HEADER SIGNALING PROTEIN 23-JUN-09 3HZH
TITLE CRYSTAL STRUCTURE OF THE CHEX-CHEY-BEF3-MG+2 COMPLEX FROM
TITLE 2 BORRELIA BURGDORFERI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS RESPONSE REGULATOR (CHEY-3);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CHEMOTAXIS OPERON PROTEIN (CHEX);
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;
SOURCE 3 ORGANISM_TAXID: 139;
SOURCE 4 GENE: BB_0672, CHEY3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15/PREP4;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;
SOURCE 12 ORGANISM_TAXID: 139;
SOURCE 13 GENE: BB_0671, CHEX;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: M15/PREP4;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS CHEMOTAXIS, PHOSPHATASE, COMPLEX, RESPONSE REGULATOR,
KEYWDS 2 RECEIVER DOMAIN, TWO-COMPONENT SIGNAL TRANSDUCTION,
KEYWDS 3 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PAZY,R.E.SILVERSMITH,M.GUARINARI,R.ZHAO
REVDAT 1 16-FEB-10 3HZH 0
JRNL AUTH Y.PAZY,M.A.MOTALEB,M.T.GUARNIERI,N.W.CHARON,R.ZHAO,
JRNL AUTH 2 R.E.SILVERSMITH
JRNL TITL IDENTICAL PHOSPHATASE MECHANISMS ACHIEVED THROUGH
JRNL TITL 2 DISTINCT MODES OF BINDING PHOSPHOPROTEIN SUBSTRATE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 1924 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20080618
JRNL DOI 10.1073/PNAS.0911185107
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 45929
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2230
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 158
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.25200
REMARK 3 B22 (A**2) : -1.25200
REMARK 3 B33 (A**2) : 2.50500
REMARK 3 B12 (A**2) : -2.05900
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.02
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HZH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053773.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97923
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45929
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 29.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.53100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: RESOLVE SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 5.6, VAPOR
REMARK 280 DIFFUSION, SITTING 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 117.12333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.56167
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 58.56167
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 117.12333
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -10
REMARK 465 ARG A -9
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ILE A 2
REMARK 465 GLN A 3
REMARK 465 LYS A 4
REMARK 465 THR A 5
REMARK 465 THR A 6
REMARK 465 ILE A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 ASP A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 MSE B -10
REMARK 465 ARG B -9
REMARK 465 GLY B -8
REMARK 465 SER B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 37
REMARK 465 GLN B 38
REMARK 465 LYS B 39
REMARK 465 ILE B 40
REMARK 465 ARG B 160
REMARK 465 VAL B 161
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 OD2 ASP B 147 NZ LYS B 149 2.01
REMARK 500 O LEU B 145 O ASP B 147 2.05
REMARK 500 O ILE B 131 N ASN B 133 2.13
REMARK 500 N THR A 125 O HOH A 224 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ILE B 26 N - CA - C ANGL. DEV. = -17.3 DEGREES
REMARK 500 SER B 35 N - CA - C ANGL. DEV. = 30.8 DEGREES
REMARK 500 ASN B 128 N - CA - CB ANGL. DEV. = -12.4 DEGREES
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 LYS A 14 96.73 -32.33
