HEADER COMPLEX(SERINE PROTEINASE-INHIBITOR) 05-SEP-88 2SEC
TITLE STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR
TITLE 2 COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBTILISIN CARLSBERG;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.21.62;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: EGLIN C;
COMPND 8 CHAIN: I;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;
SOURCE 3 ORGANISM_TAXID: 1402;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HIRUDO MEDICINALIS;
SOURCE 6 ORGANISM_COMMON: MEDICINAL LEECH;
SOURCE 7 ORGANISM_TAXID: 6421;
SOURCE 8 EXPRESSION_SYSTEM: UNIDENTIFIED;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 32644
KEYWDS COMPLEX(SERINE PROTEINASE-INHIBITOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.MCPHALEN,M.N.G.JAMES
REVDAT 8 21-FEB-24 2SEC 1 REMARK SEQADV LINK
REVDAT 7 29-NOV-17 2SEC 1 HELIX
REVDAT 6 24-FEB-09 2SEC 1 VERSN
REVDAT 5 01-APR-03 2SEC 1 JRNL
REVDAT 4 15-JAN-95 2SEC 1 COMPND
REVDAT 3 15-OCT-89 2SEC 1 SEQRES
REVDAT 2 19-APR-89 2SEC 1 JRNL
REVDAT 1 07-SEP-88 2SEC 0
SPRSDE 07-SEP-88 2SEC 1SEC
JRNL AUTH C.A.MCPHALEN,M.N.JAMES
JRNL TITL STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN
JRNL TITL 2 INHIBITOR COMPLEXES: EGLIN-C-SUBTILISIN CARLSBERG AND
JRNL TITL 3 CI-2-SUBTILISIN NOVO.
JRNL REF BIOCHEMISTRY V. 27 6582 1988
JRNL REFN ISSN 0006-2960
JRNL PMID 3064813
JRNL DOI 10.1021/BI00417A058
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.A.MCPHALEN,H.P.SCHNEBLI,M.N.G.JAMES
REMARK 1 TITL CRYSTAL AND MOLECULAR STRUCTURE OF THE INHIBITOR EGLIN FROM
REMARK 1 TITL 2 LEECHES IN COMPLEX WITH SUBTILISIN CARLSBERG
REMARK 1 REF FEBS LETT. V. 188 55 1985
REMARK 1 REFN ISSN 0014-5793
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) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 27094
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) : 0.136
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 : 2450
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 170
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) : 0.009 ; 0.008
REMARK 3 ANGLE DISTANCE (A) : 0.027 ; 0.016
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.031 ; 0.016
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.017 ; 0.012
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.146 ; 0.080
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 2SEC 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_1000178621.
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 (%): 46.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
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 THR I 15
REMARK 465 GLU I 16
REMARK 465 PHE I 17
REMARK 465 GLY I 18
REMARK 465 SER I 19
REMARK 465 GLU I 20
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 E 112 CD GLU E 112 OE2 0.068
REMARK 500 GLU E 271 CD GLU E 271 OE2 0.069
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 ASP E 14 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP E 14 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP E 41 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG E 145 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG E 249 NE - CZ - NH1 ANGL. DEV. = 4.4 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 ASN E 25 -0.47 74.52
REMARK 500 ASP E 32 -148.84 -161.18
REMARK 500 ALA E 73 25.13 -142.80
REMARK 500 ASN E 77 -148.74 -152.56
REMARK 500 ASP E 181 -169.74 -107.72
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 E 276 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 2 OE1
REMARK 620 2 ASP E 41 OD1 151.3
REMARK 620 3 ASP E 41 OD2 156.2 52.4
REMARK 620 4 LEU E 75 O 78.9 88.4 110.5
REMARK 620 5 ASN E 77 ND2 74.4 79.7 126.0 88.8
REMARK 620 6 THR E 79 O 89.2 96.5 85.2 162.9 76.1
REMARK 620 7 VAL E 81 O 79.7 125.7 79.0 87.5 154.1 102.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 278 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA E 37 O
REMARK 620 2 HIS E 39 O 88.8
REMARK 620 3 LEU E 42 O 100.8 76.3
REMARK 620 4 HOH E 373 O 55.9 129.9 77.1
REMARK 620 5 HOH E 463 O 171.0 85.8 70.9 123.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 277 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA E 169 O
REMARK 620 2 TYR E 171 O 88.1
REMARK 620 3 VAL E 174 O 96.0 79.8
REMARK 620 4 HOH E 361 O 108.8 152.3 76.9
REMARK 620 5 HOH E 430 O 129.9 93.0 133.5 92.4
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 THE CROSS-OVER CONNECTION BETWEEN STRANDS 1 AND 2 OF SHEET
REMARK 700 S1E IS LEFT-HANDED.
