HEADER SIGNALING PROTEIN 06-MAY-11 3RVN
TITLE STRUCTURE OF THE CHEY-BEF3 COMPLEX WITH SUBSTITUTIONS AT 59 AND 89:
TITLE 2 N59D AND E89Y
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: B1882, CHEY, JW1871;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23ACHEYN59DE89Y
KEYWDS RESPONSE REGULATOR, TWO-COMPONENT, SIGNAL TRANSDUCTION, CHEY, BETA-
KEYWDS 2 ALPHA PROTEIN, CHEMOTAXIS, CHEA CHEZ CHEX, PHOSPHORYLATION,
KEYWDS 3 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.STARBIRD,R.M.IMMORMINO,R.E.SILVERSMITH,R.B.BOURRET
REVDAT 3 13-SEP-23 3RVN 1 REMARK SEQADV
REVDAT 2 21-SEP-16 3RVN 1 JRNL
REVDAT 1 09-MAY-12 3RVN 0
JRNL AUTH R.M.IMMORMINO,C.A.STARBIRD,R.E.SILVERSMITH,R.B.BOURRET
JRNL TITL PROBING MECHANISTIC SIMILARITIES BETWEEN RESPONSE REGULATOR
JRNL TITL 2 SIGNALING PROTEINS AND HALOACID DEHALOGENASE PHOSPHATASES.
JRNL REF BIOCHEMISTRY V. 54 3514 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 25928369
JRNL DOI 10.1021/ACS.BIOCHEM.5B00286
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 21750
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1089
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 27.5994 - 4.4923 0.99 2847 146 0.1558 0.1866
REMARK 3 2 4.4923 - 3.5681 0.99 2708 150 0.1478 0.1771
REMARK 3 3 3.5681 - 3.1177 0.99 2673 154 0.1918 0.2372
REMARK 3 4 3.1177 - 2.8330 0.98 2610 135 0.2105 0.2762
REMARK 3 5 2.8330 - 2.6301 0.96 2591 142 0.2198 0.2385
REMARK 3 6 2.6301 - 2.4752 0.93 2488 123 0.2293 0.2976
REMARK 3 7 2.4752 - 2.3513 0.92 2444 120 0.2447 0.2854
REMARK 3 8 2.3513 - 2.2490 0.87 2300 119 0.2663 0.3040
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 39.91
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.51300
REMARK 3 B22 (A**2) : -4.34870
REMARK 3 B33 (A**2) : 2.83570
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 2107
REMARK 3 ANGLE : 1.110 2826
REMARK 3 CHIRALITY : 0.069 315
REMARK 3 PLANARITY : 0.004 355
REMARK 3 DIHEDRAL : 12.701 786
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 3RVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065432.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.25
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) : 0.97933
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI
REMARK 200 OPTICS : SAGITTAL 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 : 22709
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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 1FQW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE 2.0M TRIS 100MM PH
REMARK 280 8.25 GLYCEROL 5% (V/V) MNCL2 20MM BECL2 1MM NAF 10MM CHEY 8.9MG/
REMARK 280 ML, VAPOR DIFFUSION, HANGING 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 26.71800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.65500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.80650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.65500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.71800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.80650
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 GLY B -2
REMARK 465 SER 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 125 CG CD OE1 OE2
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 OD1 ASP A 57 BE BEF A 131 1.79
REMARK 500 OD1 ASP B 57 BE BEF B 131 1.81
REMARK 500 O HOH A 155 O HOH A 193 1.84
REMARK 500 O HOH B 149 O HOH B 184 1.90
REMARK 500 O HOH A 145 O HOH A 225 2.01
REMARK 500 O HOH A 251 O HOH A 262 2.05
REMARK 500 O HOH A 181 O HOH B 182 2.10
REMARK 500 O HOH A 186 O HOH A 257 2.10
