HEADER DNA BINDING PROTEIN 04-MAY-15 4ZMR
TITLE STRUCTURAL CHARACTERIZATION OF THE FULL-LENGTH RESPONSE REGULATOR
TITLE 2 SPR1814 IN COMPLEX WITH A PHOSPHATE ANALOGUE REVEALS A NOVEL
TITLE 3 CONFORMATIONAL PLASTICITY OF THE LINKER REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RESPONSE REGULATOR;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE (STRAIN ATCC BAA-255 /
SOURCE 3 R6);
SOURCE 4 ORGANISM_TAXID: 171101;
SOURCE 5 STRAIN: ATCC BAA-255 / R6;
SOURCE 6 GENE: RR11, SPR1814;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RESPONSE REGULATOR, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.M.CHI,A.PARK
REVDAT 4 20-MAR-24 4ZMR 1 LINK
REVDAT 3 19-FEB-20 4ZMR 1 JRNL REMARK
REVDAT 2 04-MAY-16 4ZMR 1 JRNL
REVDAT 1 27-APR-16 4ZMR 0
JRNL AUTH A.K.PARK,J.H.LEE,Y.M.CHI,H.PARK
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE FULL-LENGTH RESPONSE
JRNL TITL 2 REGULATOR SPR1814 IN COMPLEX WITH A PHOSPHATE ANALOGUE
JRNL TITL 3 REVEALS A NOVEL CONFORMATIONAL PLASTICITY OF THE LINKER
JRNL TITL 4 REGION
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 473 625 2016
JRNL REFN ESSN 1090-2104
JRNL PMID 27038544
JRNL DOI 10.1016/J.BBRC.2016.03.144
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX PHENIX.REFINE: 1.9_1692
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.540
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 29467
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 : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1473
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 37.7132 - 4.4474 0.99 2652 129 0.1525 0.1818
REMARK 3 2 4.4474 - 3.5309 1.00 2647 152 0.1415 0.1885
REMARK 3 3 3.5309 - 3.0848 1.00 2613 150 0.1840 0.2565
REMARK 3 4 3.0848 - 2.8028 0.99 2598 164 0.2029 0.2413
REMARK 3 5 2.8028 - 2.6020 0.99 2628 121 0.1996 0.2526
REMARK 3 6 2.6020 - 2.4486 0.99 2594 142 0.1979 0.2474
REMARK 3 7 2.4486 - 2.3260 0.98 2579 136 0.1925 0.2164
REMARK 3 8 2.3260 - 2.2248 0.98 2585 130 0.1924 0.2556
REMARK 3 9 2.2248 - 2.1391 0.97 2539 133 0.1997 0.2506
REMARK 3 10 2.1391 - 2.0653 0.94 2523 117 0.2116 0.2745
REMARK 3 11 2.0653 - 2.0007 0.78 2036 99 0.2342 0.2747
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.014 3221
REMARK 3 ANGLE : 1.438 4350
REMARK 3 CHIRALITY : 0.056 521
REMARK 3 PLANARITY : 0.006 555
REMARK 3 DIHEDRAL : 16.582 1236
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 4ZMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35851
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
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 (%): 50.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE TRIBASIC DIHYDRATE
REMARK 280 PH 5.0, 30%(V/V) JEFFAMINE ED-2001 PH 7, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 57.24550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: 2190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
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 LEU A 199 O
REMARK 470 LEU B 199 O
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 HE21 GLN A 142 O HOH A 301 1.42
REMARK 500 HZ3 LYS A 84 OE2 GLU A 127 1.55
REMARK 500 O HOH A 416 O HOH A 429 1.83
REMARK 500 NH2 ARG B 105 O HOH B 301 1.90
REMARK 500 O HOH A 359 O HOH A 394 1.93
REMARK 500 NE2 GLN A 142 O HOH A 301 2.12
REMARK 500 O HOH B 308 O HOH B 385 2.12
REMARK 500 O HOH B 319 O HOH B 334 2.14
REMARK 500 ND1 HIS B 0 O HOH B 302 2.15
REMARK 500 OE1 GLU A 55 O HOH A 302 2.15
REMARK 500 O HOH A 369 O HOH A 373 2.16
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 330 O HOH B 306 1556 1.79
