| 6fza-pdb | HEADER HYDROLASE 14-MAR-18 6FZA
TITLE CRYSTAL STRUCTURE OF LIPASE FROM GEOBACILLUS STEAROTHERMOPHILUS T6
TITLE 2 METHANOL STABLE VARIANT A187F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS LIPASE, METHANOL, ORGANIC SOLVENT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GIHAZ,M.KANTEEV,Y.PAZY,A.FISHMAN
REVDAT 1 17-OCT-18 6FZA 0
JRNL AUTH S.GIHAZ,M.KANTEEV,Y.PAZY,A.FISHMAN
JRNL TITL FILLING THE VOID: INTRODUCING AROMATIC INTERACTIONS INTO
JRNL TITL 2 SOLVENT TUNNELS TOWARDS LIPASE STABILITY IN METHANOL.
JRNL REF APPL. ENVIRON. MICROBIOL. 2018
JRNL REFN ESSN 1098-5336
JRNL PMID 30217852
JRNL DOI 10.1128/AEM.02143-18
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 35290
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 1733
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 38.2190 - 4.0051 1.00 3437 176 0.2034 0.2071
REMARK 3 2 4.0051 - 3.1795 1.00 3289 163 0.2035 0.2107
REMARK 3 3 3.1795 - 2.7777 0.97 3142 171 0.2218 0.2409
REMARK 3 4 2.7777 - 2.5238 0.98 3186 158 0.2238 0.2633
REMARK 3 5 2.5238 - 2.3429 0.95 3021 166 0.2220 0.2285
REMARK 3 6 2.3429 - 2.2048 0.87 2814 144 0.2186 0.2486
REMARK 3 7 2.2048 - 2.0944 0.82 2636 120 0.2215 0.2038
REMARK 3 8 2.0944 - 2.0032 0.79 2510 146 0.2245 0.2554
REMARK 3 9 2.0032 - 1.9261 0.77 2465 130 0.2231 0.2298
REMARK 3 10 1.9261 - 1.8596 0.75 2400 123 0.2315 0.2974
REMARK 3 11 1.8596 - 1.8015 0.74 2352 117 0.2474 0.2782
REMARK 3 12 1.8015 - 1.7500 0.73 2305 119 0.2542 0.2779
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.030 3198
REMARK 3 ANGLE : 1.786 4348
REMARK 3 CHIRALITY : 0.146 450
REMARK 3 PLANARITY : 0.010 571
REMARK 3 DIHEDRAL : 14.738 1133
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): -10.5707 10.1834 -18.0661
REMARK 3 T TENSOR
REMARK 3 T11: 0.0926 T22: 0.0993
REMARK 3 T33: 0.0987 T12: -0.0207
REMARK 3 T13: -0.0061 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.5907 L22: 0.9684
REMARK 3 L33: 0.5805 L12: -0.1939
REMARK 3 L13: 0.1318 L23: 0.0762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0197 S12: -0.0300 S13: -0.0039
REMARK 3 S21: 0.0186 S22: -0.0087 S23: -0.0174
REMARK 3 S31: 0.0175 S32: 0.0158 S33: 0.0232
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 6FZA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009175.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-17
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35332
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 45.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
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 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: PHASER
REMARK 200 STARTING MODEL: 4X6U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM FORMATE, 20% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 24.73550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.11150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.63000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.11150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.73550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.63000
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 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: 15420 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: 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 O HOH A 683 O HOH A 697 1.88
REMARK 500 O HOH A 534 O HOH A 691 1.89
REMARK 500 O HOH A 680 O HOH A 688 1.90
REMARK 500 O HOH A 607 O HOH A 612 2.12
REMARK 500 O HOH A 520 O HOH A 665 2.13
REMARK 500 O HOH A 507 O HOH A 519 2.14
REMARK 500 O HOH A 651 O HOH A 658 2.16
REMARK 500 O HOH A 507 O HOH A 616 2.19
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 SER A 114 -134.44 59.21
