HEADER HYDROLASE 23-MAR-01 1IAV
TITLE STRUCTURE ON NATIVE (ASN 87) SUBTILISIN FROM BACILLUS LENTUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN SAVINASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.62;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LENTUS;
SOURCE 3 ORGANISM_TAXID: 1467;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SUBTILISINS, ALTERED FLEXIBILITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KNAPP,R.BOTT
REVDAT 7 27-OCT-21 1IAV 1 REMARK SEQADV LINK
REVDAT 6 18-APR-18 1IAV 1 REMARK
REVDAT 5 04-APR-18 1IAV 1 REMARK
REVDAT 4 04-OCT-17 1IAV 1 REMARK
REVDAT 3 24-FEB-09 1IAV 1 VERSN
REVDAT 2 11-JUL-01 1IAV 1 COMPND
REVDAT 1 18-APR-01 1IAV 0
SPRSDE 18-APR-01 1IAV 1C13
JRNL AUTH T.GRAYCAR,M.KNAPP,G.GANSHAW,J.DAUBERMAN,R.BOTT
JRNL TITL ENGINEERED BACILLUS LENTUS SUBTILISINS HAVING ALTERED
JRNL TITL 2 FLEXIBILITY.
JRNL REF J.MOL.BIOL. V. 292 97 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10493860
JRNL DOI 10.1006/JMBI.1999.3033
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 73.0
REMARK 3 NUMBER OF REFLECTIONS : 16480
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) : 0.148
REMARK 3 R VALUE (WORKING SET) : NULL
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 : 1891
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 111
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) : 0.014 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 2.800 ; 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 1IAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-91
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.90
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
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 : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS CAD4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CAD4
REMARK 200 DATA SCALING SOFTWARE : CAD4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16480
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.0
REMARK 200 DATA REDUNDANCY : 1.000
REMARK 200 R MERGE (I) : 0.06900
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.90
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 26.65000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.55000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.55000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.65000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.75000
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 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 CB ASN A 204 O HOH A 351 2.13
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 ARG A 10 NH1 - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 19 CD - NE - CZ ANGL. DEV. = 28.9 DEGREES
REMARK 500 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 32 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 SER A 36 CA - CB - OG ANGL. DEV. = -16.5 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP A 60 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 60 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ALA A 73 N - CA - CB ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLU A 112 CG - CD - OE2 ANGL. DEV. = -12.4 DEGREES
REMARK 500 ARG A 186 CD - NE - CZ ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH1 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 TYR A 192 CB - CG - CD2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 TYR A 192 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 197 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 GLN A 245 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 GLU A 271 OE1 - CD - OE2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG A 275 NE - CZ - NH1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 275 NE - CZ - NH2 ANGL. DEV. = -8.6 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 -148.61 -166.16
REMARK 500 ALA A 73 34.02 -140.12
REMARK 500 ASN A 77 -146.18 -152.62
REMARK 500 VAL A 81 -163.96 -122.00
REMARK 500 SER A 259 135.39 -31.34
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 45 0.09 SIDE CHAIN
REMARK 500 ARG A 145 0.13 SIDE CHAIN
REMARK 500 ARG A 275 0.11 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 277 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 2 OE1
REMARK 620 2 ASP A 41 OD1 158.0
REMARK 620 3 ASP A 41 OD2 151.6 50.0
REMARK 620 4 LEU A 75 O 80.0 86.4 109.5
