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HEADER HYDROLASE 10-OCT-14 4V2I
TITLE BIOCHEMICAL CHARACTERIZATION AND STRUCTURAL ANALYSIS OF A
TITLE 2 NEW COLD-ACTIVE AND SALT TOLERANT ESTERASE FROM THE MARINE
TITLE 3 BACTERIUM THALASSOSPIRA SP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ESTERASE;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THALASSOSPIRA SP. GB04J01 THE STRAIN THALASSOSPIRA
COMPND 8 SP. GB04J01 WAS ISOLATED FROM A SEA FAN (PARAMURICEA PLACOMUS)
COMPND 9 DURING A RESEARCH-CRUISE WITH R/V HELMER HANSSEN TO THE
COMPND 10 VESTFJORDEN AREA (NORTHERN NORWAY AND IT IS PRESERVED AND
COMPND 11 AVAILABLE FROM AN IN-HOUSE COLLECTION AT THE UNIVERSITY OF TROMSO,
COMPND 12 NORWAY (DATABASE INDEX GB04J01).
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THALASSOSPIRA SP. GB04J01;
SOURCE 3 ORGANISM_TAXID: 1485225;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-26B-THAEST2349
KEYWDS HYDROLASE, THALIP2349
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.SANTI,H.-K.S.LEIROS,A.D.SCALA,D.D.PASCALE,B.ALTERMARK,
AUTHOR 2 N.-P.WILLASSEN
REVDAT 1 13-JAN-16 4V2I 0
JRNL AUTH C.D.SANTI,H.-K.S.LEIROS,A.D.SCALA,D.D.PASCALE,B.ALTERMARK,
JRNL AUTH 2 N.-P.WILLASSEN
JRNL TITL BIOCHEMICAL CHARACTERIZATION AND STRUCTURAL ANALYSIS OF A
JRNL TITL 2 NEW COLD-ACTIVE AND SALT TOLERANT ESTERASE FROM THE MARINE
JRNL TITL 3 BACTERIUM THALASSOSPIRA SP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.686
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.866
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.99
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.39
REMARK 3 NUMBER OF REFLECTIONS : 61289
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1451
REMARK 3 R VALUE (WORKING SET) : 0.1431
REMARK 3 FREE R VALUE : 0.1821
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3064
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 24.8687 - 4.7135 0.97 2951 155 0.1318 0.1530
REMARK 3 2 4.7135 - 3.7454 0.99 2893 152 0.1095 0.1313
REMARK 3 3 3.7454 - 3.2731 0.99 2853 151 0.1181 0.1672
REMARK 3 4 3.2731 - 2.9744 1.00 2858 150 0.1306 0.1862
REMARK 3 5 2.9744 - 2.7615 1.00 2847 150 0.1303 0.1842
REMARK 3 6 2.7615 - 2.5989 1.00 2829 149 0.1294 0.1644
REMARK 3 7 2.5989 - 2.4688 1.00 2819 148 0.1290 0.1651
REMARK 3 8 2.4688 - 2.3614 1.00 2818 148 0.1267 0.1679
REMARK 3 9 2.3614 - 2.2706 1.00 2813 149 0.1311 0.1681
REMARK 3 10 2.2706 - 2.1923 0.96 2720 142 0.1614 0.2159
REMARK 3 11 2.1923 - 2.1238 1.00 2815 148 0.1363 0.1769
REMARK 3 12 2.1238 - 2.0631 0.99 2779 146 0.1463 0.1998
REMARK 3 13 2.0631 - 2.0088 1.00 2811 148 0.1471 0.1713
REMARK 3 14 2.0088 - 1.9598 1.00 2790 147 0.1503 0.1833
REMARK 3 15 1.9598 - 1.9153 0.98 2758 146 0.2107 0.2598
REMARK 3 16 1.9153 - 1.8745 0.99 2754 145 0.2180 0.2605
REMARK 3 17 1.8745 - 1.8371 1.00 2779 146 0.2041 0.2460
REMARK 3 18 1.8371 - 1.8024 1.00 2818 148 0.1969 0.2292
REMARK 3 19 1.8024 - 1.7702 1.00 2797 147 0.1997 0.2532
REMARK 3 20 1.7702 - 1.7402 1.00 2794 147 0.1987 0.2287
REMARK 3 21 1.7402 - 1.7122 0.95 1925 102 0.2233 0.2549
REMARK 3 22 1.7122 - 1.6858 0.00 4 0 0.1737 NULL
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) : 0.16
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.008 4964
REMARK 3 ANGLE : 1.177 6808
REMARK 3 CHIRALITY : 0.045 781
REMARK 3 PLANARITY : 0.006 904
REMARK 3 DIHEDRAL : 12.875 1772
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): -20.3966 -39.6192 11.9730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0854 T22: 0.1022
REMARK 3 T33: 0.0888 T12: 0.0179
REMARK 3 T13: 0.0105 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.3744 L22: 0.5947
REMARK 3 L33: 0.2950 L12: 0.2685
REMARK 3 L13: -0.0173 L23: -0.0229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0207 S12: -0.0125 S13: -0.0018
REMARK 3 S21: 0.0029 S22: -0.0424 S23: -0.0324
REMARK 3 S31: 0.0035 S32: 0.0338 S33: 0.0209
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 4V2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-OCT-14.
