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HEADER HYDROLASE 08-JUL-07 2Z5G
TITLE CRYSTAL STRUCTURE OF T1 LIPASE F16L MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 30-416;
COMPND 5 SYNONYM: T1 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 SP. T1;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PGEX/T1S
KEYWDS LIPASE, CATION-PI INTERACTION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MATSUMURA,T.YAMAMOTO,T.INOUE,Y.KAI
REVDAT 1 30-OCT-07 2Z5G 0
JRNL AUTH H.MATSUMURA,T.YAMAMOTO,T.C.LEOW,T.MORI,A.B.SALLEH,
JRNL AUTH 2 M.BASRI,T.INOUE,Y.KAI,R.N.Z.R.A.RAHMAN
JRNL TITL NOVEL CATION-PI INTERACTION REVEALED BY CRYSTAL
JRNL TITL 2 STRUCTURE OF THERMOALKALOPHILIC LIPASE
JRNL REF PROTEINS 2007
JRNL REFN ASTM PSFGEY US ESSN 1097-0134
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
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) : 32.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 393813.080
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 79386
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4018
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11535
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 626
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6100
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 686
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.50000
REMARK 3 B22 (A**2) : -3.32000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.70000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.140 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.720 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.770 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 52.13
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Z5G COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB027544.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.60
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 ULTRAX 18
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83050
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 32.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.06000
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) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.34400
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2DSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M NACL, 0.1M KH2PO4, 0.1M
REMARK 280 NAH2PO4, 0.1M MES BUFFER, PH 6.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 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 58.89200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.55550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.89200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.55550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 B2205 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2411 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 SER A 113 -137.96 56.41
REMARK 500 VAL A 203 -55.36 68.39
REMARK 500 LEU A 208 38.61 -93.26
REMARK 500 ARG A 271 42.66 -148.79
REMARK 500 LEU A 277 -73.75 -78.72
REMARK 500 ASP A 310 -151.69 -126.26
REMARK 500 ILE A 319 -41.78 -134.58
REMARK 500 LYS A 329 -47.31 -134.42
REMARK 500 ASN A 367 85.16 -168.87
REMARK 500 SER B 113 -135.78 56.51
REMARK 500 PHE B 154 15.26 -154.73
REMARK 500 VAL B 203 -60.93 66.90
REMARK 500 LEU B 208 39.33 -97.59
REMARK 500 ARG B 271 43.46 -150.81
REMARK 500 LEU B 277 -81.46 -79.14
REMARK 500 ASP B 310 -155.64 -117.18
REMARK 500 ILE B 319 -41.10 -137.36
REMARK 500 ASN B 367 86.38 -165.52
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 A2556 DISTANCE = 5.77 ANGSTROMS
DBREF 2Z5G A 2 388 UNP Q842J9 Q842J9_9BACI 30 416
DBREF 2Z5G B 2 388 UNP Q842J9 Q842J9_9BACI 30 416
SEQADV 2Z5G LEU A 16 UNP Q842J9 PHE 44 ENGINEERED
SEQADV 2Z5G LEU B 16 UNP Q842J9 PHE 44 ENGINEERED
SEQRES 1 A 387 SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS
SEQRES 2 A 387 GLY LEU THR GLY TRP GLY ARG GLU GLU MET PHE 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 TRP 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 ILE 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 GLU 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 VAL SER 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 TYR ARG
SEQRES 22 A 387 GLY ALA LEU THR GLY ASN HIS 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 PRO THR 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 ILE 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 GLN PRO
SEQRES 1 B 387 SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS
SEQRES 2 B 387 GLY LEU THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE
SEQRES 3 B 387 LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP
SEQRES 4 B 387 LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL
SEQRES 5 B 387 GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA
SEQRES 6 B 387 TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA
