HEADER HYDROLASE(SERINE PROTEINASE) 10-JUN-92 1SUC
TITLE CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN
CAVEAT 1SUC RESIDUES 75-83 MISSING, RESIDUE A74 & A84 LINKED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN BPN' CRB-S3;
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 AMYLOLIQUEFACIENS;
SOURCE 3 ORGANISM_TAXID: 1390
KEYWDS HYDROLASE(SERINE PROTEINASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR T.GALLAGHER,P.BRYAN,G.L.GILLILAND
REVDAT 4 03-NOV-21 1SUC 1 REMARK SEQADV LINK
REVDAT 3 29-NOV-17 1SUC 1 HELIX
REVDAT 2 24-FEB-09 1SUC 1 VERSN
REVDAT 1 31-JAN-94 1SUC 0
JRNL AUTH T.GALLAGHER,P.BRYAN,G.L.GILLILAND
JRNL TITL CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN.
JRNL REF PROTEINS V. 16 205 1993
JRNL REFN ISSN 0887-3585
JRNL PMID 8332608
JRNL DOI 10.1002/PROT.340160207
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 18748
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) : 0.177
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 : 1854
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 160
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) : 0.019 ; 0.025
REMARK 3 ANGLE DISTANCE (A) : 0.036 ; 0.032
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.037 ; 0.040
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.033 ; 0.030
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.287 ; 0.250
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.374 ; 0.200
REMARK 3 MULTIPLE TORSION (A) : 0.120 ; 0.200
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.171 ; 0.200
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 5.000 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 16.900; 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) : 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 1SUC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176521.
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) : 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 (%) : 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 (%): 37.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 39.33500
REMARK 290 SMTRY3 2 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 SECONDARY STRUCTURE ASSIGNMENT IS ACCORDING TO KABSCH AND
REMARK 400 SANDER (BIOPOLYMERS 22, 2577-2637, 1983).
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 A 1
REMARK 465 GLN A 2
REMARK 465 SER A 3
REMARK 465 LEU A 75
REMARK 465 ASN A 76
REMARK 465 ASN A 77
REMARK 465 SER A 78
REMARK 465 ILE A 79
REMARK 465 GLY A 80
REMARK 465 VAL A 81
REMARK 465 LEU A 82
REMARK 465 GLY A 83
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 4 CB CG1 CG2
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 63 CB SER A 63 OG 0.081
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 VAL A 28 CA - CB - CG2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 LYS A 43 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 PHE A 58 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 SER A 63 N - CA - CB ANGL. DEV. = 13.2 DEGREES
REMARK 500 ASP A 99 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP A 106 CA - CB - CG ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP A 120 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 140 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 VAL A 150 CA - CB - CG2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 TYR A 171 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 186 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 THR A 244 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 LEU A 257 CB - CA - C ANGL. DEV. = 16.4 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 -156.69 -155.42
REMARK 500 SER A 63 -26.62 115.20
REMARK 500 LEU A 257 -119.74 -105.46
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 ANGLE, 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 VAL A 84 11.18
REMARK 500 TYR A 104 -10.56
REMARK 500 GLU A 112 -13.89
REMARK 500 ALA A 133 -11.04
REMARK 500 VAL A 198 -11.32
REMARK 500 GLY A 264 -10.76
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 K A 297 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 169 O
REMARK 620 2 TYR A 171 O 78.5
REMARK 620 3 VAL A 174 O 100.7 72.8
REMARK 620 4 ASP A 197 OD2 118.1 138.1 66.6
REMARK 620 5 HOH A 323 O 108.5 80.0 134.8 122.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACN A 298
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 OMITTING RESIDUE NUMBERS 75-83 REFLECTS THE ENGINEERED
REMARK 999 DELETION AND PRESERVES WILD TYPE NUMBERING OF RESIDUES
REMARK 999 84-275.
DBREF 1SUC A 1 275 UNP P00782 SUBT_BACAM 108 382
SEQADV 1SUC PHE A 50 UNP P00782 MET 157 ENGINEERED MUTATION
SEQADV 1SUC LYS A 217 UNP P00782 TYR 324 ENGINEERED MUTATION
SEQADV 1SUC SER A 218 UNP P00782 ASN 325 ENGINEERED MUTATION
SEQADV 1SUC CSD A 221 UNP P00782 SER 328 ENGINEERED MUTATION
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 PHE 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 LYS SER GLY THR CSD
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
MODRES 1SUC CSD A 221 CYS 3-SULFINOALANINE
HET CSD A 221 8
HET K A 297 1
HET ACN A 298 4
HETNAM CSD 3-SULFINOALANINE
HETNAM K POTASSIUM ION
HETNAM ACN ACETONE
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD C3 H7 N O4 S
FORMUL 2 K K 1+
FORMUL 3 ACN C3 H6 O
FORMUL 4 HOH *160(H2 O)
HELIX 1 A TYR A 6 GLN A 10 1 5
HELIX 2 B ALA A 13 SER A 18 1 6
HELIX 3 C HIS A 64 VAL A 84 1EXTENDED BY DELETION OF 75-83 12
HELIX 4 D TYR A 104 ALA A 116 1 13
HELIX 5 E ALA A 133 ALA A 144 1 12
HELIX 6 F THR A 220 LYS A 237 1 18
HELIX 7 G ASN A 243 ASN A 252 1 10
HELIX 8 H SER A 260 TYR A 263 1 4
HELIX 9 I VAL A 270 ALA A 274 1 5
SHEET 1 S1 7 VAL A 44 SER A 49 0
SHEET 2 S1 7 SER A 89 LYS A 94 1 O LEU A 90 N ALA A 45
SHEET 3 S1 7 LYS A 27 ASP A 32 1 N VAL A 28 O SER A 89
SHEET 4 S1 7 VAL A 121 MET A 124 1 N VAL A 121 O LYS A 27
SHEET 5 S1 7 VAL A 148 ALA A 152 1 O VAL A 148 N ILE A 122
SHEET 6 S1 7 ILE A 175 VAL A 180 1 N ILE A 175 O VAL A 149
SHEET 7 S1 7 VAL A 198 PRO A 201 1 O VAL A 198 N GLY A 178
SHEET 1 S2 2 ILE A 205 LEU A 209 0
SHEET 2 S2 2 LYS A 213 LYS A 217 -1 O LYS A 217 N ILE A 205
LINK C THR A 220 N CSD A 221 1555 1555 1.33
LINK C CSD A 221 N MET A 222 1555 1555 1.34
LINK O GLY A 169 K K A 297 1555 1555 2.63
LINK O TYR A 171 K K A 297 1555 1555 2.82
LINK O VAL A 174 K K A 297 1555 1555 2.76
LINK OD2 ASP A 197 K K A 297 1555 1555 2.96
LINK K K A 297 O HOH A 323 1555 1555 2.80
CISPEP 1 TYR A 167 PRO A 168 0 3.26
SITE 1 ACT 3 ASP A 32 HIS A 64 CSD A 221
SITE 1 AC1 6 GLY A 169 TYR A 171 VAL A 174 GLU A 195
SITE 2 AC1 6 ASP A 197 HOH A 323
SITE 1 AC2 3 SER A 37 PHE A 58 ARG A 186
CRYST1 41.370 78.670 36.780 90.00 114.73 90.00 P 1 21 1 2
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 0.024172 0.000000 0.011133 0.00000
SCALE2 0.000000 0.012711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029934 0.00000
(ATOM LINES ARE NOT SHOWN.)
END