REMARK 100 THE PDBE ID CODE IS EBI-61957.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-13
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 : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91705
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61330
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.69
REMARK 200 RESOLUTION RANGE LOW (A) : 25.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.62
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.40
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 1QZ3
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN WAS AT 10 MG/ML IN
REMARK 280 50 MM TRIS-HCL PH 8.0, 500 MM NACL AND 10% GLYCEROL.
REMARK 280 RESERVOIR: 25% PEG 3350, 0.2 M MGCL2
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 36.66300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.87350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.71450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.87350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.66300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.71450
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.5 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 1
REMARK 465 LYS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 MET B 1
REMARK 465 LYS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 45 CE
REMARK 480 GLU B 222 CD
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 HG1 THR A 74 O HOH A 2185 1.53
REMARK 500 OE1 GLU A 239 O HOH A 2399 2.19
REMARK 500 OD2 ASP A 274 O HOH A 2437 2.00
REMARK 500 OD1B ASP A 295 O HOH A 2451 2.20
REMARK 500 O SER B 242 O HOH B 2305 2.10
REMARK 500 NE2 GLN B 270 O HOH B 2417 2.17
REMARK 500 O HOH A 2211 O HOH A 2212 2.12
REMARK 500 O HOH A 2216 O HOH A 2262 2.16
REMARK 500 O HOH B 2035 O HOH B 2036 2.18
REMARK 500 O HOH B 2073 O HOH B 2086 2.18
REMARK 500 O HOH B 2216 O HOH B 2217 2.04
REMARK 500 O HOH B 2326 O HOH B 2392 2.12
REMARK 500 O HOH B 2357 O HOH B 2358 2.17
REMARK 500 O HOH B 2391 O HOH B 2394 2.13
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 OE2 GLU B 129 O HOH A 2355 3445 2.17
REMARK 500 OE1 GLU B 222 O HOH A 2087 3445 2.18
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 ALA A 86 48.95 97.71
REMARK 500 TRP A 88 -25.92 70.89
REMARK 500 SER A 158 -120.33 63.08
REMARK 500 TYR A 186 65.23 28.92
REMARK 500 TRP A 206 -64.42 72.91
REMARK 500 SER B 18 19.98 -145.19
REMARK 500 ARG B 76 97.03 -69.75
REMARK 500 ALA B 86 47.27 97.67
REMARK 500 TRP B 88 -28.91 71.75
REMARK 500 SER B 158 -121.34 62.76
REMARK 500 TYR B 186 63.37 30.49
REMARK 500 TRP B 206 -70.16 69.38
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 B1317 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 275 O
REMARK 620 2 HOH B2412 O 91.4
REMARK 620 3 HOH A2444 O 89.0 141.1
REMARK 620 4 HOH B2413 O 134.0 119.9 85.7
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 MG B1317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1318
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE GENE CONTAINS A N-TERMINAL LEADER SEQUENCE (27 AMINO
REMARK 999 ACIDS LONG) THAT WAS NOT INCLUDED IN THE CLONING CONSTRUCT.