SEQRES 7 B 387 ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG
SEQRES 8 B 387 THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY
SEQRES 9 B 387 ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR
SEQRES 10 B 387 ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN
SEQRES 11 B 387 GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU
SEQRES 12 B 387 SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER
SEQRES 13 B 387 VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU
SEQRES 14 B 387 VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU
SEQRES 15 B 387 GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN
SEQRES 16 B 387 VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP
SEQRES 17 B 387 GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP
SEQRES 18 B 387 HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR
SEQRES 19 B 387 SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY
SEQRES 20 B 387 ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN
SEQRES 21 B 387 THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR ARG
SEQRES 22 B 387 GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET
SEQRES 23 B 387 ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY
SEQRES 24 B 387 SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP ARG TRP
SEQRES 25 B 387 LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN
SEQRES 26 B 387 GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR
SEQRES 27 B 387 ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY
SEQRES 28 B 387 THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP
SEQRES 29 B 387 PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG
SEQRES 30 B 387 LEU ALA GLU GLN LEU ALA SER LEU GLN PRO
HET ZN A2001 1
HET ZN B2002 1
HET CA A2011 1
HET CA B2012 1
HET CL A2201 1
HET CL B2202 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 CA 2(CA 2+)
FORMUL 7 CL 2(CL 1-)
FORMUL 9 HOH *686(H2 O)
HELIX 1 1 GLU A 23 PHE A 27 5 5
HELIX 2 2 ASP A 36 ASN A 44 1 9
HELIX 3 3 SER A 58 GLY A 72 1 15
HELIX 4 4 GLY A 78 GLY A 86 1 9
HELIX 5 5 LEU A 98 GLY A 104 5 7
HELIX 6 6 GLN A 114 GLY A 129 1 16
HELIX 7 7 SER A 130 ASN A 141 1 12
HELIX 8 8 SER A 145 GLU A 149 5 5
HELIX 9 9 THR A 168 MET A 173 5 6
HELIX 10 10 ASP A 175 ALA A 191 1 17
HELIX 11 11 SER A 220 ARG A 230 1 11
HELIX 12 12 SER A 231 SER A 236 1 6
HELIX 13 13 THR A 239 SER A 245 1 7
HELIX 14 14 SER A 245 VAL A 256 1 12
HELIX 15 15 ASN A 288 CYS A 295 1 8
HELIX 16 16 CYS A 295 GLY A 300 1 6
HELIX 17 17 ASP A 310 LEU A 314 5 5
HELIX 18 18 ASN A 321 MET A 325 5 5
HELIX 19 19 ASP A 371 LEU A 386 1 16
HELIX 20 20 GLU B 23 PHE B 27 5 5
HELIX 21 21 GLY B 31 GLY B 35 5 5
HELIX 22 22 ASP B 36 ASN B 44 1 9
HELIX 23 23 SER B 58 GLY B 72 1 15
HELIX 24 24 GLY B 78 GLY B 86 1 9
HELIX 25 25 LEU B 98 ARG B 103 5 6
HELIX 26 26 GLN B 114 GLY B 129 1 16
HELIX 27 27 SER B 130 ASN B 141 1 12
HELIX 28 28 SER B 145 GLU B 149 5 5
HELIX 29 29 THR B 168 MET B 173 5 6
HELIX 30 30 ASP B 175 ALA B 191 1 17
HELIX 31 31 LEU B 208 GLY B 212 5 5
HELIX 32 32 SER B 220 ARG B 230 1 11
HELIX 33 33 SER B 231 SER B 236 1 6
HELIX 34 34 THR B 239 SER B 245 1 7
HELIX 35 35 SER B 245 GLN B 254 1 10
HELIX 36 36 ASN B 288 CYS B 295 1 8
HELIX 37 37 CYS B 295 GLY B 300 1 6
HELIX 38 38 ASN B 304 GLY B 308 5 5
HELIX 39 39 ASP B 310 LEU B 314 5 5
HELIX 40 40 ASN B 321 MET B 325 5 5
HELIX 41 41 ASP B 371 SER B 385 1 15
SHEET 1 A 7 THR A 48 LEU A 51 0
SHEET 2 A 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 A 7 ILE A 107 HIS A 112 1 O ILE A 110 N VAL A 11
SHEET 4 A 7 VAL A 155 ILE A 161 1 O THR A 159 N ALA A 111
SHEET 5 A 7 TYR A 263 THR A 269 1 O LEU A 265 N VAL A 158
SHEET 6 A 7 TRP A 348 TYR A 354 1 O ASN A 349 N TYR A 264
SHEET 7 A 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 B 2 GLY A 73 ASP A 76 0
SHEET 2 B 2 PHE A 90 TYR A 94 -1 O TYR A 94 N GLY A 73
SHEET 1 C 2 THR A 272 ARG A 274 0
SHEET 2 C 2 HIS A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 D 7 THR B 48 LEU B 51 0
SHEET 2 D 7 ILE B 10 LEU B 13 1 N ILE B 10 O TYR B 49
SHEET 3 D 7 ILE B 107 HIS B 112 1 O HIS B 108 N VAL B 11
SHEET 4 D 7 VAL B 155 ILE B 161 1 O THR B 159 N ALA B 111
SHEET 5 D 7 TYR B 263 THR B 269 1 O LEU B 265 N VAL B 158
SHEET 6 D 7 TRP B 348 TYR B 354 1 O ASN B 349 N TYR B 264
SHEET 7 D 7 ILE B 336 PRO B 338 1 N VAL B 337 O TRP B 348
SHEET 1 E 2 GLY B 73 ASP B 76 0
SHEET 2 E 2 PHE B 90 TYR B 94 -1 O TYR B 94 N GLY B 73
SHEET 1 F 2 THR B 272 ARG B 274 0
SHEET 2 F 2 HIS B 281 PRO B 283 -1 O TYR B 282 N TYR B 273
CRYST1 117.784 81.111 99.475 90.00 96.90 90.00 C 1 2 1 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 0.008490 0.000000 0.001028 0.00000
SCALE2 0.000000 0.012329 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010126 0.00000
TER 3051 PRO A 388
TER 6102 PRO B 388
MASTER 280 0 6 41 22 0 0 6 6792 2 0 60
END |