HEADER HYDROLASE 16-APR-04 1T1G
TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF MUTANT E23A OF KUMAMOLISIN, A
TITLE 2 SEDOLISIN TYPE PROTEINASE (PREVIOUSLY CALLED KUMAMOLYSIN OR KSCP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KUMAMOLISIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP. MN-32;
SOURCE 3 ORGANISM_TAXID: 198803;
SOURCE 4 GENE: KSCP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM 109
KEYWDS SERINE-CARBOXYL PROTEINASES, SUBTILASES, CATALYTIC MECHANISM,
KEYWDS 2 KUMAMOLISIN, SEDOLISIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.COMELLAS-BIGLER,K.MASKOS,R.HUBER,H.OYAMA,K.ODA,W.BODE
REVDAT 4 14-FEB-24 1T1G 1 REMARK
REVDAT 3 27-OCT-21 1T1G 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1T1G 1 VERSN
REVDAT 1 03-AUG-04 1T1G 0
JRNL AUTH M.COMELLAS-BIGLER,K.MASKOS,R.HUBER,H.OYAMA,K.ODA,W.BODE
JRNL TITL 1.2 A CRYSTAL STRUCTURE OF THE SERINE CARBOXYL PROTEINASE
JRNL TITL 2 PRO-KUMAMOLISIN: STRUCTURE OF AN INTACT PRO-SUBTILASE
JRNL REF STRUCTURE V. 12 1313 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15242607
JRNL DOI 10.1016/J.STR.2004.04.013
REMARK 2
REMARK 2 RESOLUTION. 1.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 98535
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 SET) : 0.202
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 500
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 : 2559
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 327
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 1T1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022192.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.050
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98535
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.180
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM ACETATE, PH
REMARK 280 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
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 39.28500
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 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 SER A 358
REMARK 465 ALA A 359
REMARK 465 SER A 360
REMARK 465 GLN A 361
REMARK 465 ALA A 362
REMARK 465 GLN A 363
REMARK 465 PRO A 364
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 19 CD OE1 OE2
REMARK 480 GLU A 39 CG CD OE1 OE2
REMARK 480 SER A 52 OG
REMARK 480 GLN A 55 CD OE1 NE2
REMARK 480 GLN A 172 CG CD OE1 NE2
REMARK 480 ARG A 223 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 297 CG CD CE NZ
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 ILE A 330 CB ILE A 330 CG1 -0.238
REMARK 500 ILE A 330 CB ILE A 330 CG2 0.373
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 GLN A 172 60.00 -119.53
REMARK 500 ALA A 244 -146.69 51.69
REMARK 500 ALA A 257 -13.44 -142.13
REMARK 500 THR A 261 41.70 -143.50
REMARK 500 PRO A 339 21.24 -77.97
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 365 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 316 OD1
REMARK 620 2 ILE A 317 O 85.7
