VAL C 54
SHEET 3 D 3 GLY C 105 VAL C 108 1 O GLY C 105 N MET C 85
LINK OD2 ASP A 13 MG MG B 302 1555 1555 3.11
LINK OD1 ASP A 13 MG MG B 302 1555 1555 2.16
LINK OD1 ASP A 57 BE BEF A 130 1555 1555 1.54
LINK OD2 ASP A 57 MG MG B 302 1555 1555 2.17
LINK O ASN A 59 MG MG B 302 1555 1555 2.28
LINK F1 BEF A 130 MG MG B 302 1555 1555 2.27
LINK MG MG A 301 OD1 ASP B 13 1555 1555 2.10
LINK MG MG A 301 OD2 ASP B 57 1555 1555 2.20
LINK MG MG A 301 O ASN B 59 1555 1555 2.47
LINK MG MG A 301 F1 BEF B 130 1555 1555 2.29
LINK MG MG A 301 O HOH B 324 1555 1555 2.17
LINK MG MG A 301 O HOH B 331 1555 1555 2.18
LINK O HOH A 416 MG MG B 302 1555 1555 2.30
LINK O HOH A 428 MG MG B 302 1555 1555 2.21
LINK OD1 ASP B 57 BE BEF B 130 1555 1555 1.55
LINK OD2 ASP C 13 MG MG C 303 1555 1555 2.72
LINK OD1 ASP C 13 MG MG C 303 1555 1555 2.52
LINK OD1 ASP C 57 BE BEF C 130 1555 1555 1.51
LINK O ASN C 59 MG MG C 303 1555 1555 2.78
LINK F1 BEF C 130 MG MG C 303 1555 1555 2.54
LINK MG MG C 303 O HOH C 310 1555 1555 3.00
LINK MG MG C 303 O HOH C 333 1555 1555 2.52
CISPEP 1 LYS A 109 PRO A 110 0 -0.61
CISPEP 2 LYS B 109 PRO B 110 0 0.11
CISPEP 3 LYS C 109 PRO C 110 0 -1.02
SITE 1 AC1 7 ASP B 12 ASP B 13 ASP B 57 ASN B 59
SITE 2 AC1 7 BEF B 130 HOH B 324 HOH B 331
SITE 1 AC2 6 ASP A 13 ASP A 57 ASN A 59 BEF A 130
SITE 2 AC2 6 HOH A 416 HOH A 428
SITE 1 AC3 7 ASP C 13 PHE C 14 ASP C 57 ASN C 59
SITE 2 AC3 7 BEF C 130 HOH C 310 HOH C 333
SITE 1 AC4 8 ASP A 57 TRP A 58 ASN A 59 THR A 87
SITE 2 AC4 8 ALA A 88 LYS A 109 HOH A 383 MG B 302
SITE 1 AC5 10 LYS A 92 MET A 129 MG A 301 ASP B 57
SITE 2 AC5 10 TRP B 58 ASN B 59 THR B 87 ALA B 88
SITE 3 AC5 10 LYS B 109 HOH B 313
SITE 1 AC6 8 ASP C 57 TRP C 58 ASN C 59 THR C 87
SITE 2 AC6 8 ALA C 88 LYS C 109 MG C 303 HOH C 333
SITE 1 AC7 4 ARG A 19 LYS A 70 HOH A 391 HOH A 406
SITE 1 AC8 6 SER A 79 HOH A 340 ARG B 19 ARG B 22
SITE 2 AC8 6 HOH B 325 HOH B 389
CRYST1 54.232 54.233 347.433 90.00 90.00 120.00 P 32 2 1 18
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 0.018439 0.010633 -0.000003 0.00000
SCALE2 0.000000 0.021285 -0.000003 0.00000
SCALE3 0.000000 0.000000 0.002878 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