REMARK 500 O HOH B 168 O HOH B 204 2.10
REMARK 500 O HOH A 198 O HOH A 247 2.11
REMARK 500 OE2 GLU A 34 O HOH A 216 2.15
REMARK 500 O HOH B 224 O HOH B 228 2.15
REMARK 500 OD1 ASN A 94 O HOH A 150 2.16
REMARK 500 O HOH B 223 O HOH B 229 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 TRP A 58 -60.09 -108.76
REMARK 500 ASN A 62 -62.73 80.68
REMARK 500 MET A 78 18.36 -145.55
REMARK 500 ALA B 2 48.81 -84.97
REMARK 500 TRP B 58 -62.39 -109.03
REMARK 500 ASN B 62 -57.56 72.58
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 MN A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF A 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 135
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 136
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 137
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 138
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 139
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF B 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 134
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 135
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR RESIDUE MN A 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR RESIDUE BEF A 131
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR RESIDUE MN B 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE FOR RESIDUE BEF B 131
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FQW RELATED DB: PDB
REMARK 900 STRUCTURE OF ACTIVATED CHEY
REMARK 900 RELATED ID: 3RVK RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY-MN2+ COMPLEX WITH SUBSTITUTIONS AT 59 AND 89
REMARK 900 RELATED ID: 3RVL RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY-BEF3 COMPLEX WITH SUBSTITUTIONS AT 59 AND 89
REMARK 900 RELATED ID: 3RVM RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY-MN2+ COMPLEX WITH SUBSTITUTIONS AT 59 AND 89
REMARK 900 RELATED ID: 3RVJ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY-BEF3 COMPLEX WITH SUBSTITUTIONS AT 59 AND 89
REMARK 900 RELATED ID: 3RVO RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY-MN2+ COMPLEX WITH SUBSTITUTIONS AT 59 AND 89
REMARK 900 RELATED ID: 3RVP RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY-BEF3 COMPLEX WITH SUBSTITUTIONS AT 59 AND 89
REMARK 900 RELATED ID: 3RVQ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY-MN2+ COMPLEX WITH SUBSTITUTIONS AT 59 AND 89
REMARK 900 RELATED ID: 3RVR RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY N59D/E89R MOLYBDATE COMPLEX
REMARK 900 RELATED ID: 3RVS RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHEY N59D/E89R TUNGSTATE COMPLEX
DBREF 3RVN A 1 129 UNP P0AE67 CHEY_ECOLI 1 129
DBREF 3RVN B 1 129 UNP P0AE67 CHEY_ECOLI 1 129
SEQADV 3RVN GLY A -2 UNP P0AE67 EXPRESSION TAG
SEQADV 3RVN SER A -1 UNP P0AE67 EXPRESSION TAG
SEQADV 3RVN HIS A 0 UNP P0AE67 EXPRESSION TAG
SEQADV 3RVN ASP A 59 UNP P0AE67 ASN 59 ENGINEERED MUTATION
SEQADV 3RVN TYR A 89 UNP P0AE67 GLU 89 ENGINEERED MUTATION
SEQADV 3RVN GLY B -2 UNP P0AE67 EXPRESSION TAG
SEQADV 3RVN SER B -1 UNP P0AE67 EXPRESSION TAG
SEQADV 3RVN HIS B 0 UNP P0AE67 EXPRESSION TAG
SEQADV 3RVN ASP B 59 UNP P0AE67 ASN 59 ENGINEERED MUTATION
SEQADV 3RVN TYR B 89 UNP P0AE67 GLU 89 ENGINEERED MUTATION
SEQRES 1 A 132 GLY SER HIS MET ALA ASP LYS GLU LEU LYS PHE LEU VAL
SEQRES 2 A 132 VAL ASP ASP PHE SER THR MET ARG ARG ILE VAL ARG ASN
SEQRES 3 A 132 LEU LEU LYS GLU LEU GLY PHE ASN ASN VAL GLU GLU ALA
SEQRES 4 A 132 GLU ASP GLY VAL ASP ALA LEU ASN LYS LEU GLN ALA GLY