REMARK 620 3 GLY A 334 O 100.2 86.1
REMARK 620 4 GLY A 336 O 91.2 173.2 88.5
REMARK 620 5 ASP A 338 OD2 165.5 81.5 85.8 102.2
REMARK 620 6 HOH A 368 O 84.5 89.0 172.9 96.7 88.5
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 CA A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 366
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 367
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GT9 RELATED DB: PDB
REMARK 900 NATIVE KUMAMOLISIN CATALYTIC DOMAIN
REMARK 900 RELATED ID: 1GTG RELATED DB: PDB
REMARK 900 NATIVE KUMAMOLISIN CATALYTIC DOMAIN
REMARK 900 RELATED ID: 1GTJ RELATED DB: PDB
REMARK 900 NATIVE KUMAMOLISIN IN COMPLEX WITH AC-ILE-ALA-PHE-CHO
REMARK 900 RELATED ID: 1GTL RELATED DB: PDB
REMARK 900 NATIVE KUMAMOLISIN IN COMPLEX WITH AC-ILE-PRO-PHE-CHO
REMARK 900 RELATED ID: 1T1E RELATED DB: PDB
REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF THE INTACT PRO-KUMAMOLISIN
REMARK 900 RELATED ID: 1T1H RELATED DB: PDB
REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF MUTANT W129A OF KUMAMOLISIN
DBREF 1T1G A 1 364 UNP Q8RR56 Q8RR56_9BACI 189 552
SEQADV 1T1G ALA A 32 UNP Q8RR56 GLU 220 ENGINEERED MUTATION
SEQRES 1 A 364 ALA ALA PRO THR ALA TYR THR PRO LEU ASP VAL ALA GLN
SEQRES 2 A 364 ALA TYR GLN PHE PRO GLU GLY LEU ASP GLY GLN GLY GLN
SEQRES 3 A 364 CYS ILE ALA ILE ILE ALA LEU GLY GLY GLY TYR ASP GLU
SEQRES 4 A 364 THR SER LEU ALA GLN TYR PHE ALA SER LEU GLY VAL SER
SEQRES 5 A 364 ALA PRO GLN VAL VAL SER VAL SER VAL ASP GLY ALA THR
SEQRES 6 A 364 ASN GLN PRO THR GLY ASP PRO ASN GLY PRO ASP GLY GLU
SEQRES 7 A 364 VAL GLU LEU ASP ILE GLU VAL ALA GLY ALA LEU ALA PRO
SEQRES 8 A 364 GLY ALA LYS ILE ALA VAL TYR PHE ALA PRO ASN THR ASP
SEQRES 9 A 364 ALA GLY PHE LEU ASN ALA ILE THR THR ALA VAL HIS ASP
SEQRES 10 A 364 PRO THR HIS LYS PRO SER ILE VAL SER ILE SER TRP GLY
SEQRES 11 A 364 GLY PRO GLU ASP SER TRP ALA PRO ALA SER ILE ALA ALA
SEQRES 12 A 364 MET ASN ARG ALA PHE LEU ASP ALA ALA ALA LEU GLY VAL
SEQRES 13 A 364 THR VAL LEU ALA ALA ALA GLY ASP SER GLY SER THR ASP
SEQRES 14 A 364 GLY GLU GLN ASP GLY LEU TYR HIS VAL ASP PHE PRO ALA
SEQRES 15 A 364 ALA SER PRO TYR VAL LEU ALA CYS GLY GLY THR ARG LEU
SEQRES 16 A 364 VAL ALA SER ALA GLY ARG ILE GLU ARG GLU THR VAL TRP
SEQRES 17 A 364 ASN ASP GLY PRO ASP GLY GLY SER THR GLY GLY GLY VAL
SEQRES 18 A 364 SER ARG ILE PHE PRO LEU PRO SER TRP GLN GLU ARG ALA
SEQRES 19 A 364 ASN VAL PRO PRO SER ALA ASN PRO GLY ALA GLY SER GLY
SEQRES 20 A 364 ARG GLY VAL PRO ASP VAL ALA GLY ASN ALA ASP PRO ALA
SEQRES 21 A 364 THR GLY TYR GLU VAL VAL ILE ASP GLY GLU THR THR VAL
SEQRES 22 A 364 ILE GLY GLY THR SER ALA VAL ALA PRO LEU PHE ALA ALA
SEQRES 23 A 364 LEU VAL ALA ARG ILE ASN GLN LYS LEU GLY LYS PRO VAL
SEQRES 24 A 364 GLY TYR LEU ASN PRO THR LEU TYR GLN LEU PRO PRO GLU
SEQRES 25 A 364 VAL PHE HIS ASP ILE THR GLU GLY ASN ASN ASP ILE ALA
SEQRES 26 A 364 ASN ARG ALA ARG ILE TYR GLN ALA GLY PRO GLY TRP ASP
SEQRES 27 A 364 PRO CYS THR GLY LEU GLY SER PRO ILE GLY ILE ARG LEU
