HEADER HYDROLASE (SERINE PROTEASE) 14-AUG-95 1SUP
TITLE SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF
TITLE 2 DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN BPN';
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SUBTILISIN NOVO;
COMPND 5 EC: 3.4.21.62
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;
SOURCE 3 ORGANISM_TAXID: 1390
KEYWDS HYDROLASE (SERINE PROTEASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR D.T.GALLAGHER,J.D.OLIVER,C.BETZEL,G.L.GILLILAND
REVDAT 2 24-FEB-09 1SUP 1 VERSN
REVDAT 1 14-NOV-95 1SUP 0
JRNL AUTH T.GALLAGHER,J.OLIVER,R.BOTT,C.BETZEL,G.L.GILLILAND
JRNL TITL SUBTILISIN BPN' AT 1.6 A RESOLUTION: ANALYSIS FOR
JRNL TITL 2 DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 52 1125 1996
JRNL REFN ISSN 0907-4449
JRNL PMID 15299573
JRNL DOI 10.1107/S0907444996007500
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26220
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) : 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 : 2018
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.50
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) : 0.020 ; 0.021
REMARK 3 ANGLE DISTANCE (A) : 0.034 ; 0.027
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.046 ; 0.040
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.029 ; 0.030
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.219 ; 0.250
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.428 ; 0.200
REMARK 3 MULTIPLE TORSION (A) : 0.355 ; 0.200
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.195 ; 0.200
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 4.700 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 15.800; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.136 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.777 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.632 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.507 ; 1.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PEPTIDE 257 - 258 IS DISCRETELY
REMARK 3 DISORDERED. THE ZONE 256 - 259 WAS REFINED IN TWO DISTINCT
REMARK 3 CONFORMATIONS. ATOMS CD, CE, AND NZ OF LYS 256 ARE FURTHER
REMARK 3 DISORDERED, SO THEIR OCCUPANCIES DO NOT SUM TO 1.0.
REMARK 4
REMARK 4 1SUP 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 : 26328
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
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 (%): 39.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
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 X+1/2,Y+1/2,Z
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 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 33.28000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.28000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.07500
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 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 472 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 SER 221 IS COVALENTLY DERIVATIZED WITH
REMARK 400 PHENYLMETHYLSULFONATE (PMS), HET GROUP 278.
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 ASP A 32 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 41 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 GLU A 54 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 GLU A 54 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 SER A 63 N - CA - CB ANGL. DEV. = 9.7 DEGREES
REMARK 500 LEU A 90 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ALA A 98 N - CA - CB ANGL. DEV. = 11.8 DEGREES
REMARK 500 TYR A 104 CA - CB - CG ANGL. DEV. = 12.3 DEGREES
REMARK 500 TYR A 104 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 140 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TYR A 217 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASN A 240 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LEU A 257 CB - CA - C ANGL. DEV. = 15.0 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 -152.21 -164.88
