HEADER SERINE PROTEASE 13-JUL-93 1SCB
TITLE ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN CARLSBERG;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.62;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;
SOURCE 3 ORGANISM_TAXID: 1402
KEYWDS SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.FITZPATRICK,A.C.U.STEINMETZ,D.RINGE,A.M.KLIBANOV
REVDAT 6 14-FEB-24 1SCB 1 REMARK SEQADV LINK
REVDAT 5 29-NOV-17 1SCB 1 HELIX
REVDAT 4 24-FEB-09 1SCB 1 VERSN
REVDAT 3 01-APR-03 1SCB 1 JRNL
REVDAT 2 15-JAN-95 1SCB 1 COMPND JRNL
REVDAT 1 31-JAN-94 1SCB 0
JRNL AUTH P.A.FITZPATRICK,A.C.STEINMETZ,D.RINGE,A.M.KLIBANOV
JRNL TITL ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 90 8653 1993
JRNL REFN ISSN 0027-8424
JRNL PMID 8378343
JRNL DOI 10.1073/PNAS.90.18.8653
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
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 : 9512
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
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 USING ALL DATA, NO SIGMA CUTOFF.
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 : 1920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 99
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.016 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.800 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SCB 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_1000176310.
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 (%): 41.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
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 38.55000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 26.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.55000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.70000
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 NH1 ARG A 249 O HOH A 400 1.93
REMARK 500 O ASN A 62 N HIS A 64 2.12
REMARK 500 O HOH A 384 O HOH A 385 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 54 CD GLU A 54 OE1 0.076
REMARK 500 GLU A 112 CD GLU A 112 OE2 0.079
REMARK 500 SER A 190 CB SER A 190 OG -0.082
REMARK 500 GLU A 271 CD GLU A 271 OE2 0.067
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 ASN A 62 CA - C - N ANGL. DEV. = 17.4 DEGREES
REMARK 500 TYR A 91 CB - CG - CD2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 TYR A 91 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 SER A 101 CB - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 SER A 125 O - C - N ANGL. DEV. = -20.0 DEGREES
REMARK 500 LEU A 126 N - CA - CB ANGL. DEV. = 18.3 DEGREES
REMARK 500 ARG A 145 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 172 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 181 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 SER A 190 N - CA - CB ANGL. DEV. = 10.6 DEGREES
REMARK 500 THR A 211 C - N - CA ANGL. DEV. = 43.2 DEGREES
REMARK 500 SER A 244 N - CA - CB ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 247 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH2 ANGL. DEV. = -4.0 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 -154.36 -156.57
REMARK 500 GLN A 36 80.06 -62.65
REMARK 500 LEU A 75 155.91 -45.21
REMARK 500 ASN A 77 -135.65 -143.62
REMARK 500 LEU A 126 124.29 146.61
REMARK 500 THR A 211 77.05 76.22
REMARK 500 SER A 259 133.98 -39.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 125 LEU A 126 -127.28
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 249 0.20 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 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 SER A 125 -19.54
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 OD2 149.5
REMARK 620 3 ASP A 41 OD1 162.4 46.6
REMARK 620 4 LEU A 75 O 83.6 107.1 97.9
REMARK 620 5 ASN A 77 OD1 81.4 122.9 81.1 100.4
REMARK 620 6 THR A 79 O 81.6 89.3 94.0 163.6 70.4
REMARK 620 7 VAL A 81 O 82.3 71.6 115.4 81.4 163.2 103.6
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCN A 416
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE ADVISORY NOTICE:
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME: SUBT_BACLI
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 THR 207 SER 103
REMARK 999 PRO 233 ALA 129
REMARK 999 SER 262 ASN 158
REMARK 999 ASN 265 SER 161
REMARK 999 SER 316 ASN 212
REMARK 999
REMARK 999 THE SEQUENCE NUMBERING USED FOR SUBTILISIN IS BASED ON THAT
REMARK 999 OF SUBTILISIN BPN' WITH A SINGLE DELETION AT RESIDUE 56.