SEQRES 28 A 364 LEU GLN ALA LEU LEU PRO SER ALA SER GLN ALA GLN PRO
HET CA A 365 1
HET SO4 A 366 5
HET SO4 A 367 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 2 CA CA 2+
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *327(H2 O)
HELIX 1 1 THR A 7 TYR A 15 1 9
HELIX 2 2 ASP A 38 LEU A 49 1 12
HELIX 3 3 PRO A 75 ALA A 90 1 16
HELIX 4 4 THR A 103 ASP A 117 1 15
HELIX 5 5 ASP A 134 TRP A 136 5 3
HELIX 6 6 ALA A 137 GLY A 155 1 19
HELIX 7 7 SER A 165 ASP A 169 5 5
HELIX 8 8 ASP A 210 GLY A 215 1 6
HELIX 9 9 PRO A 228 GLU A 232 5 5
HELIX 10 10 GLY A 276 SER A 278 5 3
HELIX 11 11 ALA A 279 GLY A 296 1 18
HELIX 12 12 LEU A 302 TYR A 307 1 6
HELIX 13 13 GLN A 308 LEU A 309 5 2
HELIX 14 14 PRO A 310 GLU A 312 5 3
HELIX 15 15 ILE A 347 LEU A 356 1 10
SHEET 1 A 3 THR A 4 TYR A 6 0
SHEET 2 A 3 THR A 261 ILE A 267 1 O GLU A 264 N TYR A 6
SHEET 3 A 3 GLU A 270 ILE A 274 -1 O ILE A 274 N TYR A 263
SHEET 1 B 7 VAL A 56 SER A 60 0
SHEET 2 B 7 LYS A 94 PHE A 99 1 O VAL A 97 N VAL A 57
SHEET 3 B 7 CYS A 27 ALA A 32 1 N ILE A 30 O TYR A 98
SHEET 4 B 7 ILE A 124 ILE A 127 1 O ILE A 124 N ALA A 29
SHEET 5 B 7 THR A 157 ALA A 161 1 O LEU A 159 N VAL A 125
SHEET 6 B 7 LEU A 188 ALA A 197 1 O CYS A 190 N ALA A 160
SHEET 7 B 7 ILE A 202 VAL A 207 -1 O ARG A 204 N VAL A 196
SHEET 1 C 7 VAL A 56 SER A 60 0
SHEET 2 C 7 LYS A 94 PHE A 99 1 O VAL A 97 N VAL A 57
SHEET 3 C 7 CYS A 27 ALA A 32 1 N ILE A 30 O TYR A 98
SHEET 4 C 7 ILE A 124 ILE A 127 1 O ILE A 124 N ALA A 29
SHEET 5 C 7 THR A 157 ALA A 161 1 O LEU A 159 N VAL A 125
SHEET 6 C 7 LEU A 188 ALA A 197 1 O CYS A 190 N ALA A 160
SHEET 7 C 7 VAL A 253 ASN A 256 1 O VAL A 253 N GLY A 191
SHEET 1 D 2 GLY A 131 PRO A 132 0
SHEET 2 D 2 ASP A 179 PHE A 180 -1 O PHE A 180 N GLY A 131
SHEET 1 E 2 GLY A 220 VAL A 221 0
SHEET 2 E 2 GLY A 249 VAL A 250 -1 O VAL A 250 N GLY A 220
SHEET 1 F 2 PHE A 314 HIS A 315 0
SHEET 2 F 2 SER A 345 PRO A 346 -1 O SER A 345 N HIS A 315
LINK OD1 ASP A 316 CA CA A 365 1555 1555 2.43
LINK O ILE A 317 CA CA A 365 1555 1555 2.46
LINK O GLY A 334 CA CA A 365 1555 1555 2.48
LINK O GLY A 336 CA CA A 365 1555 1555 2.39
LINK OD2 ASP A 338 CA CA A 365 1555 1555 2.42
LINK CA CA A 365 O HOH A 368 1555 1555 2.55
CISPEP 1 PHE A 180 PRO A 181 0 0.66
CISPEP 2 VAL A 250 PRO A 251 0 0.04
CISPEP 3 ILE A 330 TYR A 331 0 -0.37
CISPEP 4 ILE A 330 TYR A 331 0 -0.37
SITE 1 AC1 6 ASP A 316 ILE A 317 GLY A 334 GLY A 336
SITE 2 AC1 6 ASP A 338 HOH A 368
SITE 1 AC2 9 SER A 198 ALA A 199 GLY A 200 ARG A 201
SITE 2 AC2 9 PRO A 228 SER A 229 HOH A 407 HOH A 518
SITE 3 AC2 9 HOH A 569
SITE 1 AC3 8 LYS A 121 ARG A 327 ARG A 329 HOH A 389
SITE 2 AC3 8 HOH A 463 HOH A 532 HOH A 539 HOH A 575
CRYST1 42.720 78.570 49.990 90.00 106.48 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 0.023408 0.000000 0.006925 0.00000
SCALE2 0.000000 0.012728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020861 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