REMARK 700 THE BETA-SHEET OF THE INHIBITOR IS IRREGULAR, WITH
REMARK 700 WELL-ORDERED WATER MOLECULES PROVIDING ALL HYDROGEN-BONDING
REMARK 700 BRIDGES BETWEEN STRANDS 2 AND 3. SEE THE REFERENCE CITED
REMARK 700 ON THE *JRNL* RECORDS ABOVE.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: catalytic site
REMARK 800
REMARK 800 SITE_IDENTIFIER: IO1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ion binding site
REMARK 800
REMARK 800 SITE_IDENTIFIER: IO2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ion binding site
REMARK 800
REMARK 800 SITE_IDENTIFIER: IO3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ion binding site
REMARK 800
REMARK 800 SITE_IDENTIFIER: RSB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: inhibitor reactive site
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 278
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SUBTILISIN HAS BEEN ASSIGNED CHAIN IDENTIFIER *E* AND EGLIN
REMARK 999 C HAS BEEN ASSIGNED CHAIN IDENTIFIER *I*. THE AMINO ACID
REMARK 999 SEQUENCE NUMBERING USED FOR EGLIN C IS BASED ON A SEQUENCE
REMARK 999 ALIGNMENT WITH CHYMOTRYPSIN INHIBITOR 2 (CI-2) AND USES THE
REMARK 999 CI-2 NUMBERING SCHEME.
REMARK 999
REMARK 999 THE STRUCTURE OF SUBTILISIN CARLSBERG WAS REFINED ON THE
REMARK 999 BASIS OF THE PUBLISHED AMINO ACID SEQUENCE OF THE PROTEIN
REMARK 999 (E.L.SMITH ET AL., J. BIOL. CHEM., V. 243, P. 2184, 1968).
REMARK 999 THE DNA SEQUENCE OF A CARLSBERG-LIKE ENZYME FROM BACILLUS
REMARK 999 LICHENIFORMIS (JACOBS ET AL., NUCLEIC ACIDS RES., V. 13,
REMARK 999 P. 8913, 1985) DIFFERS FROM THE ORIGINAL AMINO ACID
REMARK 999 SEQUENCE OF SUBTILISIN CARLSBERG AT FIVE POSITIONS -
REMARK 999
REMARK 999 SMITH JACOBS
REMARK 999 SER E 103 THR E 103
REMARK 999 ALA E 129 PRO E 129
REMARK 999 ASN E 158 SER E 158
REMARK 999 SER E 161 ASN E 161
REMARK 999 ASN E 212 SER E 212
REMARK 999
REMARK 999 THE ELECTRON DENSITY AT POSITION 158 COULD BE CONSISTENT
REMARK 999 WITH THE DNA SEQUENCE. THE DENSITY AT THE OTHER FOUR
REMARK 999 POSITIONS IS CONSISTENT WITH THE RESULTS OF THE PROTEIN
REMARK 999 SEQUENCING.
