HEADER HYDROLASE 21-MAR-90 1ST2
TITLE THE THREE-DIMENSIONAL STRUCTURE OF BACILLUS
TITLE 2 AMYLOLIQUEFACIENS SUBTILISIN AT 1.8 ANGSTROMS AND AN
TITLE 3 ANALYSIS OF THE STRUCTURAL CONSEQUENCES OF PEROXIDE
TITLE 4 INACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN BPN';
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.14;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;
SOURCE 3 ORGANISM_TAXID: 1390;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, SERINE PROTEINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BOTT
REVDAT 3 24-FEB-09 1ST2 1 VERSN
REVDAT 2 01-APR-03 1ST2 1 JRNL
REVDAT 1 15-JUL-91 1ST2 0
JRNL AUTH R.BOTT,M.ULTSCH,A.KOSSIAKOFF,T.GRAYCAR,B.KATZ,
JRNL AUTH 2 S.POWER
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF BACILLUS
JRNL TITL 2 AMYLOLIQUEFACIENS SUBTILISIN AT 1.8 A AND AN
JRNL TITL 3 ANALYSIS OF THE STRUCTURAL CONSEQUENCES OF
JRNL TITL 4 PEROXIDE INACTIVATION.
JRNL REF J.BIOL.CHEM. V. 263 7895 1988
JRNL REFN ISSN 0021-9258
JRNL PMID 3286644
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.WELLS,E.FERRARI,D.J.HENNER,D.A.ESTELL,E.Y.CHEN
REMARK 1 TITL CLONING, SEQUENCING AND SECRETION OF BACILLUS
REMARK 1 TITL 2 AMYLOLIQUEFACIENS SUBTILISIN IN BACILLUS SUBTILIS
REMARK 1 REF NUCLEIC ACIDS RES. V. 11 7911 1983
REMARK 1 REFN ISSN 0305-1048
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1938
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 116
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.015 ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ST2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 (%) : 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 19.65000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.67500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.67500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.65000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.40000
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 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 400
REMARK 400 COMPOUND
REMARK 400 RESIDUES MHO 119, 124 AND 222
REMARK 400 ARE OXIDIZED METHIONINES.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 99 NZ LYS A 213 4465 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA A 13 CB - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 ASP A 36 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 41 CB - CG - OD1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASP A 41 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 GLU A 54 CG - CD - OE2 ANGL. DEV. = -14.0 DEGREES
REMARK 500 ASP A 60 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ALA A 74 CB - CA - C ANGL. DEV. = 10.9 DEGREES
REMARK 500 TYR A 104 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 TYR A 104 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ASP A 181 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 186 CD - NE - CZ ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TYR A 214 CB - CG - CD2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TYR A 214 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TYR A 262 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR A 263 CB - CG - CD2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 TYR A 263 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
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 ASP A 32 -145.16 -152.55
REMARK 500 ASP A 36 101.84 -56.68
REMARK 500 GLU A 54 74.39 -158.79
REMARK 500 SER A 63 -9.49 86.86
REMARK 500 ALA A 73 34.55 -145.69
REMARK 500 ASN A 77 -149.36 -149.15
REMARK 500 VAL A 81 -160.11 -108.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 186 0.10 SIDE_CHAIN
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 CA A 276 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 2 OE1
REMARK 620 2 ASP A 41 OD1 147.5
REMARK 620 3 ASP A 41 OD2 155.9 56.0
REMARK 620 4 LEU A 75 O 73.4 87.4 112.3
REMARK 620 5 ASN A 77 OD1 76.4 76.7 126.3 87.0
REMARK 620 6 ILE A 79 O 86.4 103.0 92.3 154.9 73.6
REMARK 620 7 VAL A 81 O 72.5 134.2 84.1 88.5 148.5 99.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 277 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 174 O
