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HEADER HYDROLASE 06-JUL-15 5CE5
TITLE PROBING THE ROLES OF TWO TRYPTOPHANS SURROUNDING THE UNIQUE ZINC
TITLE 2 COORDINATION SITE IN LIPASE FAMILY I.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 31-417;
COMPND 5 SYNONYM: BTL2 LIPASE;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS THERMOCATENULATUS;
SOURCE 3 ORGANISM_TAXID: 33938;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, ZINC, DOMAIN THERMOSTABILITY, THERMOACTIVITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.U.SEZERMAN,A.D.PODJARNY,T.EMEL,A.COUSIDO-SIAH,A.MITSCHLER
REVDAT 1 02-DEC-15 5CE5 0
JRNL AUTH E.TIMUCIN,A.COUSIDO-SIAH,A.MITSCHLER,A.PODJARNY,O.U.SEZERMAN
JRNL TITL PROBING THE ROLES OF TWO TRYPTOPHANS SURROUNDING THE UNIQUE
JRNL TITL 2 ZINC COORDINATION SITE IN LIPASE FAMILY I.5.
JRNL REF PROTEINS 2015
JRNL REFN ESSN 1097-0134
JRNL PMID 26573720
JRNL DOI 10.1002/PROT.24961
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1796
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 40640
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2004
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 45.2917 - 4.8067 1.00 2971 161 0.1618 0.1769
REMARK 3 2 4.8067 - 3.8159 1.00 2857 140 0.1345 0.1898
REMARK 3 3 3.8159 - 3.3337 1.00 2833 140 0.1480 0.1719
REMARK 3 4 3.3337 - 3.0289 0.99 2787 146 0.1552 0.1992
REMARK 3 5 3.0289 - 2.8119 0.99 2859 93 0.1714 0.2243
REMARK 3 6 2.8119 - 2.6461 0.99 2763 147 0.1636 0.1941
REMARK 3 7 2.6461 - 2.5136 0.99 2744 162 0.1650 0.2065
REMARK 3 8 2.5136 - 2.4042 0.99 2765 144 0.1703 0.2334
REMARK 3 9 2.4042 - 2.3116 0.99 2742 156 0.1739 0.2202
REMARK 3 10 2.3116 - 2.2319 0.99 2725 169 0.1799 0.2383
REMARK 3 11 2.2319 - 2.1621 0.99 2758 114 0.1819 0.2254
REMARK 3 12 2.1621 - 2.1003 0.98 2720 138 0.1942 0.2064
REMARK 3 13 2.1003 - 2.0450 0.96 2648 149 0.2118 0.2744
REMARK 3 14 2.0450 - 1.9951 0.90 2464 145 0.2426 0.2695
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.360
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 : 0.007 3179
REMARK 3 ANGLE : 1.022 4310
REMARK 3 CHIRALITY : 0.042 449
REMARK 3 PLANARITY : 0.004 561
REMARK 3 DIHEDRAL : 13.035 1145
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5CE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211465.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40640
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12800
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.12800
REMARK 200 FOR SHELL : 2.125
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: 2W22
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, MPD, AMMONIUM ACETATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 36.65250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.09000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.98150
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.65250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.09000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.98150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.65250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.09000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.98150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.65250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 64.09000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.98150
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: 1560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 730 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 801 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 830 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 846 LIES ON A SPECIAL POSITION.
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 THR A 18 -6.69 72.74
REMARK 500 SER A 114 -122.63 44.62
REMARK 500 TYR A 200 -24.26 79.07
REMARK 500 ARG A 272 45.36 -145.71
REMARK 500 ASN A 305 84.49 -150.61
REMARK 500 ASP A 311 -167.36 -105.99
REMARK 500 ILE A 320 -37.94 -131.22
REMARK 500 LYS A 330 -47.19 -134.61
REMARK 500 ASN A 368 89.23 -168.88
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 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 62 OD1
REMARK 620 2 ASP A 62 OD2 55.6
REMARK 620 3 HIS A 82 NE2 88.1 142.0
REMARK 620 4 HIS A 88 NE2 114.7 99.4 106.6
REMARK 620 5 ASP A 239 OD2 135.7 93.2 108.8 99.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 287 O
REMARK 620 2 GLU A 361 OE2 84.5
REMARK 620 3 ASP A 366 OD2 101.0 111.1
REMARK 620 4 PRO A 367 O 169.8 92.3 89.2
REMARK 620 5 HOH A 790 O 91.2 105.8 142.0 80.3
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 CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P15 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 407
DBREF 5CE5 A 3 389 UNP Q59260 Q59260_9BACI 31 417
