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HEADER HYDROLASE 14-MAR-18 6FZD
TITLE CRYSTAL STRUCTURE OF LIPASE FROM GEOBACILLUS STEAROTHERMOPHILUS T6
TITLE 2 VARIANT L184F/A187F/L360F
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 6FZD 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 37486
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1873
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 45.6424 - 4.2314 0.98 2928 151 0.1954 0.1884
REMARK 3 2 4.2314 - 3.3589 0.99 2792 152 0.1871 0.2063
REMARK 3 3 3.3589 - 2.9344 0.99 2764 145 0.2117 0.2358
REMARK 3 4 2.9344 - 2.6661 0.99 2755 144 0.2283 0.2139
REMARK 3 5 2.6661 - 2.4750 0.97 2656 140 0.2253 0.2381
REMARK 3 6 2.4750 - 2.3291 0.99 2749 141 0.2166 0.2526
REMARK 3 7 2.3291 - 2.2125 0.99 2695 146 0.2102 0.2236
REMARK 3 8 2.2125 - 2.1162 0.99 2727 147 0.2165 0.2507
REMARK 3 9 2.1162 - 2.0347 0.99 2705 156 0.2165 0.2487
REMARK 3 10 2.0347 - 1.9645 0.99 2689 133 0.2244 0.2943
REMARK 3 11 1.9645 - 1.9031 0.99 2721 144 0.2245 0.2382
REMARK 3 12 1.9031 - 1.8487 0.99 2713 120 0.2376 0.2891
REMARK 3 13 1.8487 - 1.8000 1.00 2719 154 0.2638 0.2875
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.060
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 : 0.028 3212
REMARK 3 ANGLE : 1.714 4366
REMARK 3 CHIRALITY : 0.287 449
REMARK 3 PLANARITY : 0.009 574
REMARK 3 DIHEDRAL : 15.057 1135
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): -10.4492 9.7340 -18.1770
REMARK 3 T TENSOR
REMARK 3 T11: 0.0893 T22: 0.0928
REMARK 3 T33: 0.0894 T12: -0.0161
REMARK 3 T13: -0.0036 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.5504 L22: 0.8298
REMARK 3 L33: 0.4055 L12: -0.1577
REMARK 3 L13: 0.0149 L23: 0.0984
REMARK 3 S TENSOR
REMARK 3 S11: -0.0193 S12: -0.0254 S13: -0.0255
REMARK 3 S21: 0.0769 S22: -0.0083 S23: -0.0109
REMARK 3 S31: 0.0264 S32: -0.0180 S33: 0.0268
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 6FZD 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_1200009182.
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 : 37550
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 45.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
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 (%): 45.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CITRATE, 25% 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 24.93000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.58350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.44050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.58350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.44050
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: 15410 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 765 O HOH A 770 1.84
REMARK 500 O HOH A 514 O HOH A 523 2.01
REMARK 500 O HOH A 717 O HOH A 725 2.11
REMARK 500 OD2 ASP A 358 N GLU A 361 2.16
REMARK 500 CD ARG A 93 OD2 ASP A 210 2.18
REMARK 500 O HOH A 705 O HOH A 722 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 VAL A 54 -167.80 -124.99
REMARK 500 SER A 114 -139.95 53.98
REMARK 500 ASP A 176 30.86 -98.31
REMARK 500 ALA A 193 33.60 73.32
REMARK 500 VAL A 204 -57.44 74.02
REMARK 500 LEU A 209 40.64 -97.59
REMARK 500 ARG A 272 44.90 -141.80
REMARK 500 ILE A 320 -38.80 -134.70
REMARK 500 LYS A 330 -49.35 -132.00
REMARK 500 ASN A 368 86.31 -173.11
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 769 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 770 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 771 DISTANCE = 6.24 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 51.9
REMARK 620 3 HIS A 82 NE2 100.4 152.2
REMARK 620 4 HIS A 88 NE2 115.6 87.9 106.0
REMARK 620 5 ASP A 239 OD2 130.2 97.1 104.3 98.1
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 ASP A 366 OD2 90.8
REMARK 620 3 PRO A 367 O 168.0 87.0
REMARK 620 4 HOH A 705 O 83.9 112.8 86.0
REMARK 620 5 HOH A 722 O 82.6 159.8 95.5 47.7
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
REMARK 900 RELATED ID: 6FZA RELATED DB: PDB
REMARK 900 RELATED ID: 6FZC RELATED DB: PDB
DBREF 6FZD A 4 389 UNP Q93A71 Q93A71_GEOSE 33 418
SEQADV 6FZD PHE A 184 UNP Q93A71 LEU 213 ENGINEERED MUTATION
SEQADV 6FZD PHE A 187 UNP Q93A71 ALA 216 ENGINEERED MUTATION