REMARK 500 SER A 63 -31.06 103.62
REMARK 500 ALA A 73 32.98 -146.02
REMARK 500 ASN A 77 -152.07 -152.75
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 ASN A 62 0.08 SIDE_CHAIN
REMARK 500 GLN A 185 0.08 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 HIS A 17 -10.03
REMARK 500 GLY A 97 -10.31
REMARK 500 TYR A 104 -11.52
REMARK 500 LEU A 257 14.07
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 ASP A 41 OD2
REMARK 620 2 LEU A 75 O 109.5
REMARK 620 3 VAL A 81 O 76.4 89.9
REMARK 620 4 GLN A 2 OE1 154.8 78.2 79.6
REMARK 620 5 ILE A 79 O 86.9 162.4 100.4 89.7
REMARK 620 6 ASN A 77 OD1 122.9 88.6 159.8 80.4 76.8
REMARK 620 7 ASP A 41 OD1 50.9 87.6 122.3 154.1 98.6 77.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 277 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 169 O
REMARK 620 2 TYR A 171 O 75.2
REMARK 620 3 VAL A 174 O 103.1 73.5
REMARK 620 4 ASP A 197 OD2 122.8 138.5 66.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
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 NA A 277
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMS A 278
DBREF 1SUP 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 MET ASP VAL ILE ASN MET 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 MET 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
HET CA A 276 1
HET NA A 277 1
HET PMS A 278 10
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM PMS BENZYLSULFINIC ACID
FORMUL 2 CA CA 2+
FORMUL 3 NA NA 1+
FORMUL 4 PMS C7 H8 O2 S
FORMUL 5 HOH *194(H2 O)
HELIX 1 1 TYR A 6 GLN A 10 1 5
HELIX 2 2 ALA A 13 GLN A 19 1 7
HELIX 3 3 HIS A 64 ALA A 73 1 10
HELIX 4 4 TYR A 104 ALA A 116 1 13
HELIX 5 5 ALA A 133 ALA A 144 1 12
HELIX 6 6 THR A 220 LYS A 237 1 18
HELIX 7 7 ASN A 243 ASN A 252 1 10
HELIX 8 8 SER A 260 TYR A 263 1 4
HELIX 9 9 VAL A 270 ALA A 273 1 4
SHEET 1 A 7 VAL A 198 PRO A 201 0
SHEET 2 A 7 ILE A 175 VAL A 180 1 N GLY A 178 O VAL A 198
SHEET 3 A 7 VAL A 148 ALA A 152 1 N ALA A 151 O ILE A 175
SHEET 4 A 7 VAL A 121 MET A 124 1 N ILE A 122 O VAL A 148
SHEET 5 A 7 LYS A 27 ASP A 32 1 N ALA A 29 O VAL A 121
SHEET 6 A 7 SER A 89 LYS A 94 1 N SER A 89 O VAL A 28
SHEET 7 A 7 VAL A 44 SER A 49 1 N ALA A 45 O LEU A 90
SHEET 1 B 2 ILE A 205 LEU A 209 0
SHEET 2 B 2 LYS A 213 TYR A 217 -1 N TYR A 217 O ILE A 205
LINK NE2BHIS A 64 C2 PMS A 278 1555 1555 1.53
LINK CD2BHIS A 64 C3 PMS A 278 1555 1555 1.34
LINK NE2BHIS A 64 C3 PMS A 278 1555 1555 1.48
LINK OG SER A 221 S PMS A 278 1555 1555 1.53
LINK CA CA A 276 OD2 ASP A 41 1555 1555 2.61
LINK CA CA A 276 O LEU A 75 1555 1555 2.27
LINK CA CA A 276 O VAL A 81 1555 1555 2.30
LINK CA CA A 276 OE1 GLN A 2 1555 1555 2.38
LINK CA CA A 276 O ILE A 79 1555 1555 2.35
LINK CA CA A 276 OD1 ASN A 77 1555 1555 2.37
LINK CA CA A 276 OD1 ASP A 41 1555 1555 2.40
LINK O GLY A 169 NA NA A 277 1555 1555 2.82
LINK O TYR A 171 NA NA A 277 1555 1555 2.98
LINK O VAL A 174 NA NA A 277 1555 1555 2.76
LINK OD2 ASP A 197 NA NA A 277 1555 1555 2.85
CISPEP 1 TYR A 167 PRO A 168 0 5.98
SITE 1 ACT 3 SER A 221 HIS A 64 ASP A 32
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 7 GLY A 169 TYR A 171 VAL A 174 GLU A 195
SITE 2 AC2 7 ASP A 197 HOH A 313 HOH A 368
SITE 1 AC3 8 HIS A 64 SER A 125 ASN A 155 TYR A 217
SITE 2 AC3 8 ASN A 218 SER A 221 MET A 222 HOH A 393
CRYST1 66.560 54.150 62.730 90.00 91.87 90.00 C 1 2 1 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 0.015024 0.000000 0.000491 0.00000
SCALE2 0.000000 0.018467 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015950 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
