HEADER CELL CYCLE 29-DEC-09 3L7X
TITLE THE CRYSTAL STRUCTURE OF SMU.412C FROM STREPTOCOCCUS MUTANS UA159
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HIT-LIKE PROTEIN INVOLVED IN CELL-CYCLE
COMPND 3 REGULATION;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: SMU.412C;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS;
SOURCE 3 ORGANISM_TAXID: 210007;
SOURCE 4 STRAIN: UA159;
SOURCE 5 GENE: SMU.412C;
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: PET28A
KEYWDS HIT-LIKE PROTEIN, CELL-CYCLE REGULATION, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.-D.SU,Z.Y.YE,X.LIU
REVDAT 2 01-NOV-23 3L7X 1 REMARK SEQADV LINK
REVDAT 1 08-DEC-10 3L7X 0
JRNL AUTH X.-D.SU,Z.Y.YE,X.LIU
JRNL TITL THE CRYSTAL STRUCTURE OF SMU.412C FROM STREPTOCOCCUS MUTANS
JRNL TITL 2 UA159
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23313
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.580
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 35.2818 - 4.0933 0.99 1676 157 0.1884 0.1978
REMARK 3 2 4.0933 - 3.2497 1.00 1585 149 0.1693 0.1860
REMARK 3 3 3.2497 - 2.8391 1.00 1538 145 0.2019 0.2274
REMARK 3 4 2.8391 - 2.5796 1.00 1541 144 0.1952 0.2449
REMARK 3 5 2.5796 - 2.3948 1.00 1503 141 0.1766 0.1917
REMARK 3 6 2.3948 - 2.2536 1.00 1510 142 0.1804 0.2208
REMARK 3 7 2.2536 - 2.1408 1.00 1513 142 0.1726 0.1992
REMARK 3 8 2.1408 - 2.0476 1.00 1508 141 0.1688 0.2143
REMARK 3 9 2.0476 - 1.9688 1.00 1501 141 0.1780 0.2125
REMARK 3 10 1.9688 - 1.9008 1.00 1489 140 0.1774 0.2090
REMARK 3 11 1.9008 - 1.8414 1.00 1478 139 0.1879 0.2257
REMARK 3 12 1.8414 - 1.7888 1.00 1490 139 0.1867 0.2329
REMARK 3 13 1.7888 - 1.7417 1.00 1501 141 0.1943 0.2421
REMARK 3 14 1.7417 - 1.6992 1.00 1480 139 0.2221 0.2816
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 : 0.39
REMARK 3 B_SOL : 72.80
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.90100
REMARK 3 B22 (A**2) : 4.90100
REMARK 3 B33 (A**2) : -9.80100
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 : 0.021 1207
REMARK 3 ANGLE : 1.875 1631
REMARK 3 CHIRALITY : 0.154 188
REMARK 3 PLANARITY : 0.010 216
REMARK 3 DIHEDRAL : 18.476 434
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6919 -10.3415 -6.3348
REMARK 3 T TENSOR
REMARK 3 T11: 0.0868 T22: 0.1330
REMARK 3 T33: 0.1324 T12: -0.0103
REMARK 3 T13: -0.0011 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.4763 L22: 0.5916
REMARK 3 L33: 2.5144 L12: -0.0980
REMARK 3 L13: -0.2148 L23: 0.2291
REMARK 3 S TENSOR
REMARK 3 S11: 0.0003 S12: 0.0917 S13: 0.0230
REMARK 3 S21: -0.0740 S22: -0.0025 S23: -0.0197
REMARK 3 S31: -0.1550 S32: 0.1644 S33: 0.0037
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 3L7X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000056945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23340
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.699
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1Y23
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8M SODIUM ACETATE TRIHYDRATE PH7.0,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.52950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 26.67400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 26.67400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.26475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 26.67400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 26.67400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 105.79425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 26.67400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.67400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.26475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 26.67400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.67400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.79425
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.52950
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: 5900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -33
REMARK 465 GLY A -32
REMARK 465 SER A -31
REMARK 465 SER A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 SER A -23
REMARK 465 SER A -22
REMARK 465 GLY A -21
REMARK 465 ARG A -2
REMARK 465 ASP A 108
REMARK 465 ALA A 139
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 -20 CG CD1 CD2
REMARK 470 MET A -10 CG SD CE
REMARK 470 GLU A 23 CG CD OE1 OE2
REMARK 470 SER A 109 OG
REMARK 470 ARG A 115 NE CZ NH1 NH2
REMARK 470 ARG A 125 NE CZ NH1 NH2
REMARK 470 GLU A 131 CG CD OE1 OE2
REMARK 470 LYS A 135 CE NZ
REMARK 470 GLU A 138 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 GLU A 88 165.00 74.76
REMARK 500 PHE A 96 46.13 -93.23
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 NA A 142 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A -11 OG
REMARK 620 2 THR A -9 OG1 80.8
REMARK 620 3 GLY A -8 O 87.1 113.6
REMARK 620 4 GLU A 52 O 163.7 83.1 102.0
REMARK 620 5 HOH A 160 O 93.5 94.7 151.3 85.0
REMARK 620 6 HOH A 180 O 100.4 162.1 84.3 94.0 67.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 140 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 4 SG