REMARK 999 GB KJ365310
DBREF1 4V2I A 2 317 UNP A0A023T3X2_9PROT
DBREF2 4V2I A A0A023T3X2 28 343
DBREF1 4V2I B 2 317 UNP A0A023T3X2_9PROT
DBREF2 4V2I B A0A023T3X2 28 343
SEQADV 4V2I MET A 1 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS A 318 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS A 319 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS A 320 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS A 321 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS A 322 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS A 323 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I MET B 1 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS B 318 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS B 319 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS B 320 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS B 321 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS B 322 UNP A0A023T3X2 EXPRESSION TAG
SEQADV 4V2I HIS B 323 UNP A0A023T3X2 EXPRESSION TAG
SEQRES 1 A 323 MET PRO VAL LEU GLU PRO THR THR GLN LYS PHE ILE ASN
SEQRES 2 A 323 ALA LEU SER ALA SER GLY GLY PRO ALA ILE TYR THR LEU
SEQRES 3 A 323 THR PRO ALA GLU ALA ARG ASP VAL LEU SER GLY ALA GLN
SEQRES 4 A 323 SER GLY GLU ILE ALA LYS PRO ALA VAL ASP ILE THR ASP
SEQRES 5 A 323 THR THR PHE ALA VAL GLY PRO THR GLY ALA THR LYS VAL
SEQRES 6 A 323 ARG ILE ILE ARG PRO GLN GLY ASN THR ASP ARG LEU PRO
SEQRES 7 A 323 VAL ILE VAL TYR PHE HIS GLY ALA GLY TRP VAL MET GLY
SEQRES 8 A 323 ASP THR GLY THR HIS ASP ARG LEU VAL ARG GLU LEU SER
SEQRES 9 A 323 VAL ARG ALA ASN ALA ALA LEU VAL PHE VAL ASP TYR GLU
SEQRES 10 A 323 ARG SER PRO GLU ALA ARG TYR PRO VAL ALA ILE GLU GLN
SEQRES 11 A 323 ASP TYR ALA VAL THR LYS TYR VAL ALA GLU HIS SER GLU
SEQRES 12 A 323 GLN LEU ASN VAL ASP PRO THR ARG LEU ALA ILE ALA GLY
SEQRES 13 A 323 ASP SER VAL GLY GLY ASN MET THR ALA VAL VAL SER LEU
SEQRES 14 A 323 LEU ALA GLN GLU ARG GLY GLY PRO ASP ILE THR ALA GLN
SEQRES 15 A 323 VAL LEU PHE TYR PRO VAL THR ASP ALA ASP PHE ASP ASN
SEQRES 16 A 323 GLY SER TYR THR GLU PHE ALA ASN GLY PRO TRP LEU THR
SEQRES 17 A 323 LYS PRO ALA MET ASP TRP PHE TRP ASN GLN TYR LEU PRO
SEQRES 18 A 323 GLU GLY ILE ASP ARG THR ASP PRO LYS ILE THR PRO ILE
SEQRES 19 A 323 HIS ALA THR SER GLU GLN LEU SER GLY GLN ALA PRO ALA
SEQRES 20 A 323 LEU VAL ILE THR ALA GLU ASN ASP VAL LEU ARG ASP GLU
SEQRES 21 A 323 GLY GLU ALA TYR ALA ARG LYS LEU SER GLN ALA GLY VAL
SEQRES 22 A 323 ASP VAL THR VAL THR ARG TYR ASN GLY THR ILE HIS ASP
