HEADER SIGNALING PROTEIN 26-AUG-10 3OLY
TITLE STRUCTURAL AND FUNCTIONAL EFFECTS OF SUBSTITUTION AT POSITION T+1 IN
TITLE 2 CHEY: CHEYA88M-BEF3-MN COMPLEX
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: K12;
SOURCE 5 GENE: CHEY;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K0641 RECA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRS3
KEYWDS ALPHA-BETA REPEAT, CHEMOTAXIS, TWO-COMPONENT SIGNALING, RESPONSE
KEYWDS 2 REGULATOR, CHEA, CHEZ, PHOSPHORYLATION, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.IMMORMINO,R.B.BOURRET
REVDAT 4 06-SEP-23 3OLY 1 REMARK SEQADV LINK
REVDAT 3 19-OCT-16 3OLY 1 JRNL
REVDAT 2 21-SEP-16 3OLY 1 JRNL
REVDAT 1 31-AUG-11 3OLY 0
JRNL AUTH R.M.IMMORMINO,R.E.SILVERSMITH,R.B.BOURRET
JRNL TITL A VARIABLE ACTIVE SITE RESIDUE INFLUENCES THE KINETICS OF
JRNL TITL 2 RESPONSE REGULATOR PHOSPHORYLATION AND DEPHOSPHORYLATION.
JRNL REF BIOCHEMISTRY V. 55 5595 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 27589219
JRNL DOI 10.1021/ACS.BIOCHEM.6B00645
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_336)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 28710
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.340
REMARK 3 FREE R VALUE TEST SET COUNT : 1534
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 26.7248 - 4.5523 0.99 2736 156 0.1560 0.1702
REMARK 3 2 4.5523 - 3.6162 1.00 2606 142 0.1277 0.1495
REMARK 3 3 3.6162 - 3.1599 1.00 2565 140 0.1632 0.1947
REMARK 3 4 3.1599 - 2.8713 0.99 2570 144 0.2086 0.2313
REMARK 3 5 2.8713 - 2.6657 0.98 2488 141 0.2155 0.2783
REMARK 3 6 2.6657 - 2.5087 0.98 2474 142 0.2147 0.2909
REMARK 3 7 2.5087 - 2.3831 0.96 2444 140 0.2159 0.2586
REMARK 3 8 2.3831 - 2.2795 0.95 2418 136 0.2139 0.2745
REMARK 3 9 2.2795 - 2.1917 0.93 2353 136 0.2247 0.2494
REMARK 3 10 2.1917 - 2.1161 0.91 2281 136 0.2434 0.2775
REMARK 3 11 2.1161 - 2.0500 0.89 2241 121 0.2828 0.3601
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 53.45
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.35
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.78440
REMARK 3 B22 (A**2) : 2.28320
REMARK 3 B33 (A**2) : 0.50120
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2093
REMARK 3 ANGLE : 1.063 2820
REMARK 3 CHIRALITY : 0.072 319
REMARK 3 PLANARITY : 0.004 363
REMARK 3 DIHEDRAL : 12.618 809
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3OLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : SAGITAL CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30464
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.67300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3MYY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE 2.4 M GLYCEROL 2.5%
REMARK 280 (V/V) TRIS 100 MM PH 8.0 MNCL2 20MM BECL2 1MM NAF 10MM 4.8 MG/ML
REMARK 280 CHEY A88M 1-10-10, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 26.72250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.54100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.77350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.54100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.72250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.77350