REMARK 620 2 CYS A 7 SG 117.4
REMARK 620 3 HIS A 46 ND1 111.2 108.0
REMARK 620 4 HIS A 97 ND1 107.5 113.9 96.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 141 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 147 O
REMARK 620 2 HOH A 153 O 152.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 142
DBREF 3L7X A 1 139 UNP Q8DVQ8 Q8DVQ8_STRMU 1 139
SEQADV 3L7X MET A -33 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLY A -32 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X SER A -31 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X SER A -30 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X HIS A -29 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X HIS A -28 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X HIS A -27 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X HIS A -26 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X HIS A -25 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X HIS A -24 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X SER A -23 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X SER A -22 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLY A -21 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X LEU A -20 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X VAL A -19 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X PRO A -18 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X ARG A -17 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLY A -16 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X SER A -15 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X HIS A -14 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X MET A -13 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X ALA A -12 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X SER A -11 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X MET A -10 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X THR A -9 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLY A -8 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLY A -7 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLN A -6 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLN A -5 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X MET A -4 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLY A -3 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X ARG A -2 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X GLY A -1 UNP Q8DVQ8 EXPRESSION TAG
SEQADV 3L7X SER A 0 UNP Q8DVQ8 EXPRESSION TAG
SEQRES 1 A 173 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 173 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 173 GLY GLN GLN MET GLY ARG GLY SER MET ASN ASP CYS LEU
SEQRES 4 A 173 PHE CYS LYS ILE VAL ALA GLY ASP ILE PRO SER SER LYS
SEQRES 5 A 173 VAL TYR GLU ASP GLU ASP VAL LEU ALA PHE LEU ASP ILE
SEQRES 6 A 173 SER GLN ALA THR LYS GLY HIS THR LEU VAL ILE PRO LYS
SEQRES 7 A 173 GLU HIS VAL ARG ASN ALA LEU GLU MET THR GLN THR GLN
SEQRES 8 A 173 ALA ALA ASN LEU PHE ALA ARG ILE PRO LYS ILE ALA ARG
SEQRES 9 A 173 ALA LEU GLN LYS ALA THR LYS ALA ASP GLY LEU ASN ILE
SEQRES 10 A 173 ILE ASN ASN ASN GLU GLU THR ALA GLY GLN THR VAL PHE
SEQRES 11 A 173 HIS ALA HIS VAL HIS LEU VAL PRO ARG PHE ALA ASP SER
SEQRES 12 A 173 ASP GLU PHE ASP ILE ARG PHE VAL GLN HIS GLU PRO ASP
SEQRES 13 A 173 PHE THR ARG LEU GLY GLN LEU ALA GLU ASP ILE GLN LYS
SEQRES 14 A 173 GLU ILE GLU ALA
HET ZN A 140 1
HET NA A 141 1
HET NA A 142 1
HETNAM ZN ZINC ION
HETNAM NA SODIUM ION
FORMUL 2 ZN ZN 2+
FORMUL 3 NA 2(NA 1+)
FORMUL 5 HOH *60(H2 O)
HELIX 1 1 CYS A 4 ALA A 11 1 8
HELIX 2 2 ASN A 49 MET A 53 5 5
HELIX 3 3 THR A 54 ARG A 64 1 11
HELIX 4 4 ARG A 64 LYS A 77 1 14
HELIX 5 5 GLU A 88 GLY A 92 5 5
HELIX 6 6 ASP A 122 GLU A 138 1 17
SHEET 1 A 5 LYS A 18 GLU A 21 0
SHEET 2 A 5 VAL A 25 LEU A 29 -1 O ALA A 27 N TYR A 20
SHEET 3 A 5 THR A 39 PRO A 43 -1 O ILE A 42 N LEU A 26
SHEET 4 A 5 VAL A 100 ARG A 105 -1 O LEU A 102 N THR A 39
SHEET 5 A 5 GLY A 80 ASN A 85 -1 N ILE A 84 O HIS A 101
LINK OG SER A -11 NA NA A 142 1555 1555 2.47
LINK OG1 THR A -9 NA NA A 142 1555 1555 2.47
LINK O GLY A -8 NA NA A 142 1555 1555 2.56
LINK SG CYS A 4 ZN ZN A 140 1555 1555 2.28
LINK SG CYS A 7 ZN ZN A 140 1555 1555 2.31
LINK ND1 HIS A 46 ZN ZN A 140 1555 1555 2.14
LINK O GLU A 52 NA NA A 142 1555 1555 2.34
LINK ND1 HIS A 97 ZN ZN A 140 1555 1555 2.11
LINK NA NA A 141 O HOH A 147 1555 1555 2.87
LINK NA NA A 141 O HOH A 153 1555 1555 2.60
LINK NA NA A 142 O HOH A 160 1555 1555 2.43
LINK NA NA A 142 O HOH A 180 1555 1555 2.61
SITE 1 AC1 4 CYS A 4 CYS A 7 HIS A 46 HIS A 97
SITE 1 AC2 5 ASN A 86 HIS A 99 HIS A 101 HOH A 147
SITE 2 AC2 5 HOH A 153
SITE 1 AC3 6 THR A -9 GLY A -8 SER A -11 GLU A 52
SITE 2 AC3 6 HOH A 160 HOH A 180
CRYST1 53.348 53.348 141.059 90.00 90.00 90.00 P 41 21 2 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 0.018745 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018745 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007089 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