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 MET B 111 CG - SD - CE ANGL. DEV. = -10.0 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 HIS A 0 59.86 -155.38
REMARK 500 VAL A 58 -60.72 79.33
REMARK 500 ASP A 182 56.76 37.08
REMARK 500 GLU B 7 127.50 -170.36
REMARK 500 VAL B 58 -69.26 69.29
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 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 8 OD1
REMARK 620 2 ASP A 53 OD2 84.7
REMARK 620 3 GLU A 55 O 99.0 92.2
REMARK 620 4 HOH A 322 O 85.9 82.5 172.5
REMARK 620 5 HOH A 393 O 98.0 170.6 96.3 88.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 8 OD1
REMARK 620 2 ASP B 53 OD1 79.9
REMARK 620 3 GLU B 55 O 92.4 89.4
REMARK 620 4 HOH B 325 O 87.4 85.1 174.4
REMARK 620 5 HOH B 389 O 100.1 174.3 96.3 89.2
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEF A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEF B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZMS RELATED DB: PDB
DBREF 4ZMR A 1 199 UNP Q8DNC2 Q8DNC2_STRR6 1 199
DBREF 4ZMR B 1 199 UNP Q8DNC2 Q8DNC2_STRR6 1 199
SEQADV 4ZMR GLY A -7 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR LEU A -6 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR VAL A -5 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR PRO A -4 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR ARG A -3 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR GLY A -2 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR SER A -1 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR HIS A 0 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR GLY B -7 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR LEU B -6 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR VAL B -5 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR PRO B -4 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR ARG B -3 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR GLY B -2 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR SER B -1 UNP Q8DNC2 EXPRESSION TAG
SEQADV 4ZMR HIS B 0 UNP Q8DNC2 EXPRESSION TAG
SEQRES 1 A 207 GLY LEU VAL PRO ARG GLY SER HIS MET LYS VAL LEU VAL
SEQRES 2 A 207 ALA GLU ASP GLN SER MET LEU ARG ASP ALA MET CYS GLN
SEQRES 3 A 207 LEU LEU THR LEU GLN PRO ASP VAL GLU SER VAL LEU GLN
SEQRES 4 A 207 ALA LYS ASN GLY GLN GLU ALA ILE GLN LEU LEU GLU LYS
SEQRES 5 A 207 GLU SER VAL ASP ILE ALA ILE LEU ASP VAL GLU MET PRO
SEQRES 6 A 207 VAL LYS THR GLY LEU GLU VAL LEU GLU TRP ILE ARG SER
SEQRES 7 A 207 GLU LYS LEU GLU THR LYS VAL VAL VAL VAL THR THR PHE
SEQRES 8 A 207 LYS ARG ALA GLY TYR PHE GLU ARG ALA VAL LYS ALA GLY
SEQRES 9 A 207 VAL ASP ALA TYR VAL LEU LYS GLU ARG SER ILE ALA ASP
SEQRES 10 A 207 LEU MET GLN THR LEU HIS THR VAL LEU GLU GLY ARG LYS
SEQRES 11 A 207 GLU TYR SER PRO GLU LEU MET GLU MET VAL MET THR ARG
SEQRES 12 A 207 PRO ASN PRO LEU THR GLU GLN GLU ILE ALA VAL LEU LYS
SEQRES 13 A 207 GLY ILE ALA ARG GLY LEU SER ASN GLN GLU ILE ALA ASP
SEQRES 14 A 207 GLN LEU TYR LEU SER ASN GLY THR ILE ARG ASN TYR VAL
SEQRES 15 A 207 THR ASN ILE LEU SER LYS LEU ASP ALA GLY ASN ARG THR
SEQRES 16 A 207 GLU ALA ALA ASN ILE ALA LYS GLU SER GLY TRP LEU
SEQRES 1 B 207 GLY LEU VAL PRO ARG GLY SER HIS MET LYS VAL LEU VAL
SEQRES 2 B 207 ALA GLU ASP GLN SER MET LEU ARG ASP ALA MET CYS GLN
SEQRES 3 B 207 LEU LEU THR LEU GLN PRO ASP VAL GLU SER VAL LEU GLN
SEQRES 4 B 207 ALA LYS ASN GLY GLN GLU ALA ILE GLN LEU LEU GLU LYS
SEQRES 5 B 207 GLU SER VAL ASP ILE ALA ILE LEU ASP VAL GLU MET PRO