DBREF 2SEC E 1 275 UNP P00780 SUBT_BACLI 106 379
DBREF 2SEC I 15 83 UNP P01051 ICIC_HIRME 1 70
SEQADV 2SEC SER E 103 UNP P00780 THR 207 CONFLICT
SEQADV 2SEC ALA E 129 UNP P00780 PRO 233 CONFLICT
SEQADV 2SEC ASN E 158 UNP P00780 SER 262 CONFLICT
SEQADV 2SEC SER E 161 UNP P00780 ASN 265 CONFLICT
SEQADV 2SEC ASN E 212 UNP P00780 SER 316 CONFLICT
SEQADV 2SEC ASN I 47 UNP P01051 ASP 33 CONFLICT
SEQRES 1 E 274 ALA GLN THR VAL PRO TYR GLY ILE PRO LEU ILE LYS ALA
SEQRES 2 E 274 ASP LYS VAL GLN ALA GLN GLY PHE LYS GLY ALA ASN VAL
SEQRES 3 E 274 LYS VAL ALA VAL LEU ASP THR GLY ILE GLN ALA SER HIS
SEQRES 4 E 274 PRO ASP LEU ASN VAL VAL GLY GLY ALA SER PHE VAL ALA
SEQRES 5 E 274 GLY GLU ALA TYR ASN THR ASP GLY ASN GLY HIS GLY THR
SEQRES 6 E 274 HIS VAL ALA GLY THR VAL ALA ALA LEU ASP ASN THR THR
SEQRES 7 E 274 GLY VAL LEU GLY VAL ALA PRO SER VAL SER LEU TYR ALA
SEQRES 8 E 274 VAL LYS VAL LEU ASN SER SER GLY SER GLY SER TYR SER
SEQRES 9 E 274 GLY ILE VAL SER GLY ILE GLU TRP ALA THR THR ASN GLY
SEQRES 10 E 274 MET ASP VAL ILE ASN MET SER LEU GLY GLY ALA SER GLY
SEQRES 11 E 274 SER THR ALA MET LYS GLN ALA VAL ASP ASN ALA TYR ALA
SEQRES 12 E 274 ARG GLY VAL VAL VAL VAL ALA ALA ALA GLY ASN SER GLY
SEQRES 13 E 274 ASN SER GLY SER THR ASN THR ILE GLY TYR PRO ALA LYS
SEQRES 14 E 274 TYR ASP SER VAL ILE ALA VAL GLY ALA VAL ASP SER ASN
SEQRES 15 E 274 SER ASN ARG ALA SER PHE SER SER VAL GLY ALA GLU LEU
SEQRES 16 E 274 GLU VAL MET ALA PRO GLY ALA GLY VAL TYR SER THR TYR
SEQRES 17 E 274 PRO THR ASN THR TYR ALA THR LEU ASN GLY THR SER MET
SEQRES 18 E 274 ALA SER PRO HIS VAL ALA GLY ALA ALA ALA LEU ILE LEU
SEQRES 19 E 274 SER LYS HIS PRO ASN LEU SER ALA SER GLN VAL ARG ASN
SEQRES 20 E 274 ARG LEU SER SER THR ALA THR TYR LEU GLY SER SER PHE
SEQRES 21 E 274 TYR TYR GLY LYS GLY LEU ILE ASN VAL GLU ALA ALA ALA
SEQRES 22 E 274 GLN
SEQRES 1 I 70 THR GLU PHE GLY SER GLU LEU LYS SER PHE PRO GLU VAL
SEQRES 2 I 70 VAL GLY LYS THR VAL ASP GLN ALA ARG GLU TYR PHE THR
SEQRES 3 I 70 LEU HIS TYR PRO GLN TYR ASN VAL TYR PHE LEU PRO GLU
SEQRES 4 I 70 GLY SER PRO VAL THR LEU ASP LEU ARG TYR ASN ARG VAL
SEQRES 5 I 70 ARG VAL PHE TYR ASN PRO GLY THR ASN VAL VAL ASN HIS
SEQRES 6 I 70 VAL PRO HIS VAL GLY
HET CA E 276 1
HET CA E 277 1
HET CA E 278 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 3(CA 2+)
FORMUL 6 HOH *170(H2 O)
HELIX 1 EA TYR E 6 ILE E 11 1 6
HELIX 2 EB ALA E 13 ALA E 18 1 6
HELIX 3 EC GLY E 63 ALA E 74 1 12
HELIX 4 ED SER E 103 ASN E 117 1 15
HELIX 5 EE SER E 132 ARG E 145 1 14