SEQADV 6FZD ALA A 323 UNP Q93A71 THR 352 CONFLICT
SEQADV 6FZD PHE A 360 UNP Q93A71 LEU 389 ENGINEERED MUTATION
SEQADV 6FZD HIS A 390 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZD HIS A 391 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZD HIS A 392 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZD HIS A 393 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZD HIS A 394 UNP Q93A71 EXPRESSION TAG
SEQADV 6FZD HIS A 395 UNP Q93A71 EXPRESSION TAG
SEQRES 1 A 392 SER ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY
SEQRES 2 A 392 PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS
SEQRES 3 A 392 TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU
SEQRES 4 A 392 ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY
SEQRES 5 A 392 PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR
SEQRES 6 A 392 ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA
SEQRES 7 A 392 HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG THR
SEQRES 8 A 392 TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG
SEQRES 9 A 392 ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA
SEQRES 10 A 392 ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU
SEQRES 11 A 392 GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER
SEQRES 12 A 392 PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL
SEQRES 13 A 392 THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL
SEQRES 14 A 392 ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP PHE GLN
SEQRES 15 A 392 LYS PHE VAL LEU LYS ALA ALA ALA VAL ALA SER ASN VAL
SEQRES 16 A 392 PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN
SEQRES 17 A 392 TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP GLN
SEQRES 18 A 392 TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER
SEQRES 19 A 392 THR ASP THR ALA ARG TYR ASP LEU SER VAL PRO GLY ALA
SEQRES 20 A 392 GLU LYS LEU ASN GLN TRP VAL LYS ALA SER PRO ASN THR
SEQRES 21 A 392 TYR TYR LEU SER PHE ALA THR GLU ARG THR TYR ARG GLY
SEQRES 22 A 392 ALA LEU THR GLY ASN TYR TYR PRO GLU LEU GLY MET ASN
SEQRES 23 A 392 ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER
SEQRES 24 A 392 TYR ARG ASN ALA THR LEU GLY ILE ASP ASP ARG TRP LEU
SEQRES 25 A 392 GLU ASN ASP GLY ILE VAL ASN ALA PHE SER MET ASN GLY
SEQRES 26 A 392 PRO LYS ARG GLY SER THR ASP ARG ILE VAL PRO TYR ASP
SEQRES 27 A 392 GLY THR ILE LYS LYS GLY VAL TRP ASN ASP MET GLY THR
SEQRES 28 A 392 TYR ASN VAL ASP HIS PHE GLU VAL ILE GLY VAL ASP PRO
SEQRES 29 A 392 ASN PRO LEU PHE ASP ILE ARG ALA PHE TYR LEU ARG LEU
SEQRES 30 A 392 ALA GLU GLN LEU ALA SER LEU GLN PRO HIS HIS HIS HIS
SEQRES 31 A 392 HIS 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 *271(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 SER A 221 ARG A 231 1 11
HELIX 12 AB3 SER A 232 SER A 237 1 6
HELIX 13 AB4 THR A 240 SER A 246 1 7
HELIX 14 AB5 SER A 246 GLN A 255 1 10
HELIX 15 AB6 ASN A 289 VAL A 294 1 6
HELIX 16 AB7 VAL A 295 GLY A 301 1 7
HELIX 17 AB8 ASP A 311 LEU A 315 5 5
HELIX 18 AB9 ASN A 322 MET A 326 5 5
HELIX 19 AC1 ASP A 372 SER A 386 1 15
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 ILE A 111 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 LEU A 266 N THR A 161
SHEET 6 AA1 7 TRP A 349 TYR A 355 1 O TYR A 355 N ALA 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 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 2.14
LINK OD2 ASP A 62 ZN ZN A 401 1555 1555 2.68
LINK NE2 HIS A 82 ZN ZN A 401 1555 1555 2.18
LINK NE2 HIS A 88 ZN ZN A 401 1555 1555 2.18
LINK OD2 ASP A 239 ZN ZN A 401 1555 1555 1.91
LINK O GLY A 287 CA CA A 402 1555 1555 2.26
LINK OD2 ASP A 366 CA CA A 402 1555 1555 2.58
LINK O PRO A 367 CA CA A 402 1555 1555 2.47
LINK CA CA A 402 O HOH A 705 1555 1555 2.44
LINK CA CA A 402 O HOH A 722 1555 1555 2.89
SITE 1 AC1 4 ASP A 62 HIS A 82 HIS A 88 ASP A 239
SITE 1 AC2 6 GLY A 287 GLU A 361 ASP A 366 PRO A 367
SITE 2 AC2 6 HOH A 705 HOH A 722
CRYST1 49.860 70.881 113.167 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 0.020056 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014108 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008836 0.00000
TER 3120 HIS A 395
MASTER 318 0 2 19 11 0 3 6 3392 1 14 31
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