REMARK 620 5 ASN A 77 OD1 83.9 78.4 122.2 88.2
REMARK 620 6 ILE A 79 O 90.3 98.9 84.7 164.6 78.9
REMARK 620 7 VAL A 81 O 76.0 121.6 77.1 90.4 159.9 98.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 278 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 169 O
REMARK 620 2 TYR A 171 O 74.5
REMARK 620 3 ALA A 174 O 88.0 68.5
REMARK 620 4 GLY A 195 O 100.9 159.3 132.0
REMARK 620 5 ASP A 197 OD2 120.5 136.2 71.1 63.7
REMARK 620 6 HOH A 339 O 128.9 81.4 123.7 86.5 108.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 278
DBREF 1IAV A 1 275 UNP P29600 SUBS_BACLE 1 269
SEQADV 1IAV ASN A 87 UNP P29600 SER 85 ENGINEERED MUTATION
SEQADV 1IAV SEB A 221 UNP P29600 SER 215 MODIFIED RESIDUE
SEQRES 1 A 269 ALA GLN SER VAL PRO TRP GLY ILE SER ARG VAL GLN ALA
SEQRES 2 A 269 PRO ALA ALA HIS ASN ARG GLY LEU THR GLY SER GLY VAL
SEQRES 3 A 269 LYS VAL ALA VAL LEU ASP THR GLY ILE SER THR HIS PRO
SEQRES 4 A 269 ASP LEU ASN ILE ARG GLY GLY ALA SER PHE VAL PRO GLY
SEQRES 5 A 269 GLU PRO SER THR GLN ASP GLY ASN GLY HIS GLY THR HIS
SEQRES 6 A 269 VAL ALA GLY THR ILE ALA ALA LEU ASN ASN SER ILE GLY
SEQRES 7 A 269 VAL LEU GLY VAL ALA PRO ASN ALA GLU LEU TYR ALA VAL
SEQRES 8 A 269 LYS VAL LEU GLY ALA SER GLY SER GLY SER VAL SER SER
SEQRES 9 A 269 ILE ALA GLN GLY LEU GLU TRP ALA GLY ASN ASN GLY MET
SEQRES 10 A 269 HIS VAL ALA ASN LEU SER LEU GLY SER PRO SER PRO SER
SEQRES 11 A 269 ALA THR LEU GLU GLN ALA VAL ASN SER ALA THR SER ARG
SEQRES 12 A 269 GLY VAL LEU VAL VAL ALA ALA SER GLY ASN SER GLY ALA
SEQRES 13 A 269 GLY SER ILE SER TYR PRO ALA ARG TYR ALA ASN ALA MET
SEQRES 14 A 269 ALA VAL GLY ALA THR ASP GLN ASN ASN ASN ARG ALA SER
SEQRES 15 A 269 PHE SER GLN TYR GLY ALA GLY LEU ASP ILE VAL ALA PRO
SEQRES 16 A 269 GLY VAL ASN VAL GLN SER THR TYR PRO GLY SER THR TYR
SEQRES 17 A 269 ALA SER LEU ASN GLY THR SEB MET ALA THR PRO HIS VAL
SEQRES 18 A 269 ALA GLY ALA ALA ALA LEU VAL LYS GLN LYS ASN PRO SER
SEQRES 19 A 269 TRP SER ASN VAL GLN ILE ARG ASN HIS LEU LYS ASN THR
SEQRES 20 A 269 ALA THR SER LEU GLY SER THR ASN LEU TYR GLY SER GLY
SEQRES 21 A 269 LEU VAL ASN ALA GLU ALA ALA THR ARG
MODRES 1IAV SEB A 221 SER O-BENZYLSULFONYL-SERINE
HET SEB A 221 16
HET SO4 A 276 5
HET CA A 277 1
HET CA A 278 1
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM SO4 SULFATE ION
HETNAM CA CALCIUM ION
FORMUL 1 SEB C10 H13 N O5 S
FORMUL 2 SO4 O4 S 2-
FORMUL 3 CA 2(CA 2+)
FORMUL 5 HOH *111(H2 O)
HELIX 1 1 PRO A 5 VAL A 11 1 7
HELIX 2 2 GLN A 12 ASN A 18 1 7
HELIX 3 3 GLY A 63 ALA A 74 1 12
HELIX 4 4 SER A 103 ASN A 117 1 15
HELIX 5 5 SER A 132 ARG A 145 1 14
HELIX 6 6 ALA A 223 ASN A 238 1 16
HELIX 7 7 SER A 242 THR A 253 1 12
HELIX 8 8 SER A 259 GLY A 264 1 6
HELIX 9 9 ASN A 269 THR A 274 1 6
SHEET 1 A 7 ILE A 44 SER A 49 0
SHEET 2 A 7 GLU A 89 LYS A 94 1 O LEU A 90 N ARG 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 121 LEU A 124 1 O VAL A 121 N ALA A 29
SHEET 5 A 7 LEU A 148 ALA A 152 1 O LEU A 148 N ALA A 122
SHEET 6 A 7 ALA A 174 THR A 180 1 N MET A 175 O VAL A 149
SHEET 7 A 7 LEU A 196 PRO A 201 1 N ASP A 197 O ALA A 176
SHEET 1 B 2 VAL A 205 TYR A 209 0
SHEET 2 B 2 THR A 213 LEU A 217 -1 N THR A 213 O TYR A 209
LINK C THR A 220 N SEB A 221 1555 1555 1.33
LINK C SEB A 221 N MET A 222 1555 1555 1.34
LINK OE1 GLN A 2 CA CA A 277 1555 1555 2.46
LINK OD1 ASP A 41 CA CA A 277 1555 1555 2.47
LINK OD2 ASP A 41 CA CA A 277 1555 1555 2.58
LINK O LEU A 75 CA CA A 277 1555 1555 2.24
LINK OD1 ASN A 77 CA CA A 277 1555 1555 2.46
LINK O ILE A 79 CA CA A 277 1555 1555 2.43
LINK O VAL A 81 CA CA A 277 1555 1555 2.42
LINK O ALA A 169 CA CA A 278 1555 1555 2.71
LINK O TYR A 171 CA CA A 278 1555 1555 3.06
LINK O ALA A 174 CA CA A 278 1555 1555 2.72
LINK O GLY A 195 CA CA A 278 1555 1555 2.73
LINK OD2 ASP A 197 CA CA A 278 1555 1555 3.10
LINK CA CA A 278 O HOH A 339 1555 1555 2.84
CISPEP 1 TYR A 167 PRO A 168 0 4.52
SITE 1 AC1 4 SER A 132 ALA A 133 THR A 134 HOH A 349
SITE 1 AC2 6 GLN A 2 ASP A 41 LEU A 75 ASN A 77
SITE 2 AC2 6 ILE A 79 VAL A 81
SITE 1 AC3 6 ALA A 169 TYR A 171 ALA A 174 GLY A 195
SITE 2 AC3 6 ASP A 197 HOH A 339
CRYST1 53.300 61.500 75.100 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 0.018762 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016260 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013316 0.00000
(ATOM LINES ARE NOT SHOWN.)
END