SEQRES 23 A 323 PHE VAL MET LEU ASN VAL LEU ALA ASP THR PRO ALA ALA
SEQRES 24 A 323 LYS GLY ALA ILE ALA GLN ALA GLY GLN TYR LEU HIS THR
SEQRES 25 A 323 ALA LEU HIS GLY LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 323 MET PRO VAL LEU GLU PRO THR THR GLN LYS PHE ILE ASN
SEQRES 2 B 323 ALA LEU SER ALA SER GLY GLY PRO ALA ILE TYR THR LEU
SEQRES 3 B 323 THR PRO ALA GLU ALA ARG ASP VAL LEU SER GLY ALA GLN
SEQRES 4 B 323 SER GLY GLU ILE ALA LYS PRO ALA VAL ASP ILE THR ASP
SEQRES 5 B 323 THR THR PHE ALA VAL GLY PRO THR GLY ALA THR LYS VAL
SEQRES 6 B 323 ARG ILE ILE ARG PRO GLN GLY ASN THR ASP ARG LEU PRO
SEQRES 7 B 323 VAL ILE VAL TYR PHE HIS GLY ALA GLY TRP VAL MET GLY
SEQRES 8 B 323 ASP THR GLY THR HIS ASP ARG LEU VAL ARG GLU LEU SER
SEQRES 9 B 323 VAL ARG ALA ASN ALA ALA LEU VAL PHE VAL ASP TYR GLU
SEQRES 10 B 323 ARG SER PRO GLU ALA ARG TYR PRO VAL ALA ILE GLU GLN
SEQRES 11 B 323 ASP TYR ALA VAL THR LYS TYR VAL ALA GLU HIS SER GLU
SEQRES 12 B 323 GLN LEU ASN VAL ASP PRO THR ARG LEU ALA ILE ALA GLY
SEQRES 13 B 323 ASP SER VAL GLY GLY ASN MET THR ALA VAL VAL SER LEU
SEQRES 14 B 323 LEU ALA GLN GLU ARG GLY GLY PRO ASP ILE THR ALA GLN
SEQRES 15 B 323 VAL LEU PHE TYR PRO VAL THR ASP ALA ASP PHE ASP ASN
SEQRES 16 B 323 GLY SER TYR THR GLU PHE ALA ASN GLY PRO TRP LEU THR
SEQRES 17 B 323 LYS PRO ALA MET ASP TRP PHE TRP ASN GLN TYR LEU PRO
SEQRES 18 B 323 GLU GLY ILE ASP ARG THR ASP PRO LYS ILE THR PRO ILE
SEQRES 19 B 323 HIS ALA THR SER GLU GLN LEU SER GLY GLN ALA PRO ALA
SEQRES 20 B 323 LEU VAL ILE THR ALA GLU ASN ASP VAL LEU ARG ASP GLU
SEQRES 21 B 323 GLY GLU ALA TYR ALA ARG LYS LEU SER GLN ALA GLY VAL
SEQRES 22 B 323 ASP VAL THR VAL THR ARG TYR ASN GLY THR ILE HIS ASP
SEQRES 23 B 323 PHE VAL MET LEU ASN VAL LEU ALA ASP THR PRO ALA ALA
SEQRES 24 B 323 LYS GLY ALA ILE ALA GLN ALA GLY GLN TYR LEU HIS THR
SEQRES 25 B 323 ALA LEU HIS GLY LYS HIS HIS HIS HIS HIS HIS
HET MG B1317 1
HET MG A1317 1
HET MG B1318 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 3(MG 2+)
FORMUL 4 HOH *926(H2 O)
HELIX 1 1 GLU A 5 GLY A 19 1 15
HELIX 2 2 ALA A 22 LEU A 26 5 5
HELIX 3 3 THR A 27 GLN A 39 1 13
HELIX 4 4 HIS A 96 ASN A 108 1 13
HELIX 5 5 PRO A 125 HIS A 141 1 17
HELIX 6 6 HIS A 141 ASN A 146 1 6
HELIX 7 7 SER A 158 GLY A 175 1 18
HELIX 8 8 ASN A 195 PHE A 201 1 7
HELIX 9 9 THR A 208 LEU A 220 1 13
HELIX 10 10 THR A 232 ALA A 236 5 5
HELIX 11 11 THR A 237 SER A 242 1 6
HELIX 12 12 LEU A 257 ALA A 271 1 15
HELIX 13 13 LEU A 290 ALA A 294 5 5
HELIX 14 14 THR A 296 GLY A 316 1 21