REMARK 500 VAL A 204 -56.66 67.87
REMARK 500 LEU A 209 47.00 -96.26
REMARK 500 ASN A 305 95.56 -164.98
REMARK 500 ASP A 311 -163.82 -117.59
REMARK 500 ILE A 320 -37.56 -139.13
REMARK 500 LYS A 330 -45.79 -134.50
REMARK 500 ASN A 368 82.91 -168.99
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 703 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A 704 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH A 705 DISTANCE = 6.79 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 52.6
REMARK 620 3 HIS A 82 NE2 95.7 147.2
REMARK 620 4 HIS A 88 NE2 117.1 93.8 110.4
REMARK 620 5 ASP A 239 OD2 126.5 92.4 103.2 102.3
REMARK 620 N 1 2 3 4
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 99.8
REMARK 620 3 ASP A 366 OD2 90.2 102.0
REMARK 620 4 PRO A 367 O 162.3 96.9 80.6
REMARK 620 5 HOH A 667 O 93.9 93.2 163.3 90.9
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
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4X6U RELATED DB: PDB
REMARK 900 RELATED ID: 6FZ1 RELATED DB: PDB
REMARK 900 RELATED ID: 6FZ7 RELATED DB: PDB
REMARK 900 RELATED ID: 6FZ8 RELATED DB: PDB
REMARK 900 RELATED ID: 6FZ9 RELATED DB: PDB
DBREF 6FZA A 5 389 UNP Q93A71 Q93A71_GEOSE 34 418
SEQADV 6FZA PHE A 187 UNP Q93A71 ALA 216 ENGINEERED MUTATION
SEQADV 6FZA ALA A 323 UNP Q93A71 THR 352 CONFLICT
SEQADV 6FZA HIS A 390 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZA HIS A 391 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZA HIS A 392 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZA HIS A 393 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZA HIS A 394 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZA 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 HIS 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 PHE 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 ALA 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 ARG 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 *205(H2 O)
HELIX 1 AA1 GLU A 24 PHE A 28 5 5
HELIX 2 AA2 GLY A 32 GLY A 36 5 5
HELIX 3 AA3 ASP A 37 ASN A 45 1 9
HELIX 4 AA4 SER A 59 GLY A 73 1 15
HELIX 5 AA5 GLY A 79 GLY A 87 1 9
HELIX 6 AA6 LEU A 99 GLY A 105 5 7
HELIX 7 AA7 GLN A 115 GLY A 130 1 16
HELIX 8 AA8 SER A 131 ASN A 142 1 12
HELIX 9 AA9 SER A 146 GLU A 150 5 5
HELIX 10 AB1 THR A 169 MET A 174 5 6
HELIX 11 AB2 ASP A 176 ALA A 192 1 17
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 LEU A 245 1 6
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 LEU A 360 GLY A 364 5 5
HELIX 21 AC3 ASP A 372 SER A 386 1 15
SHEET 1 AA1 7 THR A 49 THR A 51 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 TYR A 264 N LEU A 157
SHEET 6 AA1 7 TRP A 349 TYR A 355 1 O ASN A 350 N TYR A 265
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 TYR A 95 N GLY A 74
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 2.08
LINK OD2 ASP A 62 ZN ZN A 401 1555 1555 2.66
LINK NE2 HIS A 82 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 88 ZN ZN A 401 1555 1555 2.19
LINK OD2 ASP A 239 ZN ZN A 401 1555 1555 1.85
LINK O GLY A 287 CA CA A 402 1555 1555 2.35
LINK OE2 GLU A 361 CA CA A 402 1555 1555 2.27
LINK OD2 ASP A 366 CA CA A 402 1555 1555 2.63
LINK O PRO A 367 CA CA A 402 1555 1555 2.49
LINK CA CA A 402 O HOH A 667 1555 1555 2.29
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 667
CRYST1 49.471 71.260 112.223 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 0.020214 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014033 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008911 0.00000
TER 3108 HIS A 395
MASTER 315 0 2 21 11 0 3 6 3314 1 14 31
END
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