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HEADER HYDROLASE 10-DEC-14 4X85
TITLE CRYSTAL STRUCTURE OF LIPASE FROM GEOBACILLUS STEAROTHERMOPHILUS T6
TITLE 2 METHANOL STABLE VARIANT H86Y/A269T/R374W
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS T6;
SOURCE 3 ORGANISM_TAXID: 646309;
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: PET9A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KANTEEV,A.DROR,S.GIHAZ,A.FISHMAN
REVDAT 1 10-JUN-15 4X85 0
JRNL AUTH A.DROR,M.KANTEEV,I.KAGAN,S.GIHAZ,A.SHAHAR,A.FISHMAN
JRNL TITL STRUCTURAL INSIGHTS INTO METHANOL-STABLE VARIANTS OF LIPASE
JRNL TITL 2 T6 FROM GEOBACILLUS STEAROTHERMOPHILUS.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2015
JRNL REFN ESSN 1432-0614
JRNL PMID 26026940
JRNL DOI 10.1007/S00253-015-6700-4
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 20085
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.230
REMARK 3 FREE R VALUE TEST SET COUNT : 1050
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 24.8496 - 4.3765 0.94 2528 128 0.1827 0.2006
REMARK 3 2 4.3765 - 3.4768 0.94 2426 124 0.1719 0.1988
REMARK 3 3 3.4768 - 3.0382 0.94 2341 168 0.2015 0.2338
REMARK 3 4 3.0382 - 2.7608 0.95 2367 148 0.2187 0.2386
REMARK 3 5 2.7608 - 2.5631 0.94 2366 127 0.2285 0.2746
REMARK 3 6 2.5631 - 2.4121 0.94 2365 117 0.2325 0.2816
REMARK 3 7 2.4121 - 2.2914 0.94 2336 118 0.2229 0.2528
REMARK 3 8 2.2914 - 2.1917 0.92 2306 120 0.2414 0.3213
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 35.39
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.84380
REMARK 3 B22 (A**2) : -4.74040
REMARK 3 B33 (A**2) : 7.58410
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 : 0.020 3210
REMARK 3 ANGLE : 1.291 4375
REMARK 3 CHIRALITY : 0.084 451
REMARK 3 PLANARITY : 0.006 570
REMARK 3 DIHEDRAL : 13.524 1130
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 5:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4746 -8.3861 -17.5857
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.1798
REMARK 3 T33: 0.1710 T12: -0.0411
REMARK 3 T13: 0.0018 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 0.2185 L22: 0.2728
REMARK 3 L33: 0.1488 L12: -0.3183
REMARK 3 L13: 0.2202 L23: -0.1615
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: 0.0464 S13: 0.0019
REMARK 3 S21: -0.0418 S22: -0.1665 S23: -0.1505
REMARK 3 S31: 0.0165 S32: 0.1179 S33: -0.0325
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 87:107)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9782 -17.5155 -13.0059
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.2809
REMARK 3 T33: 0.2878 T12: 0.0128
REMARK 3 T13: 0.0020 T23: 0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 0.1786 L22: 0.2485
REMARK 3 L33: 0.3611 L12: -0.0606
REMARK 3 L13: 0.1023 L23: 0.0966
REMARK 3 S TENSOR
REMARK 3 S11: -0.1062 S12: -0.2294 S13: 0.1438
REMARK 3 S21: 0.0616 S22: -0.1970 S23: -0.0881
REMARK 3 S31: -0.2902 S32: -0.3463 S33: -0.0193
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 108:149)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1020 -22.9633 -10.5067
REMARK 3 T TENSOR
REMARK 3 T11: 0.1630 T22: 0.1479
REMARK 3 T33: 0.1222 T12: -0.0233
REMARK 3 T13: 0.0199 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 0.2236 L22: 0.2609