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 1
REMARK 465 MET B 1
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 GLU A 93 CG CD OE1 OE2
REMARK 470 GLU A 125 CG CD OE1 OE2
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 LEU A 6 128.15 -39.71
REMARK 500 TRP A 58 -66.31 -103.15
REMARK 500 ASN A 62 -60.93 74.28
REMARK 500 TRP B 58 -65.86 -106.36
REMARK 500 ASN B 62 -59.06 73.57
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 131 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 ASP A 57 OD2 86.3
REMARK 620 3 ASN A 59 O 86.5 90.9
REMARK 620 4 BEF A 130 F2 169.6 83.5 92.0
REMARK 620 5 HOH A 137 O 96.3 175.4 85.4 93.8
REMARK 620 6 HOH A 138 O 89.6 85.2 174.7 91.2 98.7
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 106.1
REMARK 620 3 BEF A 130 F2 102.9 115.4
REMARK 620 4 BEF A 130 F3 103.3 114.2 113.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 131 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 13 OD1
REMARK 620 2 ASP B 57 OD2 83.1
REMARK 620 3 ASN B 59 O 88.8 88.0
REMARK 620 4 BEF B 130 F2 165.4 82.6 94.1
REMARK 620 5 HOH B 139 O 103.4 173.2 90.3 91.0
REMARK 620 6 HOH B 142 O 84.5 83.7 169.9 90.6 98.6
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 111.0
REMARK 620 3 BEF B 130 F2 101.8 112.5
REMARK 620 4 BEF B 130 F3 104.0 114.5 111.9
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 BEF A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF B 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 134
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FQW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACTIVATED CHEY
REMARK 900 RELATED ID: 3OLV RELATED DB: PDB
REMARK 900 STRUCTURAL AND FUNCTIONAL EFFECTS OF SUBSTITUTION AT POSITION T+1
REMARK 900 IN CHEY: CHEYA88V-BEF3-MG COMPLEX
REMARK 900 RELATED ID: 3OLW RELATED DB: PDB
REMARK 900 STRUCTURAL AND FUNCTIONAL EFFECTS OF SUBSTITUTION AT POSITION T+1
REMARK 900 IN CHEY: CHEYA88T-BEF3-MG COMPLEX
REMARK 900 RELATED ID: 3OLX RELATED DB: PDB
REMARK 900 STRUCTURAL AND FUNCTIONAL EFFECTS OF SUBSTITUTION AT POSITION T+1
REMARK 900 IN CHEY: CHEYA88S-BEF3-MG COMPLEX
DBREF 3OLY A 1 129 UNP P0AE67 CHEY_ECOLI 1 129
DBREF 3OLY B 1 129 UNP P0AE67 CHEY_ECOLI 1 129
SEQADV 3OLY MET A 88 UNP P0AE67 ALA 88 ENGINEERED MUTATION
SEQADV 3OLY MET B 88 UNP P0AE67 ALA 88 ENGINEERED MUTATION
SEQRES 1 A 129 MET ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP
SEQRES 2 A 129 PHE SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS
SEQRES 3 A 129 GLU LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY
SEQRES 4 A 129 VAL ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY
SEQRES 5 A 129 PHE VAL ILE SER ASP TRP ASN MET PRO ASN MET ASP GLY
SEQRES 6 A 129 LEU GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET
SEQRES 7 A 129 SER ALA LEU PRO VAL LEU MET VAL THR MET GLU ALA LYS
SEQRES 8 A 129 LYS GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER
SEQRES 9 A 129 GLY TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU
SEQRES 10 A 129 GLU LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET
SEQRES 1 B 129 MET ALA ASP LYS GLU LEU LYS PHE LEU VAL VAL ASP ASP
SEQRES 2 B 129 PHE SER THR MET ARG ARG ILE VAL ARG ASN LEU LEU LYS
SEQRES 3 B 129 GLU LEU GLY PHE ASN ASN VAL GLU GLU ALA GLU ASP GLY
SEQRES 4 B 129 VAL ASP ALA LEU ASN LYS LEU GLN ALA GLY GLY TYR GLY
SEQRES 5 B 129 PHE VAL ILE SER ASP TRP ASN MET PRO ASN MET ASP GLY
SEQRES 6 B 129 LEU GLU LEU LEU LYS THR ILE ARG ALA ASP GLY ALA MET
SEQRES 7 B 129 SER ALA LEU PRO VAL LEU MET VAL THR MET GLU ALA LYS
SEQRES 8 B 129 LYS GLU ASN ILE ILE ALA ALA ALA GLN ALA GLY ALA SER
SEQRES 9 B 129 GLY TYR VAL VAL LYS PRO PHE THR ALA ALA THR LEU GLU
SEQRES 10 B 129 GLU LYS LEU ASN LYS ILE PHE GLU LYS LEU GLY MET
HET BEF A 130 4
HET MN A 131 1
HET GOL A 502 6
HET GOL A 503 6
HET GOL A 505 6
HET MN A 132 1
HET MN A 133 1
HET BEF B 130 4
HET MN B 131 1
HET GOL B 501 6
HET GOL B 504 6
HET MN B 132 1
HET MN B 133 1
HET SO4 B 134 5
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 BEF 2(BE F3 1-)
FORMUL 4 MN 6(MN 2+)
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 16 SO4 O4 S 2-
FORMUL 17 HOH *323(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 GLY A 128 1 17
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 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 VAL B 54
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 131 1555 1555 2.18
LINK OG ASER A 15 MN MN A 132 1555 1555 2.47
LINK OD1 ASP A 57 BE BEF A 130 1555 1555 1.73
LINK OD2 ASP A 57 MN MN A 131 1555 1555 2.06
LINK O ASN A 59 MN MN A 131 1555 1555 2.30
LINK F2 BEF A 130 MN MN A 131 1555 1555 2.19
LINK MN MN A 131 O HOH A 137 1555 1555 2.12
LINK MN MN A 131 O HOH A 138 1555 1555 2.34
LINK OD1 ASP B 13 MN MN B 131 1555 1555 2.25
LINK OD1 ASP B 57 BE BEF B 130 1555 1555 1.82
LINK OD2 ASP B 57 MN MN B 131 1555 1555 2.10
LINK O ASN B 59 MN MN B 131 1555 1555 2.25
LINK F2 BEF B 130 MN MN B 131 1555 1555 2.22
LINK MN MN B 131 O HOH B 139 1555 1555 2.17
LINK MN MN B 131 O HOH B 142 1555 1555 2.42
CISPEP 1 LYS A 109 PRO A 110 0 -5.63
CISPEP 2 LYS B 109 PRO B 110 0 -1.45
SITE 1 AC1 7 ASP A 57 TRP A 58 ASN A 59 THR A 87
SITE 2 AC1 7 MET A 88 LYS A 109 MN A 131
SITE 1 AC2 6 ASP A 13 ASP A 57 ASN A 59 BEF A 130
SITE 2 AC2 6 HOH A 137 HOH A 138
SITE 1 AC3 4 LYS A 7 ASN A 32 GLY A 50 HOH A 226
SITE 1 AC4 4 LYS A 91 LYS A 92 GLU A 93 HOH B 202
SITE 1 AC5 5 ARG A 19 LYS A 70 HOH A 157 HOH A 170
SITE 2 AC5 5 LYS B 126
SITE 1 AC6 1 SER A 15
SITE 1 AC7 1 GLY A 50
SITE 1 AC8 7 ASP B 57 TRP B 58 ASN B 59 THR B 87
SITE 2 AC8 7 MET B 88 LYS B 109 MN B 131
SITE 1 AC9 6 ASP B 13 ASP B 57 ASN B 59 BEF B 130
SITE 2 AC9 6 HOH B 139 HOH B 142
SITE 1 BC1 5 TRP B 58 ASN B 59 GLU B 89 ASN B 94
SITE 2 BC1 5 HOH B 312
SITE 1 BC2 4 LYS B 7 ASN B 32 GLY B 50 HOH B 284
SITE 1 BC3 1 SER B 15
SITE 1 BC4 2 LYS A 92 LYS B 92
SITE 1 BC5 6 ARG B 19 HOH B 175 HOH B 191 HOH B 223
SITE 2 BC5 6 HOH B 226 HOH B 287
CRYST1 53.445 53.547 161.082 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 0.018711 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018675 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006208 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
