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HEADER HYDROLASE 18-JAN-02 1KU0
TITLE STRUCTURE OF THE BACILLUS STEAROTHERMOPHILUS L1 LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L1 LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 30-417(SEQ DB NUMBER);
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS HYDROLASE, LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-T.JEONG,H.-K.KIM,S.-J.KIM,S.-W.CHI,J.-G.PAN,T.-K.OH,S.-
AUTHOR 2 E.RYU
REVDAT 1 21-AUG-02 1KU0 0
JRNL AUTH S.-T.JEONG,H.-K.KIM,S.-J.KIM,S.-W.CHI,J.-G.PAN,
JRNL AUTH 2 T.-K.OH,S.-E.RYU
JRNL TITL NOVEL ZINC-BINDING CENTER AND A TEMPERATURE SWITCH
JRNL TITL 2 IN THE BACILLUS STEAROTHERMOPHILUS L1 LIPASE
JRNL REF J.BIOL.CHEM. V. 277 17041 2002
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 60432
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3206
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 257
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KU0 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JAN-2002.
REMARK 100 THE RCSB ID CODE IS RCSB015343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 59.81000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.52000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.81000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.52000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA B 1001
REMARK 465 SER B 1002
REMARK 465 PRO B 1003
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 121 CE MET A 121 SD -0.047
REMARK 500 MET A 173 CE MET A 173 SD -0.049
REMARK 500 MET A 325 CE MET A 325 SD 0.046
REMARK 500 MET A 351 CE MET A 351 SD -0.083
REMARK 500 MET B1325 CE MET B1325 SD -0.169
REMARK 500 MET B1351 CE MET B1351 SD -0.099
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 17 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 GLY A 86 N - CA - C ANGL. DEV. = 7.0 DEGREES
REMARK 500 LEU A 252 CA - CB - CG ANGL. DEV. = 10.1 DEGREES
REMARK 500 ALA A 289 N - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 VAL A 294 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 CYS A 295 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 ILE A 309 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 MET A 325 N - CA - C ANGL. DEV. = 13.6 DEGREES
REMARK 500 THR B1017 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 PHE B1027 N - CA - C ANGL. DEV. = -7.0 DEGREES
REMARK 500 GLY B1086 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 ILE B1110 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 THR B1235 N - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 LEU B1252 CA - CB - CG ANGL. DEV. = 11.7 DEGREES
REMARK 500 LEU B1285 CA - CB - CG ANGL. DEV. = 7.0 DEGREES
REMARK 500 VAL B1294 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 CYS B1295 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU B1299 CA - CB - CG ANGL. DEV. = 7.2 DEGREES
REMARK 500 MET B1325 N - CA - C ANGL. DEV. = 15.4 DEGREES
DBREF 1KU0 A 1 388 SWS O66015 O66015 30 417
DBREF 1KU0 B 1001 1388 SWS O66015 O66015 30 417
SEQADV 1KU0 LYS A 84 SWS O66015 ASN 113 CONFLICT
SEQADV 1KU0 HIS A 85 SWS O66015 ASP 114 CONFLICT
SEQADV 1KU0 ASN A 355 SWS O66015 LYS 384 CONFLICT
SEQADV 1KU0 LYS B 1084 SWS O66015 ASN 113 CONFLICT
SEQADV 1KU0 HIS B 1085 SWS O66015 ASP 114 CONFLICT
SEQADV 1KU0 ASN B 1355 SWS O66015 LYS 384 CONFLICT
SEQRES 1 A 388 ALA SER PRO ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU
SEQRES 2 A 388 HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET LEU GLY
SEQRES 3 A 388 PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN
SEQRES 4 A 388 TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA
SEQRES 5 A 388 VAL GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU
SEQRES 6 A 388 ALA TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY
SEQRES 7 A 388 ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY
SEQRES 8 A 388 ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY
SEQRES 9 A 388 GLY ARG VAL HIS ILE ILE ALA HIS SER GLN GLY GLY GLN
SEQRES 10 A 388 THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER
SEQRES 11 A 388 GLN GLU GLU ARG GLU TYR ALA LYS GLU HIS ASN VAL SER
SEQRES 12 A 388 LEU SER PRO LEU PHE GLU GLY GLY HIS ARG PHE VAL LEU
SEQRES 13 A 388 SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR
SEQRES 14 A 388 LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP
SEQRES 15 A 388 LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER
SEQRES 16 A 388 ASN ALA PRO TYR THR SER GLU ILE TYR ASP PHE LYS LEU
SEQRES 17 A 388 ASP GLN TRP GLY LEU ARG ARG GLU PRO GLY GLU SER PHE
SEQRES 18 A 388 ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP
SEQRES 19 A 388 THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL PRO
SEQRES 20 A 388 GLY ALA GLU THR LEU ASN ARG TRP VAL LYS ALA SER PRO
SEQRES 21 A 388 ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR
SEQRES 22 A 388 ARG GLY ALA LEU THR GLY ASN TYR TYR PRO GLU LEU GLY
SEQRES 23 A 388 MET ASN ALA PHE SER ALA ILE VAL CYS ALA PRO PHE LEU
SEQRES 24 A 388 GLY SER TYR ARG ASN ALA ALA LEU GLY ILE ASP SER HIS
SEQRES 25 A 388 TRP LEU GLY ASN ASP GLY ILE VAL ASN THR ILE SER MET
SEQRES 26 A 388 ASN GLY PRO LYS ARG GLY SER ASN ASP ARG ILE VAL PRO
SEQRES 27 A 388 TYR ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET
SEQRES 28 A 388 GLY THR TYR ASN VAL ASP HIS LEU GLU VAL ILE GLY VAL
SEQRES 29 A 388 ASP PRO ASN PRO SER PHE ASN ILE ARG ALA PHE TYR LEU
SEQRES 30 A 388 ARG LEU ALA GLU GLN LEU ALA SER LEU ARG PRO
SEQRES 1 B 388 ALA SER PRO ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU
SEQRES 2 B 388 HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET LEU GLY
SEQRES 3 B 388 PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN
SEQRES 4 B 388 TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA
SEQRES 5 B 388 VAL GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU
SEQRES 6 B 388 ALA TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY
SEQRES 7 B 388 ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY
SEQRES 8 B 388 ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY
SEQRES 9 B 388 GLY ARG VAL HIS ILE ILE ALA HIS SER GLN GLY GLY GLN
SEQRES 10 B 388 THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER
SEQRES 11 B 388 GLN GLU GLU ARG GLU TYR ALA LYS GLU HIS ASN VAL SER
SEQRES 12 B 388 LEU SER PRO LEU PHE GLU GLY GLY HIS ARG PHE VAL LEU
SEQRES 13 B 388 SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR
SEQRES 14 B 388 LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP
SEQRES 15 B 388 LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER
SEQRES 16 B 388 ASN ALA PRO TYR THR SER GLU ILE TYR ASP PHE LYS LEU
SEQRES 17 B 388 ASP GLN TRP GLY LEU ARG ARG GLU PRO GLY GLU SER PHE
SEQRES 18 B 388 ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP
SEQRES 19 B 388 THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL PRO
SEQRES 20 B 388 GLY ALA GLU THR LEU ASN ARG TRP VAL LYS ALA SER PRO