REMARK 3 L33: -0.0029 L12: -0.2519
REMARK 3 L13: 0.1439 L23: -0.0932
REMARK 3 S TENSOR
REMARK 3 S11: -0.0820 S12: -0.0117 S13: -0.1707
REMARK 3 S21: -0.0974 S22: 0.0338 S23: 0.1649
REMARK 3 S31: 0.0789 S32: -0.0397 S33: -0.0113
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 150:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8221 -10.7945 -26.6709
REMARK 3 T TENSOR
REMARK 3 T11: 0.1673 T22: 0.1616
REMARK 3 T33: 0.1169 T12: -0.0029
REMARK 3 T13: -0.0006 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.0539 L22: 0.5846
REMARK 3 L33: 0.1557 L12: 0.1439
REMARK 3 L13: 0.0362 L23: 0.1015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: 0.0581 S13: 0.0897
REMARK 3 S21: -0.0163 S22: -0.0080 S23: -0.0222
REMARK 3 S31: 0.0077 S32: 0.0274 S33: 0.0034
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 213:254)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6122 -18.5295 -31.1392
REMARK 3 T TENSOR
REMARK 3 T11: 0.1594 T22: 0.1830
REMARK 3 T33: 0.1738 T12: -0.0168
REMARK 3 T13: 0.0167 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.1077 L22: 0.2281
REMARK 3 L33: 0.2658 L12: 0.0287
REMARK 3 L13: 0.0328 L23: 0.1482
REMARK 3 S TENSOR
REMARK 3 S11: -0.0474 S12: -0.0897 S13: -0.1073
REMARK 3 S21: -0.0173 S22: -0.0314 S23: 0.0119
REMARK 3 S31: 0.1326 S32: 0.0581 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 255:360)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2719 -5.1720 -16.1502
REMARK 3 T TENSOR
REMARK 3 T11: 0.1808 T22: 0.1712
REMARK 3 T33: 0.2000 T12: -0.0037
REMARK 3 T13: 0.0173 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.5084 L22: 0.9909
REMARK 3 L33: 0.3179 L12: -0.0132
REMARK 3 L13: 0.1993 L23: -0.1036
REMARK 3 S TENSOR
REMARK 3 S11: 0.0463 S12: 0.0088 S13: 0.0536
REMARK 3 S21: 0.1137 S22: -0.0409 S23: 0.1617
REMARK 3 S31: 0.0063 S32: 0.0227 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 361:395)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9100 3.3134 -7.4772
REMARK 3 T TENSOR
REMARK 3 T11: 0.2568 T22: 0.1686
REMARK 3 T33: 0.1953 T12: -0.0123
REMARK 3 T13: -0.0229 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.4760 L22: 0.2148
REMARK 3 L33: 0.3598 L12: 0.0712
REMARK 3 L13: -0.0674 L23: 0.2765
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: 0.0648 S13: 0.0381
REMARK 3 S21: 0.2288 S22: 0.1533 S23: 0.0101
REMARK 3 S31: -0.0238 S32: -0.0359 S33: 0.0012
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 4X85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205233.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.56
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69491
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
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 (%) : 93.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.29600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CITRATE , 25% PEG3350,
REMARK 280 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 24.84800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.78200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.69550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.78200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.84800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.69550