HELIX 15 15 GLU B 5 GLY B 19 1 15
HELIX 16 16 ALA B 22 LEU B 26 5 5
HELIX 17 17 THR B 27 GLN B 39 1 13
HELIX 18 18 HIS B 96 ASN B 108 1 13
HELIX 19 19 PRO B 125 HIS B 141 1 17
HELIX 20 20 HIS B 141 ASN B 146 1 6
HELIX 21 21 SER B 158 GLY B 175 1 18
HELIX 22 22 ASN B 195 PHE B 201 1 7
HELIX 23 23 THR B 208 LEU B 220 1 13
HELIX 24 24 THR B 232 ALA B 236 5 5
HELIX 25 25 THR B 237 SER B 242 1 6
HELIX 26 26 LEU B 257 ALA B 271 1 15
HELIX 27 27 LEU B 290 ALA B 294 5 5
HELIX 28 28 THR B 296 GLY B 316 1 21
SHEET 1 AA16 VAL A 48 PHE A 55 0
SHEET 2 AA16 THR A 63 PRO A 70 -1 O THR A 63 N PHE A 55
SHEET 3 AA16 ALA A 110 ASP A 115 -1 O LEU A 111 N ILE A 68
SHEET 4 AA16 LEU A 77 PHE A 83 1 O PRO A 78 N ALA A 110
SHEET 5 AA16 VAL A 147 ASP A 157 1 N ASP A 148 O LEU A 77
SHEET 6 AA16 ALA A 181 PHE A 185 1 O ALA A 181 N ILE A 154
SHEET 7 AA16 ALA A 247 ASN A 254 1 O LEU A 248 N LEU A 184
SHEET 8 AA16 VAL A 275 ILE A 284 1 O THR A 276 N VAL A 249
SHEET 9 AA16 VAL B 275 ILE B 284 -1 O VAL B 277 N ASN A 281
SHEET 10 AA16 ALA B 247 ASN B 254 1 O ALA B 247 N THR B 276
SHEET 11 AA16 ALA B 181 PHE B 185 1 O GLN B 182 N LEU B 248
SHEET 12 AA16 VAL B 147 ASP B 157 1 O ILE B 154 N VAL B 183
SHEET 13 AA16 LEU B 77 PHE B 83 1 O LEU B 77 N ASP B 148
SHEET 14 AA16 ALA B 110 VAL B 114 1 O ALA B 110 N ILE B 80
SHEET 15 AA16 THR B 63 PRO B 70 -1 O ARG B 66 N PHE B 113
SHEET 16 AA16 VAL B 48 PHE B 55 -1 O ASP B 49 N ARG B 69
LINK MG MG A1317 OD2 ASP A 255 1555 1555 2.82
LINK MG MG B1317 O VAL B 275 1555 1555 2.70
LINK MG MG B1317 O HOH B2412 1555 1555 2.67
LINK MG MG B1317 O HOH A2444 1555 1555 2.81
LINK MG MG B1317 O HOH B2413 1555 1555 2.69
LINK MG MG B1318 OD2 ASP B 255 1555 1555 2.82
CISPEP 1 SER A 119 PRO A 120 0 1.98
CISPEP 2 TYR A 124 PRO A 125 0 2.79
CISPEP 3 GLY A 176 PRO A 177 0 1.59
CISPEP 4 GLY A 204 PRO A 205 0 10.07
CISPEP 5 SER B 119 PRO B 120 0 6.96
CISPEP 6 TYR B 124 PRO B 125 0 7.23
CISPEP 7 GLY B 176 PRO B 177 0 -1.31
CISPEP 8 GLY B 204 PRO B 205 0 7.99
SITE 1 AC1 6 GLU A 5 HOH A2444 SER B 269 VAL B 275
SITE 2 AC1 6 HOH B2412 HOH B2413
SITE 1 AC2 6 TYR A 186 THR A 251 ALA A 252 ASP A 255
SITE 2 AC2 6 ARG A 258 HOH A2329
SITE 1 AC3 5 TYR B 186 THR B 251 ALA B 252 ASP B 255
SITE 2 AC3 5 ARG B 258
CRYST1 73.326 85.429 91.747 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 0.013638 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010900 0.00000
TER 4767 GLY A 316
TER 9577 GLY B 316
MASTER 425 0 3 28 16 0 6 610504 2 9 50
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