SEQRES 21 B 388 ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR
SEQRES 22 B 388 ARG GLY ALA LEU THR GLY ASN TYR TYR PRO GLU LEU GLY
SEQRES 23 B 388 MET ASN ALA PHE SER ALA ILE VAL CYS ALA PRO PHE LEU
SEQRES 24 B 388 GLY SER TYR ARG ASN ALA ALA LEU GLY ILE ASP SER HIS
SEQRES 25 B 388 TRP LEU GLY ASN ASP GLY ILE VAL ASN THR ILE SER MET
SEQRES 26 B 388 ASN GLY PRO LYS ARG GLY SER ASN ASP ARG ILE VAL PRO
SEQRES 27 B 388 TYR ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET
SEQRES 28 B 388 GLY THR TYR ASN VAL ASP HIS LEU GLU VAL ILE GLY VAL
SEQRES 29 B 388 ASP PRO ASN PRO SER PHE ASN ILE ARG ALA PHE TYR LEU
SEQRES 30 B 388 ARG LEU ALA GLU GLN LEU ALA SER LEU ARG PRO
HET ZN2 A 701 1
HET ZN2 B 702 1
HET CA A 703 1
HET CA B 704 1
HETNAM ZN2 ZINC ION ON 3-FOLD CRYSTAL AXIS
HETNAM CA CALCIUM ION
FORMUL 3 ZN2 2(ZN1 2+)
FORMUL 5 CA 2(CA1 2+)
FORMUL 7 HOH *257(H2 O1)
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 SER A 195 1 21
HELIX 11 11 PRO A 198 GLU A 202 5 5
HELIX 12 12 LEU A 208 GLY A 212 5 5
HELIX 13 13 SER A 220 ARG A 230 1 11
HELIX 14 14 SER A 231 SER A 236 1 6
HELIX 15 15 THR A 239 SER A 245 1 7
HELIX 16 16 SER A 245 VAL A 256 1 12
HELIX 17 17 ASN A 288 CYS A 295 1 8
HELIX 18 18 CYS A 295 GLY A 300 1 6
HELIX 19 19 ASN A 304 GLY A 308 5 5
HELIX 20 20 ASP A 310 LEU A 314 5 5
HELIX 21 21 ASN A 321 MET A 325 5 5
HELIX 22 22 ASN A 371 SER A 385 1 15
HELIX 23 23 GLU B 1023 PHE B 1027 5 5
HELIX 24 24 ASP B 1036 ASN B 1044 1 9
HELIX 25 25 SER B 1058 GLY B 1072 1 15
HELIX 26 26 GLY B 1078 GLY B 1086 1 9
HELIX 27 27 LEU B 1098 GLY B 1104 5 7
HELIX 28 28 GLN B 1114 GLY B 1129 1 16
HELIX 29 29 SER B 1130 HIS B 1140 1 11
HELIX 30 30 SER B 1145 GLU B 1149 5 5
HELIX 31 31 THR B 1168 MET B 1173 5 6
HELIX 32 32 ASP B 1175 ALA B 1191 1 17
HELIX 33 33 LEU B 1208 GLY B 1212 5 5
HELIX 34 34 SER B 1220 ARG B 1230 1 11
HELIX 35 35 SER B 1231 SER B 1236 1 6
HELIX 36 36 THR B 1239 SER B 1245 1 7
HELIX 37 37 SER B 1245 VAL B 1256 1 12
HELIX 38 38 ASN B 1288 CYS B 1295 1 8
HELIX 39 39 CYS B 1295 GLY B 1300 1 6
HELIX 40 40 ASP B 1310 LEU B 1314 5 5
HELIX 41 41 ASN B 1321 MET B 1325 5 5
HELIX 42 42 ASN B 1371 ALA B 1384 1 14
SHEET 1 A 7 THR A 48 THR A 50 0
SHEET 2 A 7 ILE A 10 LEU A 13 1 N ILE A 10 O TYR A 49
SHEET 3 A 7 VAL 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 PHE A 267 N THR A 160
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 TYR A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 D 7 THR B1048 THR B1050 0
SHEET 2 D 7 ILE B1010 LEU B1013 1 N ILE B1010 O TYR B1049
SHEET 3 D 7 VAL B1107 HIS B1112 1 O ILE B1110 N VAL B1011
SHEET 4 D 7 VAL B1155 ILE B1161 1 O THR B1159 N ALA B1111
SHEET 5 D 7 TYR B1263 THR B1269 1 O PHE B1267 N THR B1160
SHEET 6 D 7 TRP B1348 TYR B1354 1 O ASN B1349 N TYR B1264
SHEET 7 D 7 ILE B1336 PRO B1338 1 N VAL B1337 O TRP B1348
SHEET 1 E 2 GLY B1073 ASP B1076 0
SHEET 2 E 2 PHE B1090 TYR B1094 -1 O TYR B1094 N GLY B1073
SHEET 1 F 2 THR B1272 ARG B1274 0
SHEET 2 F 2 TYR B1281 PRO B1283 -1 O TYR B1282 N TYR B1273
LINK ZN ZN2 A 701 OD1 ASP A 61
LINK ZN ZN2 A 701 NE2 HIS A 81
LINK ZN ZN2 A 701 OD2 ASP A 238
LINK ZN ZN2 B 702 OD1 ASP B1061
LINK ZN ZN2 B 702 NE2 HIS B1081
LINK ZN ZN2 B 702 OD2 ASP B1238
CRYST1 119.620 85.040 98.360 90.00 99.73 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 0.008360 0.000000 0.001433 0.00000
SCALE2 0.000000 0.011759 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010315 0.00000
END |