REMARK 500 THR A 22 -21.45 -143.95
REMARK 500 TYR A 70 -64.25 3.48
REMARK 500 LYS A 84 -51.06 57.62
REMARK 500 ASN B 25 88.72 93.43
REMARK 500 SER B 35 169.80 -19.18
REMARK 500 PHE B 114 -141.15 -105.36
REMARK 500 ASN B 128 31.48 -69.56
REMARK 500 LYS B 130 89.09 -10.26
REMARK 500 ILE B 131 -0.70 -57.89
REMARK 500 SER B 132 98.67 -25.34
REMARK 500 ASN B 133 -153.43 -73.19
REMARK 500 LYS B 134 115.33 -161.88
REMARK 500 SER B 136 144.61 176.60
REMARK 500 GLU B 137 103.45 -21.81
REMARK 500 PRO B 146 -44.20 -25.79
REMARK 500 ARG B 158 51.10 -92.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TYR A 70 23.7 L L OUTSIDE RANGE
REMARK 500 LYS B 34 23.1 L L OUTSIDE RANGE
REMARK 500 SER B 35 15.8 L L OUTSIDE RANGE
REMARK 500 ASN B 133 24.6 L L OUTSIDE RANGE
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 A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 33 OD1
REMARK 620 2 BFD A 79 OD2 84.3
REMARK 620 3 THR A 81 O 88.6 80.8
REMARK 620 4 HOH A 158 O 93.0 166.6 86.1
REMARK 620 5 HOH A 157 O 89.3 81.9 162.6 111.2
REMARK 620 N 1 2 3 4
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 202
DBREF 3HZH A 2 146 UNP O51615 O51615_BORBU 2 146
DBREF 3HZH B 2 161 UNP O51614 O51614_BORBU 2 161
SEQADV 3HZH MET A -10 UNP O51615 EXPRESSION TAG
SEQADV 3HZH ARG A -9 UNP O51615 EXPRESSION TAG
SEQADV 3HZH GLY A -8 UNP O51615 EXPRESSION TAG
SEQADV 3HZH SER A -7 UNP O51615 EXPRESSION TAG
SEQADV 3HZH HIS A -6 UNP O51615 EXPRESSION TAG
SEQADV 3HZH HIS A -5 UNP O51615 EXPRESSION TAG
SEQADV 3HZH HIS A -4 UNP O51615 EXPRESSION TAG
SEQADV 3HZH HIS A -3 UNP O51615 EXPRESSION TAG
SEQADV 3HZH HIS A -2 UNP O51615 EXPRESSION TAG
SEQADV 3HZH HIS A -1 UNP O51615 EXPRESSION TAG
SEQADV 3HZH GLY A 0 UNP O51615 EXPRESSION TAG
SEQADV 3HZH SER A 1 UNP O51615 EXPRESSION TAG
SEQADV 3HZH MSE B -10 UNP O51614 EXPRESSION TAG
SEQADV 3HZH ARG B -9 UNP O51614 EXPRESSION TAG
SEQADV 3HZH GLY B -8 UNP O51614 EXPRESSION TAG
SEQADV 3HZH SER B -7 UNP O51614 EXPRESSION TAG
SEQADV 3HZH HIS B -6 UNP O51614 EXPRESSION TAG
SEQADV 3HZH HIS B -5 UNP O51614 EXPRESSION TAG
SEQADV 3HZH HIS B -4 UNP O51614 EXPRESSION TAG
SEQADV 3HZH HIS B -3 UNP O51614 EXPRESSION TAG
SEQADV 3HZH HIS B -2 UNP O51614 EXPRESSION TAG
SEQADV 3HZH HIS B -1 UNP O51614 EXPRESSION TAG
SEQADV 3HZH GLY B 0 UNP O51614 EXPRESSION TAG
SEQADV 3HZH SER B 1 UNP O51614 EXPRESSION TAG
SEQRES 1 A 157 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE
SEQRES 2 A 157 GLN LYS THR THR ILE ALA ALA ASP SER SER SER LYS PRO
SEQRES 3 A 157 ARG GLY ILE ASN TYR ASP THR GLY ILE PRO PHE ASN VAL
SEQRES 4 A 157 LEU ILE VAL ASP ASP SER VAL PHE THR VAL LYS GLN LEU
SEQRES 5 A 157 THR GLN ILE PHE THR SER GLU GLY PHE ASN ILE ILE ASP
SEQRES 6 A 157 THR ALA ALA ASP GLY GLU GLU ALA VAL ILE LYS TYR LYS
SEQRES 7 A 157 ASN HIS TYR PRO ASN ILE ASP ILE VAL THR LEU BFD ILE
SEQRES 8 A 157 THR MET PRO LYS MET ASP GLY ILE THR CYS LEU SER ASN
SEQRES 9 A 157 ILE MET GLU PHE ASP LYS ASN ALA ARG VAL ILE MET ILE
SEQRES 10 A 157 SER ALA LEU GLY LYS GLU GLN LEU VAL LYS ASP CYS LEU
SEQRES 11 A 157 ILE LYS GLY ALA LYS THR PHE ILE VAL LYS PRO LEU ASP
SEQRES 12 A 157 ARG ALA LYS VAL LEU GLN ARG VAL MET SER VAL PHE VAL
SEQRES 13 A 157 LYS
SEQRES 1 B 172 MSE ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 B 172 ILE ASP TYR ILE GLU PRO PHE LEU ASP ALA ALA SER SER
SEQRES 3 B 172 VAL LEU ARG ASP MSE LEU LEU VAL GLU ASN ILE GLU MSE
SEQRES 4 B 172 GLY LYS PRO GLY LEU LYS SER ILE ASN GLN LYS ILE LYS