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 103 34.39 -79.83
REMARK 500 ARG A 104 37.55 -164.80
REMARK 500 SER A 114 -139.01 58.80
REMARK 500 VAL A 204 -57.87 69.00
REMARK 500 LEU A 209 38.00 -87.97
REMARK 500 ARG A 272 47.75 -146.55
REMARK 500 ASP A 311 -163.53 -118.00
REMARK 500 ILE A 320 -43.31 -135.01
REMARK 500 LYS A 330 -50.31 -137.39
REMARK 500 ASP A 351 99.20 -63.81
REMARK 500 HIS A 359 -72.36 -28.94
REMARK 500 ASN A 368 89.94 -161.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 737 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 754 DISTANCE = 5.95 ANGSTROMS
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 62 OD1
REMARK 620 2 ASP A 62 OD2 54.2
REMARK 620 3 HIS A 82 NE2 98.7 152.8
REMARK 620 4 HIS A 88 NE2 116.7 91.3 104.5
REMARK 620 5 ASP A 239 OD1 100.1 102.3 79.0 141.5
REMARK 620 6 ASP A 239 OD2 137.0 92.7 109.7 87.1 56.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 287 O
REMARK 620 2 GLU A 361 OE2 89.9
REMARK 620 3 ASP A 366 OD2 102.9 103.5
REMARK 620 4 PRO A 367 O 167.7 96.2 86.1
REMARK 620 5 HOH A 616 O 82.4 158.4 59.3 95.4
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 ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
DBREF 4X85 A 5 389 UNP Q93A71 Q93A71_GEOSE 34 418
SEQADV 4X85 TYR A 86 UNP Q93A71 HIS 115 ENGINEERED MUTATION
SEQADV 4X85 THR A 269 UNP Q93A71 ALA 298 ENGINEERED MUTATION
SEQADV 4X85 ALA A 323 UNP Q93A71 THR 352 CONFLICT
SEQADV 4X85 TRP A 374 UNP Q93A71 ARG 403 ENGINEERED MUTATION
SEQADV 4X85 HIS A 390 UNP Q93A71 EXPRESSION TAG
SEQADV 4X85 HIS A 391 UNP Q93A71 EXPRESSION TAG
SEQADV 4X85 HIS A 392 UNP Q93A71 EXPRESSION TAG
SEQADV 4X85 HIS A 393 UNP Q93A71 EXPRESSION TAG
SEQADV 4X85 HIS A 394 UNP Q93A71 EXPRESSION TAG
SEQADV 4X85 HIS A 395 UNP Q93A71 EXPRESSION TAG
SEQRES 1 A 391 ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY PHE
SEQRES 2 A 391 THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS TYR
SEQRES 3 A 391 TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU ASN
SEQRES 4 A 391 ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY PRO
SEQRES 5 A 391 LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR ALA
SEQRES 6 A 391 GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA HIS
SEQRES 7 A 391 ALA ALA LYS TYR GLY HIS ALA ARG PHE GLY ARG THR TYR
SEQRES 8 A 391 PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG ILE
SEQRES 9 A 391 HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA ARG
SEQRES 10 A 391 MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU GLU
SEQRES 11 A 391 ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER PRO
SEQRES 12 A 391 LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL THR
SEQRES 13 A 391 THR ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL ASN
SEQRES 14 A 391 MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN LYS
SEQRES 15 A 391 ALA VAL LEU LYS ALA ALA ALA VAL ALA SER ASN VAL PRO
SEQRES 16 A 391 TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN TRP
SEQRES 17 A 391 GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP GLN TYR
SEQRES 18 A 391 PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER THR