REMARK 620 2 ASP A 197 OD2 69.8
REMARK 620 3 HOH A 388 O 117.2 71.8
REMARK 620 N 1 2
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 276
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 277
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 278
DBREF 1ST2 A 1 275 UNP P00782 SUBT_BACAM 108 382
SEQRES 1 A 275 ALA GLN SER VAL PRO TYR GLY VAL SER GLN ILE LYS ALA
SEQRES 2 A 275 PRO ALA LEU HIS SER GLN GLY TYR THR GLY SER ASN VAL
SEQRES 3 A 275 LYS VAL ALA VAL ILE ASP SER GLY ILE ASP SER SER HIS
SEQRES 4 A 275 PRO ASP LEU LYS VAL ALA GLY GLY ALA SER MET VAL PRO
SEQRES 5 A 275 SER GLU THR ASN PRO PHE GLN ASP ASN ASN SER HIS GLY
SEQRES 6 A 275 THR HIS VAL ALA GLY THR VAL ALA ALA LEU ASN ASN SER
SEQRES 7 A 275 ILE GLY VAL LEU GLY VAL ALA PRO SER ALA SER LEU TYR
SEQRES 8 A 275 ALA VAL LYS VAL LEU GLY ALA ASP GLY SER GLY GLN TYR
SEQRES 9 A 275 SER TRP ILE ILE ASN GLY ILE GLU TRP ALA ILE ALA ASN
SEQRES 10 A 275 ASN MHO ASP VAL ILE ASN MHO SER LEU GLY GLY PRO SER
SEQRES 11 A 275 GLY SER ALA ALA LEU LYS ALA ALA VAL ASP LYS ALA VAL
SEQRES 12 A 275 ALA SER GLY VAL VAL VAL VAL ALA ALA ALA GLY ASN GLU
SEQRES 13 A 275 GLY THR SER GLY SER SER SER THR VAL GLY TYR PRO GLY
SEQRES 14 A 275 LYS TYR PRO SER VAL ILE ALA VAL GLY ALA VAL ASP SER
SEQRES 15 A 275 SER ASN GLN ARG ALA SER PHE SER SER VAL GLY PRO GLU
SEQRES 16 A 275 LEU ASP VAL MET ALA PRO GLY VAL SER ILE GLN SER THR
SEQRES 17 A 275 LEU PRO GLY ASN LYS TYR GLY ALA TYR ASN GLY THR SER
SEQRES 18 A 275 MHO ALA SER PRO HIS VAL ALA GLY ALA ALA ALA LEU ILE
SEQRES 19 A 275 LEU SER LYS HIS PRO ASN TRP THR ASN THR GLN VAL ARG
SEQRES 20 A 275 SER SER LEU GLU ASN THR THR THR LYS LEU GLY ASP SER
SEQRES 21 A 275 PHE TYR TYR GLY LYS GLY LEU ILE ASN VAL GLN ALA ALA
SEQRES 22 A 275 ALA GLN
MODRES 1ST2 MHO A 119 MET S-OXYMETHIONINE
MODRES 1ST2 MHO A 124 MET S-OXYMETHIONINE
MODRES 1ST2 MHO A 222 MET S-OXYMETHIONINE
HET MHO A 119 9
HET MHO A 124 9
HET MHO A 222 9
HET CA A 276 1
HET CA A 277 1
HET SO4 A 278 5
HETNAM MHO S-OXYMETHIONINE
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 1 MHO 3(C5 H11 N O3 S)
FORMUL 2 CA 2(CA 2+)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *116(H2 O)
HELIX 1 1 PRO A 5 ILE A 11 1 7
HELIX 2 2 LYS A 12 SER A 18 1 7
HELIX 3 3 SER A 63 ALA A 74 1 12
HELIX 4 4 GLN A 103 ASN A 117 1 15
HELIX 5 5 SER A 132 GLY A 146 1 15
HELIX 6 6 GLY A 219 HIS A 238 1 20
HELIX 7 7 THR A 242 ASN A 252 1 11
HELIX 8 8 ASP A 259 GLY A 264 1 6
HELIX 9 9 ASN A 269 ALA A 274 1 6
SHEET 1 A 7 VAL A 44 SER A 49 0
SHEET 2 A 7 SER A 89 LYS A 94 1 O LEU A 90 N ALA A 45
SHEET 3 A 7 LYS A 27 ASP A 32 1 O VAL A 28 N TYR A 91
SHEET 4 A 7 VAL A 148 ALA A 152 1 O VAL A 148 N ILE A 122
SHEET 5 A 7 ILE A 175 VAL A 180 1 N ILE A 175 O VAL A 149
SHEET 6 A 7 VAL A 198 PRO A 201 1 O VAL A 198 N GLY A 178
SHEET 1 B 2 ILE A 205 LEU A 209 0
SHEET 2 B 2 LYS A 213 TYR A 217 -1 O LYS A 213 N LEU A 209
LINK C ASN A 118 N MHO A 119 1555 1555 1.31
LINK C MHO A 119 N ASP A 120 1555 1555 1.33
LINK C ASN A 123 N MHO A 124 1555 1555 1.31
LINK C MHO A 124 N SER A 125 1555 1555 1.33
LINK C SER A 221 N MHO A 222 1555 1555 1.33
LINK C MHO A 222 N ALA A 223 1555 1555 1.34
LINK OE1 GLN A 2 CA CA A 276 1555 1555 2.46
LINK OD1 ASP A 41 CA CA A 276 1555 1555 2.27
LINK OD2 ASP A 41 CA CA A 276 1555 1555 2.30
LINK O LEU A 75 CA CA A 276 1555 1555 2.49
LINK OD1 ASN A 77 CA CA A 276 1555 1555 2.43
LINK O ILE A 79 CA CA A 276 1555 1555 2.34
LINK O VAL A 81 CA CA A 276 1555 1555 2.32
LINK O VAL A 174 CA CA A 277 1555 1555 2.68
LINK OD2 ASP A 197 CA CA A 277 1555 1555 2.89
LINK CA CA A 277 O HOH A 388 1555 1555 2.88
CISPEP 1 TYR A 167 PRO A 168 0 3.65
SITE 1 AC1 6 GLN A 2 ASP A 41 LEU A 75 ASN A 77
SITE 2 AC1 6 ILE A 79 VAL A 81
SITE 1 AC2 6 GLY A 169 TYR A 171 VAL A 174 GLU A 195
SITE 2 AC2 6 ASP A 197 HOH A 388
SITE 1 AC3 4 TYR A 104 SER A 105 HIS A 238 TRP A 241
CRYST1 39.300 72.800 75.350 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 0.025445 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013736 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013271 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