SEQRES 6 B 207 VAL LYS THR GLY LEU GLU VAL LEU GLU TRP ILE ARG SER
SEQRES 7 B 207 GLU LYS LEU GLU THR LYS VAL VAL VAL VAL THR THR PHE
SEQRES 8 B 207 LYS ARG ALA GLY TYR PHE GLU ARG ALA VAL LYS ALA GLY
SEQRES 9 B 207 VAL ASP ALA TYR VAL LEU LYS GLU ARG SER ILE ALA ASP
SEQRES 10 B 207 LEU MET GLN THR LEU HIS THR VAL LEU GLU GLY ARG LYS
SEQRES 11 B 207 GLU TYR SER PRO GLU LEU MET GLU MET VAL MET THR ARG
SEQRES 12 B 207 PRO ASN PRO LEU THR GLU GLN GLU ILE ALA VAL LEU LYS
SEQRES 13 B 207 GLY ILE ALA ARG GLY LEU SER ASN GLN GLU ILE ALA ASP
SEQRES 14 B 207 GLN LEU TYR LEU SER ASN GLY THR ILE ARG ASN TYR VAL
SEQRES 15 B 207 THR ASN ILE LEU SER LYS LEU ASP ALA GLY ASN ARG THR
SEQRES 16 B 207 GLU ALA ALA ASN ILE ALA LYS GLU SER GLY TRP LEU
HET MG A 201 1
HET BEF A 202 4
HET MG B 201 1
HET BEF B 202 4
HETNAM MG MAGNESIUM ION
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
FORMUL 3 MG 2(MG 2+)
FORMUL 4 BEF 2(BE F3 1-)
FORMUL 7 HOH *257(H2 O)
HELIX 1 AA1 GLN A 9 GLN A 23 1 15
HELIX 2 AA2 ASN A 34 GLU A 43 1 10
HELIX 3 AA3 THR A 60 GLU A 71 1 12
HELIX 4 AA4 ARG A 85 ALA A 95 1 11
HELIX 5 AA5 SER A 106 GLU A 119 1 14
HELIX 6 AA6 SER A 125 THR A 134 1 10
HELIX 7 AA7 THR A 140 ALA A 151 1 12
HELIX 8 AA8 SER A 155 TYR A 164 1 10
HELIX 9 AA9 SER A 166 LEU A 181 1 16
HELIX 10 AB1 ASN A 185 SER A 196 1 12
HELIX 11 AB2 GLN B 9 GLN B 23 1 15
HELIX 12 AB3 ASN B 34 GLU B 45 1 12
HELIX 13 AB4 THR B 60 GLU B 71 1 12
HELIX 14 AB5 ARG B 85 ALA B 95 1 11
HELIX 15 AB6 SER B 106 GLU B 119 1 14
HELIX 16 AB7 SER B 125 THR B 134 1 10
HELIX 17 AB8 THR B 140 ARG B 152 1 13
HELIX 18 AB9 SER B 155 TYR B 164 1 10
HELIX 19 AC1 SER B 166 ASP B 182 1 17
HELIX 20 AC2 ASN B 185 SER B 196 1 12
SHEET 1 AA1 6 VAL A 26 ALA A 32 0
SHEET 2 AA1 6 MET A 1 ALA A 6 1 N VAL A 5 O LEU A 30
SHEET 3 AA1 6 ILE A 49 LEU A 52 1 O ILE A 51 N LEU A 4
SHEET 4 AA1 6 LYS A 76 THR A 81 1 O VAL A 78 N LEU A 52
SHEET 5 AA1 6 ALA A 99 LEU A 102 1 O ALA A 99 N VAL A 79
SHEET 6 AA1 6 GLU A 123 TYR A 124 1 O GLU A 123 N TYR A 100
SHEET 1 AA2 6 VAL B 26 ALA B 32 0
SHEET 2 AA2 6 MET B 1 ALA B 6 1 N VAL B 5 O LEU B 30
SHEET 3 AA2 6 ILE B 49 LEU B 52 1 O ILE B 51 N LEU B 4
SHEET 4 AA2 6 LYS B 76 THR B 81 1 O LYS B 76 N ALA B 50
SHEET 5 AA2 6 ALA B 99 LEU B 102 1 O ALA B 99 N VAL B 79
SHEET 6 AA2 6 GLU B 123 TYR B 124 1 O GLU B 123 N TYR B 100
LINK OD1 ASP A 8 MG MG A 201 1555 1555 2.04
LINK OD2 ASP A 53 MG MG A 201 1555 1555 2.15
LINK O GLU A 55 MG MG A 201 1555 1555 1.91
LINK MG MG A 201 O HOH A 322 1555 1555 2.35
LINK MG MG A 201 O HOH A 393 1555 1555 2.22
LINK OD1 ASP B 8 MG MG B 201 1555 1555 2.03
LINK OD1 ASP B 53 MG MG B 201 1555 1555 2.04
LINK O GLU B 55 MG MG B 201 1555 1555 2.09
LINK MG MG B 201 O HOH B 325 1555 1555 2.14
LINK MG MG B 201 O HOH B 389 1555 1555 2.11
SITE 1 AC1 6 ASP A 8 ASP A 53 GLU A 55 BEF A 202
SITE 2 AC1 6 HOH A 322 HOH A 393
SITE 1 AC2 11 ASP A 53 VAL A 54 GLU A 55 THR A 81
SITE 2 AC2 11 THR A 82 PHE A 83 LYS A 103 MG A 201
SITE 3 AC2 11 HOH A 322 HOH A 393 HOH A 409
SITE 1 AC3 6 ASP B 8 ASP B 53 GLU B 55 BEF B 202
SITE 2 AC3 6 HOH B 325 HOH B 389
SITE 1 AC4 11 ASP B 53 VAL B 54 GLU B 55 THR B 81
SITE 2 AC4 11 THR B 82 PHE B 83 LYS B 103 MG B 201
SITE 3 AC4 11 HOH B 325 HOH B 389 HOH B 413
CRYST1 40.233 114.491 50.148 90.00 92.12 90.00 P 1 21 1 4
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 0.024855 0.000000 0.000922 0.00000
SCALE2 0.000000 0.008734 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019955 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