SEQRES 5 A 132 GLY TYR GLY PHE VAL ILE SER ASP TRP ASP MET PRO ASN
SEQRES 6 A 132 MET ASP GLY LEU GLU LEU LEU LYS THR ILE ARG ALA ASP
SEQRES 7 A 132 GLY ALA MET SER ALA LEU PRO VAL LEU MET VAL THR ALA
SEQRES 8 A 132 TYR ALA LYS LYS GLU ASN ILE ILE ALA ALA ALA GLN ALA
SEQRES 9 A 132 GLY ALA SER GLY TYR VAL VAL LYS PRO PHE THR ALA ALA
SEQRES 10 A 132 THR LEU GLU GLU LYS LEU ASN LYS ILE PHE GLU LYS LEU
SEQRES 11 A 132 GLY MET
SEQRES 1 B 132 GLY SER HIS MET ALA ASP LYS GLU LEU LYS PHE LEU VAL
SEQRES 2 B 132 VAL ASP ASP PHE SER THR MET ARG ARG ILE VAL ARG ASN
SEQRES 3 B 132 LEU LEU LYS GLU LEU GLY PHE ASN ASN VAL GLU GLU ALA
SEQRES 4 B 132 GLU ASP GLY VAL ASP ALA LEU ASN LYS LEU GLN ALA GLY
SEQRES 5 B 132 GLY TYR GLY PHE VAL ILE SER ASP TRP ASP MET PRO ASN
SEQRES 6 B 132 MET ASP GLY LEU GLU LEU LEU LYS THR ILE ARG ALA ASP
SEQRES 7 B 132 GLY ALA MET SER ALA LEU PRO VAL LEU MET VAL THR ALA
SEQRES 8 B 132 TYR ALA LYS LYS GLU ASN ILE ILE ALA ALA ALA GLN ALA
SEQRES 9 B 132 GLY ALA SER GLY TYR VAL VAL LYS PRO PHE THR ALA ALA
SEQRES 10 B 132 THR LEU GLU GLU LYS LEU ASN LYS ILE PHE GLU LYS LEU
SEQRES 11 B 132 GLY MET
HET MN A 130 1
HET BEF A 131 4
HET SO4 A 132 5
HET SO4 A 133 5
HET GOL A 134 6
HET GOL A 135 6
HET GOL A 136 6
HET GOL A 137 6
HET GOL A 138 6
HET GOL A 139 6
HET MN B 130 1
HET BEF B 131 4
HET SO4 B 132 5
HET SO4 B 133 5
HET GOL B 134 6
HET GOL B 135 6
HETNAM MN MANGANESE (II) ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MN 2(MN 2+)
FORMUL 4 BEF 2(BE F3 1-)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 7 GOL 8(C3 H8 O3)
FORMUL 19 HOH *245(H2 O)
HELIX 1 1 PHE A 14 LEU A 28 1 15
HELIX 2 2 ASP A 38 GLY A 49 1 12
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 LEU B 28 1 15
HELIX 7 7 ASP B 38 GLN B 47 1 10
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 PHE A 8 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 VAL A 54
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
CISPEP 1 LYS A 109 PRO A 110 0 -0.11
CISPEP 2 LYS B 109 PRO B 110 0 -1.85
SITE 1 AC1 6 ASP A 13 ASP A 57 ASP A 59 BEF A 131
SITE 2 AC1 6 HOH A 146 HOH A 174
SITE 1 AC2 7 ASP A 57 TRP A 58 ASP A 59 THR A 87
SITE 2 AC2 7 ALA A 88 LYS A 109 MN A 130
SITE 1 AC3 5 LYS A 92 HOH A 211 HOH A 215 HOH A 257
SITE 2 AC3 5 LYS B 92
SITE 1 AC4 5 ASP A 13 PHE A 14 SER A 15 HOH A 167
SITE 2 AC4 5 HOH A 172
SITE 1 AC5 3 HIS A 0 GLY A 49 GLY A 50
SITE 1 AC6 4 ARG A 19 LYS A 70 HOH A 182 LYS B 126
SITE 1 AC7 3 LYS A 91 LYS A 92 GLU A 93
SITE 1 AC8 5 ALA A 2 LYS A 4 LEU A 28 GLY A 29
SITE 2 AC8 5 HOH A 219
SITE 1 AC9 3 ARG A 18 GLU A 35 ASP A 41
SITE 1 BC1 4 LYS A 7 ASN A 32 GLY A 50 HOH A 217
SITE 1 BC2 6 ASP B 13 ASP B 57 ASP B 59 BEF B 131
SITE 2 BC2 6 HOH B 137 HOH B 153
SITE 1 BC3 7 ASP B 57 TRP B 58 ASP B 59 THR B 87
SITE 2 BC3 7 ALA B 88 LYS B 109 MN B 130
SITE 1 BC4 4 ASP B 13 PHE B 14 SER B 15 HOH B 146
SITE 1 BC5 3 LYS B 7 ASN B 32 HOH B 244
SITE 1 BC6 4 ARG B 19 LYS B 70 HOH B 140 HOH B 209
SITE 1 BC7 4 ALA B 2 LYS B 4 LEU B 28 GLY B 29
SITE 1 CC1 6 ASP A 13 ASP A 57 ASP A 59 BEF A 131
SITE 2 CC1 6 HOH A 146 HOH A 174
SITE 1 CC2 7 ASP A 57 TRP A 58 ASP A 59 THR A 87
SITE 2 CC2 7 ALA A 88 LYS A 109 MN A 130
SITE 1 CC3 6 ASP B 13 ASP B 57 ASP B 59 BEF B 131
SITE 2 CC3 6 HOH B 137 HOH B 153
SITE 1 CC4 7 ASP B 57 TRP B 58 ASP B 59 THR B 87
SITE 2 CC4 7 ALA B 88 LYS B 109 MN B 130
CRYST1 53.436 53.613 161.310 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 0.018714 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006199 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