SEQRES 5 B 172 GLY VAL SER VAL ILE VAL GLY LEU ALA GLY SER VAL GLU
SEQRES 6 B 172 GLY SER ILE ILE ILE ASP MSE ASP ILE GLU THR ALA LEU
SEQRES 7 B 172 PHE VAL ALA SER LYS LEU ASN PHE GLU GLU TYR ASP ASP
SEQRES 8 B 172 PHE ASP ASP GLU GLU THR LYS GLU MSE VAL ALA ALA THR
SEQRES 9 B 172 LEU THR GLU VAL GLY ASN ILE ILE ALA GLY ASN PHE VAL
SEQRES 10 B 172 THR THR LEU HIS ALA LYS GLY PHE VAL PHE ASP ILE THR
SEQRES 11 B 172 PRO PRO ALA PHE ILE TYR GLY GLU ASN MSE LYS ILE SER
SEQRES 12 B 172 ASN LYS GLY SER GLU ALA LEU ILE VAL PRO PHE SER LEU
SEQRES 13 B 172 PRO ASP GLY LYS ILE ILE GLU VAL ASN ILE ALA ILE ARG
SEQRES 14 B 172 GLU ARG VAL
MODRES 3HZH BFD A 79 ASP ASPARTATE BERYLLIUM TRIFLUORIDE
MODRES 3HZH MSE B 20 MET SELENOMETHIONINE
MODRES 3HZH MSE B 28 MET SELENOMETHIONINE
MODRES 3HZH MSE B 61 MET SELENOMETHIONINE
MODRES 3HZH MSE B 89 MET SELENOMETHIONINE
MODRES 3HZH MSE B 129 MET SELENOMETHIONINE
HET BFD A 79 12
HET MSE B 20 8
HET MSE B 28 8
HET MSE B 61 8
HET MSE B 89 8
HET MSE B 129 8
HET MG A 202 1
HETNAM BFD ASPARTATE BERYLLIUM TRIFLUORIDE
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
FORMUL 1 BFD C4 H6 BE F3 N O4 2-
FORMUL 2 MSE 5(C5 H11 N O2 SE)
FORMUL 3 MG MG 2+
FORMUL 4 HOH *158(H2 O)
HELIX 1 1 SER A 34 GLU A 48 1 15
HELIX 2 2 ASP A 58 TYR A 70 1 13
HELIX 3 3 PRO A 71 ILE A 73 5 3
HELIX 4 4 ASP A 86 ASP A 98 1 13
HELIX 5 5 LYS A 111 LYS A 121 1 11
HELIX 6 6 ASP A 132 VAL A 143 1 12
HELIX 7 7 TYR B 5 LEU B 21 1 17
HELIX 8 8 ASP B 62 PHE B 75 1 14
HELIX 9 9 GLU B 85 THR B 108 1 24
SHEET 1 A 5 ASN A 51 ALA A 56 0
SHEET 2 A 5 ASN A 27 VAL A 31 1 N VAL A 28 O ASN A 51
SHEET 3 A 5 ILE A 75 LEU A 78 1 O ILE A 75 N LEU A 29
SHEET 4 A 5 VAL A 103 SER A 107 1 O ILE A 104 N VAL A 76
SHEET 5 A 5 THR A 125 VAL A 128 1 O ILE A 127 N MET A 105
SHEET 1 B 6 GLU B 27 MSE B 28 0
SHEET 2 B 6 ALA B 138 SER B 144 -1 O SER B 144 N GLU B 27
SHEET 3 B 6 ILE B 150 ILE B 157 -1 O ILE B 151 N PHE B 143
SHEET 4 B 6 GLY B 55 MSE B 61 -1 N ILE B 58 O ASN B 154
SHEET 5 B 6 VAL B 43 GLY B 51 -1 N VAL B 43 O MSE B 61
SHEET 6 B 6 PHE B 116 ILE B 118 -1 O ASP B 117 N ALA B 50
SHEET 1 C 6 GLU B 27 MSE B 28 0
SHEET 2 C 6 ALA B 138 SER B 144 -1 O SER B 144 N GLU B 27
SHEET 3 C 6 ILE B 150 ILE B 157 -1 O ILE B 151 N PHE B 143
SHEET 4 C 6 GLY B 55 MSE B 61 -1 N ILE B 58 O ASN B 154
SHEET 5 C 6 VAL B 43 GLY B 51 -1 N VAL B 43 O MSE B 61
SHEET 6 C 6 ALA B 122 ILE B 124 -1 O ILE B 124 N SER B 44
LINK C LEU A 78 N BFD A 79 1555 1555 1.33
LINK C BFD A 79 N ILE A 80 1555 1555 1.33
LINK C ASP B 19 N MSE B 20 1555 1555 1.33
LINK C MSE B 20 N LEU B 21 1555 1555 1.33
LINK C GLU B 27 N MSE B 28 1555 1555 1.33
LINK C MSE B 28 N GLY B 29 1555 1555 1.33
LINK C ASP B 60 N MSE B 61 1555 1555 1.33
LINK C MSE B 61 N ASP B 62 1555 1555 1.33
LINK C GLU B 88 N MSE B 89 1555 1555 1.33
LINK C MSE B 89 N VAL B 90 1555 1555 1.34
LINK C ASN B 128 N MSE B 129 1555 1555 1.32
LINK C MSE B 129 N LYS B 130 1555 1555 1.33
LINK OD1 ASP A 33 MG MG A 202 1555 1555 2.08
LINK OD2 BFD A 79 MG MG A 202 1555 1555 2.21
LINK O THR A 81 MG MG A 202 1555 1555 2.22
LINK MG MG A 202 O HOH A 158 1555 1555 2.22
LINK MG MG A 202 O HOH A 157 1555 1555 2.31
CISPEP 1 LYS A 129 PRO A 130 0 -2.69
SITE 1 AC1 5 ASP A 33 BFD A 79 THR A 81 HOH A 157
SITE 2 AC1 5 HOH A 158
CRYST1 63.705 63.705 175.685 90.00 90.00 120.00 P 32 2 1 6
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 0.015697 0.009063 0.000000 0.00000
SCALE2 0.000000 0.018126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005692 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