HELIX 6 EF THR E 220 HIS E 238 1INTERRUPTED BY PRO 225 19
HELIX 7 EG SER E 242 SER E 252 1 11
HELIX 8 EH SER E 259 GLY E 264 1 6
HELIX 9 EI ASN E 269 ALA E 274 1 6
HELIX 10 IA THR I 31 TYR I 43 1 13
SHEET 1 S1E 7 GLY E 46 PHE E 50 0
SHEET 2 S1E 7 SER E 89 VAL E 95 1 N ALA E 92 O GLY E 46
SHEET 3 S1E 7 VAL E 26 ASP E 32 1 N ASP E 32 O VAL E 93
SHEET 4 S1E 7 ASP E 120 MET E 124 1 O VAL E 121 N ALA E 29
SHEET 5 S1E 7 VAL E 148 ALA E 153 1 O VAL E 148 N ILE E 122
SHEET 6 S1E 7 ILE E 175 VAL E 180 1 N ILE E 175 O VAL E 149
SHEET 7 S1E 7 VAL E 198 GLY E 202 1 O VAL E 198 N GLY E 178
SHEET 1 S2E 2 VAL E 205 TYR E 209 0
SHEET 2 S2E 2 THR E 213 LEU E 217 -1 O LEU E 217 N VAL E 205
SHEET 1 S1I 4 LYS I 22 PHE I 24 0
SHEET 2 S1I 4 PRO I 80 VAL I 82 -1 N VAL I 82 O LYS I 22
SHEET 3 S1I 4 ASN I 64 TYR I 70 -1
SHEET 4 S1I 4 ASN I 47 GLU I 53 1 N ASN I 47 O ASN I 64
LINK OE1 GLN E 2 CA CA E 276 1555 1555 2.39
LINK O ALA E 37 CA CA E 278 1555 1555 2.81
LINK O HIS E 39 CA CA E 278 1555 1555 2.64
LINK OD1 ASP E 41 CA CA E 276 1555 1555 2.35
LINK OD2 ASP E 41 CA CA E 276 1555 1555 2.55
LINK O LEU E 42 CA CA E 278 1555 1555 2.58
LINK O LEU E 75 CA CA E 276 1555 1555 2.23
LINK ND2 ASN E 77 CA CA E 276 1555 1555 2.37
LINK O THR E 79 CA CA E 276 1555 1555 2.41
LINK O VAL E 81 CA CA E 276 1555 1555 2.28
LINK O ALA E 169 CA CA E 277 1555 1555 2.57
LINK O TYR E 171 CA CA E 277 1555 1555 2.57
LINK O VAL E 174 CA CA E 277 1555 1555 2.54
LINK CA CA E 277 O HOH E 361 1555 1555 2.59
LINK CA CA E 277 O HOH E 430 1555 1555 2.53
LINK CA CA E 278 O HOH E 373 1555 1555 3.17
LINK CA CA E 278 O HOH E 463 1555 1555 3.06
CISPEP 1 TYR E 167 PRO E 168 0 8.40
CISPEP 2 PRO E 210 THR E 211 0 -5.16
SITE 1 ACT 3 ASP E 32 HIS E 64 SER E 221
SITE 1 IO1 6 GLN E 2 ASP E 41 LEU E 75 ASN E 77
SITE 2 IO1 6 THR E 79 VAL E 81
SITE 1 IO2 5 ALA E 169 TYR E 171 VAL E 174 HOH E 361
SITE 2 IO2 5 HOH E 430
SITE 1 IO3 5 ALA E 37 HIS E 39 LEU E 42 HOH E 373
SITE 2 IO3 5 HOH E 463
SITE 1 RSB 2 LEU I 59 ASP I 60
SITE 1 AC1 6 GLN E 2 ASP E 41 LEU E 75 ASN E 77
SITE 2 AC1 6 THR E 79 VAL E 81
SITE 1 AC2 5 ALA E 169 TYR E 171 VAL E 174 HOH E 361
SITE 2 AC2 5 HOH E 430
SITE 1 AC3 3 ALA E 37 HIS E 39 LEU E 42
CRYST1 38.310 41.410 56.500 69.51 83.67 75.32 P 1 1
ORIGX1 0.026103 -0.006838 -0.000642 0.00000
ORIGX2 0.000000 0.024964 -0.008876 0.00000
ORIGX3 0.000000 0.000000 0.018900 0.00000
SCALE1 0.026103 -0.006838 -0.000642 0.00000
SCALE2 0.000000 0.024964 -0.008876 0.00000
SCALE3 0.000000 0.000000 0.018900 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