SEQRES 19 A 391 ASP THR ALA ARG TYR ASP LEU SER VAL PRO GLY ALA GLU
SEQRES 20 A 391 LYS LEU ASN GLN TRP VAL LYS ALA SER PRO ASN THR TYR
SEQRES 21 A 391 TYR LEU SER PHE THR THR GLU ARG THR TYR ARG GLY ALA
SEQRES 22 A 391 LEU THR GLY ASN TYR TYR PRO GLU LEU GLY MET ASN ALA
SEQRES 23 A 391 PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER TYR
SEQRES 24 A 391 ARG ASN ALA THR LEU GLY ILE ASP ASP ARG TRP LEU GLU
SEQRES 25 A 391 ASN ASP GLY ILE VAL ASN ALA PHE SER MET ASN GLY PRO
SEQRES 26 A 391 LYS ARG GLY SER THR ASP ARG ILE VAL PRO TYR ASP GLY
SEQRES 27 A 391 THR ILE LYS LYS GLY VAL TRP ASN ASP MET GLY THR TYR
SEQRES 28 A 391 ASN VAL ASP HIS LEU GLU VAL ILE GLY VAL ASP PRO ASN
SEQRES 29 A 391 PRO LEU PHE ASP ILE TRP ALA PHE TYR LEU ARG LEU ALA
SEQRES 30 A 391 GLU GLN LEU ALA SER LEU GLN PRO HIS HIS HIS HIS HIS
SEQRES 31 A 391 HIS
HET ZN A 401 1
HET CA A 402 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CA CA 2+
FORMUL 4 HOH *259(H2 O)
HELIX 1 AA1 GLU A 24 PHE A 28 5 5
HELIX 2 AA2 ASP A 37 ASN A 45 1 9
HELIX 3 AA3 SER A 59 GLY A 73 1 15
HELIX 4 AA4 GLY A 79 GLY A 87 1 9
HELIX 5 AA5 LEU A 99 GLY A 105 5 7
HELIX 6 AA6 GLN A 115 GLY A 130 1 16
HELIX 7 AA7 SER A 131 ASN A 142 1 12
HELIX 8 AA8 SER A 146 GLU A 150 5 5
HELIX 9 AA9 THR A 169 MET A 174 5 6
HELIX 10 AB1 ASP A 176 ALA A 192 1 17
HELIX 11 AB2 LEU A 209 GLY A 213 5 5
HELIX 12 AB3 SER A 221 ARG A 231 1 11
HELIX 13 AB4 SER A 232 SER A 237 1 6
HELIX 14 AB5 THR A 240 SER A 246 1 7
HELIX 15 AB6 SER A 246 GLN A 255 1 10
HELIX 16 AB7 ASN A 289 CYS A 296 1 8
HELIX 17 AB8 CYS A 296 GLY A 301 1 6
HELIX 18 AB9 ASP A 311 LEU A 315 5 5
HELIX 19 AC1 ASN A 322 MET A 326 5 5
HELIX 20 AC2 ASP A 358 VAL A 362 5 5
HELIX 21 AC3 ASP A 372 ALA A 385 1 14
SHEET 1 AA1 7 THR A 49 LEU A 52 0
SHEET 2 AA1 7 ILE A 11 LEU A 14 1 N ILE A 11 O TYR A 50
SHEET 3 AA1 7 ILE A 108 HIS A 113 1 O HIS A 109 N VAL A 12
SHEET 4 AA1 7 VAL A 156 ILE A 162 1 O THR A 160 N ALA A 112
SHEET 5 AA1 7 TYR A 264 THR A 270 1 O PHE A 268 N THR A 161
SHEET 6 AA1 7 TRP A 349 TYR A 355 1 O TYR A 355 N THR A 269
SHEET 7 AA1 7 ILE A 337 PRO A 339 1 N VAL A 338 O TRP A 349
SHEET 1 AA2 2 GLY A 74 ASP A 77 0
SHEET 2 AA2 2 PHE A 91 TYR A 95 -1 O ARG A 93 N VAL A 76
SHEET 1 AA3 2 THR A 273 ARG A 275 0
SHEET 2 AA3 2 TYR A 282 PRO A 284 -1 O TYR A 283 N TYR A 274
LINK OD1 ASP A 62 ZN ZN A 401 1555 1555 2.05
LINK OD2 ASP A 62 ZN ZN A 401 1555 1555 2.63
LINK NE2 HIS A 82 ZN ZN A 401 1555 1555 2.09
LINK NE2 HIS A 88 ZN ZN A 401 1555 1555 2.14
LINK OD1 ASP A 239 ZN ZN A 401 1555 1555 2.39
LINK OD2 ASP A 239 ZN ZN A 401 1555 1555 2.10
LINK O GLY A 287 CA CA A 402 1555 1555 2.27
LINK OE2 GLU A 361 CA CA A 402 1555 1555 1.97
LINK OD2 ASP A 366 CA CA A 402 1555 1555 2.46
LINK O PRO A 367 CA CA A 402 1555 1555 2.38
LINK CA CA A 402 O HOH A 616 1555 1555 2.49
SITE 1 AC1 4 ASP A 62 HIS A 82 HIS A 88 ASP A 239
SITE 1 AC2 5 GLY A 287 GLU A 361 ASP A 366 PRO A 367
SITE 2 AC2 5 HOH A 616
CRYST1 49.696 71.391 113.564 90.00 90.00 90.00 P 21 21 21 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 0.020122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014007 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008806 0.00000
TER 3109 HIS A 395
MASTER 382 0 2 21 11 0 3 6 3369 1 15 31
END |