SEQADV 5CE5 ALA A 61 UNP Q59260 TRP 89 ENGINEERED MUTATION
SEQADV 5CE5 TYR A 355 UNP Q59260 CYS 383 CONFLICT
SEQRES 1 A 387 SER PRO ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS
SEQRES 2 A 387 GLY PHE THR GLY TRP GLY ARG GLU GLU MET LEU GLY PHE
SEQRES 3 A 387 LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP
SEQRES 4 A 387 LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL
SEQRES 5 A 387 GLY PRO LEU SER SER ASN ALA ASP ARG ALA CYS GLU ALA
SEQRES 6 A 387 TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA
SEQRES 7 A 387 ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG
SEQRES 8 A 387 THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY
SEQRES 9 A 387 ARG VAL HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR
SEQRES 10 A 387 ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN
SEQRES 11 A 387 GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU
SEQRES 12 A 387 SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER
SEQRES 13 A 387 VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU
SEQRES 14 A 387 VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU
SEQRES 15 A 387 GLN LYS ALA VAL LEU LYS ALA ALA ALA VAL ALA SER ASN
SEQRES 16 A 387 VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP
SEQRES 17 A 387 GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP
SEQRES 18 A 387 HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR
SEQRES 19 A 387 SER THR ASP THR ALA ARG TYR ASP LEU SER ILE PRO GLY
SEQRES 20 A 387 ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN
SEQRES 21 A 387 THR TYR TYR LEU SER PHE SER THR GLU ARG THR HIS ARG
SEQRES 22 A 387 GLY ALA LEU THR GLY ASN TYR TYR PRO GLU LEU GLY MET
SEQRES 23 A 387 ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY
SEQRES 24 A 387 SER TYR ARG ASN GLU ALA LEU GLY ILE ASP ASP ARG TRP
SEQRES 25 A 387 LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN
SEQRES 26 A 387 GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR
SEQRES 27 A 387 ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY
SEQRES 28 A 387 THR TYR ASN VAL ASP HIS LEU GLU VAL ILE GLY VAL ASP
SEQRES 29 A 387 PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG
SEQRES 30 A 387 LEU ALA GLU GLN LEU ALA SER LEU ARG PRO
HET CA A 401 1
HET ZN A 402 1
HET P15 A 403 20
HET 1PE A 404 16
HET MPD A 405 8
HET MPD A 406 8
HET MPD A 407 8
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN 1PE PEG400
FORMUL 2 CA CA 2+
FORMUL 3 ZN ZN 2+
FORMUL 4 P15 C13 H28 O7
FORMUL 5 1PE C10 H22 O6
FORMUL 6 MPD 3(C6 H14 O2)
FORMUL 9 HOH *352(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 SER A 114 GLY A 130 1 17
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 170 ASP A 179 1 10
HELIX 11 AB2 ASP A 183 ASN A 197 1 15
HELIX 12 AB3 TYR A 200 TYR A 205 1 6
HELIX 13 AB4 LEU A 209 GLY A 213 5 5
HELIX 14 AB5 SER A 221 ARG A 231 1 11
HELIX 15 AB6 SER A 232 SER A 237 5 6
HELIX 16 AB7 THR A 240 SER A 246 1 7
HELIX 17 AB8 SER A 246 VAL A 257 1 12
HELIX 18 AB9 ASN A 289 CYS A 296 1 8
HELIX 19 AC1 CYS A 296 GLY A 301 1 6
HELIX 20 AC2 ASN A 305 GLY A 309 5 5
HELIX 21 AC3 ASP A 311 LEU A 315 5 5
HELIX 22 AC4 ASN A 322 MET A 326 5 5
HELIX 23 AC5 ASP A 372 LEU A 387 1 16
SHEET 1 AA1 7 THR A 49 THR A 51 0
SHEET 2 AA1 7 ILE A 11 LEU A 14 1 N LEU A 13 O TYR A 50
SHEET 3 AA1 7 VAL 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 LEU A 266 N THR A 161
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 HIS A 274
LINK OD1 ASP A 62 ZN ZN A 402 1555 1555 2.15
LINK OD2 ASP A 62 ZN ZN A 402 1555 1555 2.49
LINK NE2 HIS A 82 ZN ZN A 402 1555 1555 2.03
LINK NE2 HIS A 88 ZN ZN A 402 1555 1555 2.08
LINK OD2 ASP A 239 ZN ZN A 402 1555 1555 1.92
LINK O GLY A 287 CA CA A 401 1555 1555 2.40
LINK OE2 GLU A 361 CA CA A 401 1555 1555 2.34
LINK OD2 ASP A 366 CA CA A 401 1555 1555 2.53
LINK O PRO A 367 CA CA A 401 1555 1555 2.54
LINK CA CA A 401 O HOH A 790 1555 1555 2.58
SITE 1 AC1 5 GLY A 287 GLU A 361 ASP A 366 PRO A 367
SITE 2 AC1 5 HOH A 790
SITE 1 AC2 4 ASP A 62 HIS A 82 HIS A 88 ASP A 239
SITE 1 AC3 9 PHE A 17 LEU A 57 SER A 114 GLN A 115
SITE 2 AC3 9 LEU A 184 LEU A 189 THR A 240 ILE A 320
SITE 3 AC3 9 HIS A 359
SITE 1 AC4 6 THR A 18 MET A 174 THR A 178 PHE A 222
SITE 2 AC4 6 LEU A 360 HOH A 556
SITE 1 AC5 6 THR A 18 LEU A 57 VAL A 188 TYR A 205
SITE 2 AC5 6 PHE A 207 HOH A 504
SITE 1 AC6 4 ASN A 142 VAL A 143 HOH A 573 HOH A 644
SITE 1 AC7 2 ASN A 197 ARG A 216
CRYST1 73.305 128.180 127.963 90.00 90.00 90.00 I 2 2 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 0.013642 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007802 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007815 0.00000
TER 3043 PRO A 389
MASTER 311 0 7 23 11 0 12 6 3456 1 74 30
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