DBREF 1SCB A 1 275 UNP P00780 SUBT_BACLI 106 379
SEQADV 1SCB SER A 103 UNP P00780 THR 207 CONFLICT
SEQADV 1SCB ALA A 129 UNP P00780 PRO 233 CONFLICT
SEQADV 1SCB ASN A 158 UNP P00780 SER 262 CONFLICT
SEQADV 1SCB SER A 161 UNP P00780 ASN 265 CONFLICT
SEQADV 1SCB ASN A 212 UNP P00780 SER 316 CONFLICT
SEQRES 1 A 274 ALA GLN THR VAL PRO TYR GLY ILE PRO LEU ILE LYS ALA
SEQRES 2 A 274 ASP LYS VAL GLN ALA GLN GLY PHE LYS GLY ALA ASN VAL
SEQRES 3 A 274 LYS VAL ALA VAL LEU ASP THR GLY ILE GLN ALA SER HIS
SEQRES 4 A 274 PRO ASP LEU ASN VAL VAL GLY GLY ALA SER PHE VAL ALA
SEQRES 5 A 274 GLY GLU ALA TYR ASN THR ASP GLY ASN GLY HIS GLY THR
SEQRES 6 A 274 HIS VAL ALA GLY THR VAL ALA ALA LEU ASP ASN THR THR
SEQRES 7 A 274 GLY VAL LEU GLY VAL ALA PRO SER VAL SER LEU TYR ALA
SEQRES 8 A 274 VAL LYS VAL LEU ASN SER SER GLY SER GLY SER TYR SER
SEQRES 9 A 274 GLY ILE VAL SER GLY ILE GLU TRP ALA THR THR ASN GLY
SEQRES 10 A 274 MET ASP VAL ILE ASN MET SER LEU GLY GLY ALA SER GLY
SEQRES 11 A 274 SER THR ALA MET LYS GLN ALA VAL ASP ASN ALA TYR ALA
SEQRES 12 A 274 ARG GLY VAL VAL VAL VAL ALA ALA ALA GLY ASN SER GLY
SEQRES 13 A 274 ASN SER GLY SER THR ASN THR ILE GLY TYR PRO ALA LYS
SEQRES 14 A 274 TYR ASP SER VAL ILE ALA VAL GLY ALA VAL ASP SER ASN
SEQRES 15 A 274 SER ASN ARG ALA SER PHE SER SER VAL GLY ALA GLU LEU
SEQRES 16 A 274 GLU VAL MET ALA PRO GLY ALA GLY VAL TYR SER THR TYR
SEQRES 17 A 274 PRO THR ASN THR TYR ALA THR LEU ASN GLY THR SER MET
SEQRES 18 A 274 ALA SER PRO HIS VAL ALA GLY ALA ALA ALA LEU ILE LEU
SEQRES 19 A 274 SER LYS HIS PRO ASN LEU SER ALA SER GLN VAL ARG ASN
SEQRES 20 A 274 ARG LEU SER SER THR ALA THR TYR LEU GLY SER SER PHE
SEQRES 21 A 274 TYR TYR GLY LYS GLY LEU ILE ASN VAL GLU ALA ALA ALA
SEQRES 22 A 274 GLN
HET CA A 276 1
HET CCN A 404 3
HET CCN A 405 3
HET CCN A 406 3
HET CCN A 407 3
HET CCN A 408 3
HET CCN A 409 3
HET CCN A 410 3
HET CCN A 411 3
HET CCN A 413 3
HET CCN A 414 3
HET CCN A 415 3
HET CCN A 416 3
HETNAM CA CALCIUM ION
HETNAM CCN ACETONITRILE
FORMUL 2 CA CA 2+
FORMUL 3 CCN 12(C2 H3 N)
FORMUL 15 HOH *99(H2 O)
HELIX 1 1 TYR A 6 ILE A 11 1 6
HELIX 2 2 LYS A 12 GLN A 19 1 8
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 GLY A 146 1 15
HELIX 6 6 THR A 220 HIS A 238 1PERTURBATION AT SER 221 19
HELIX 7 7 SER A 242 THR A 253 1 12
HELIX 8 8 ASN A 269 ALA A 274 1 6
SHEET 1 SH1 8 ASN A 43 PHE A 50 0
SHEET 2 SH1 8 SER A 89 VAL A 95 1 O LEU A 90 N VAL A 45
SHEET 3 SH1 8 VAL A 26 ASP A 32 1 O VAL A 28 N TYR A 91
SHEET 4 SH1 8 ASP A 120 MET A 124 1 N ASP A 120 O LYS A 27
SHEET 5 SH1 8 VAL A 148 ALA A 153 1 N VAL A 150 O ILE A 122
SHEET 6 SH1 8 ILE A 175 VAL A 180 1 N ILE A 175 O VAL A 149
SHEET 7 SH1 8 GLU A 197 GLY A 202 1 N GLY A 202 O VAL A 180
SHEET 8 SH1 8 LYS A 265 ILE A 268 1 O GLY A 266 N MET A 199
LINK OE1 GLN A 2 CA CA A 276 1555 1555 2.42
LINK OD2 ASP A 41 CA CA A 276 1555 1555 2.94
LINK OD1 ASP A 41 CA CA A 276 1555 1555 2.42
LINK O LEU A 75 CA CA A 276 1555 1555 2.62
LINK OD1 ASN A 77 CA CA A 276 1555 1555 2.32
LINK O THR A 79 CA CA A 276 1555 1555 2.42
LINK O VAL A 81 CA CA A 276 1555 1555 2.36
CISPEP 1 TYR A 167 PRO A 168 0 5.13
SITE 1 ACT 3 ASP A 32 HIS A 64 SER A 221
SITE 1 AC1 6 GLN A 2 ASP A 41 LEU A 75 ASN A 77
SITE 2 AC1 6 THR A 79 VAL A 81
SITE 1 AC2 5 GLY A 100 LEU A 126 GLY A 127 HOH A 383
SITE 2 AC2 5 CCN A 407
SITE 1 AC3 5 LEU A 126 GLY A 127 GLY A 154 SER A 221
SITE 2 AC3 5 CCN A 407
SITE 1 AC4 5 ASN A 155 ASN A 218 GLY A 219 THR A 220
SITE 2 AC4 5 SER A 221
SITE 1 AC5 6 HIS A 64 GLY A 100 SER A 125 LEU A 126
SITE 2 AC5 6 CCN A 404 CCN A 405
SITE 1 AC6 4 ASN A 62 GLY A 63 TYR A 209 PRO A 210
SITE 1 AC7 3 TYR A 143 SER A 242 SER A 244
SITE 1 AC8 1 ARG A 145
SITE 1 AC9 4 PRO A 9 LYS A 12 ASP A 14 TYR A 262
SITE 1 BC1 4 PHE A 50 VAL A 51 ALA A 52 HOH A 280
SITE 1 BC2 1 ASN A 117
SITE 1 BC3 2 ASP A 60 GLY A 61
SITE 1 BC4 2 ALA A 129 HOH A 389
CRYST1 77.100 55.400 53.600 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 0.012970 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018051 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018657 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
