HEADER HYDROLASE/HYDROLASE INHIBITOR 18-APR-86 1SGC
TITLE THE 1.8 ANGSTROMS STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND
TITLE 2 STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE
TITLE 3 CATALYTIC TETRAHEDRAL INTERMEDIATES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CHYMOSTATIN A;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES GRISEUS;
SOURCE 3 ORGANISM_TAXID: 1911;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES
KEYWDS HYDROLASE (SERINE PROTEINASE), HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.T.J.DELBAERE,G.D.BRAYER
REVDAT 4 13-JUL-11 1SGC 1 VERSN
REVDAT 3 24-FEB-09 1SGC 1 VERSN
REVDAT 2 01-APR-03 1SGC 1 JRNL
REVDAT 1 14-JUL-86 1SGC 0
JRNL AUTH L.T.DELBAERE,G.D.BRAYER
JRNL TITL THE 1.8 A STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND
JRNL TITL 2 STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE
JRNL TITL 3 CATALYTIC TETRAHEDRAL INTERMEDIATES.
JRNL REF J.MOL.BIOL. V. 183 89 1985
JRNL REFN ISSN 0022-2836
JRNL PMID 3892018
JRNL DOI 10.1016/0022-2836(85)90283-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.T.J.DELBAERE,G.D.BRAYER
REMARK 1 TITL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE
REMARK 1 TITL 2 BACTERIAL-PRODUCED INHIBITOR CHYMOSTATIN AND THE SERINE
REMARK 1 TITL 3 ENZYME STREPTOMYCES GRISEUS PROTEASE A
REMARK 1 REF J.MOL.BIOL. V. 139 45 1980
REMARK 1 REFN ISSN 0022-2836
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) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.123
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 : 1303
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 217
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) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
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 1SGC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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 : 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 (%): 46.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42
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 -Y,X,Z+1/2
REMARK 290 4555 Y,-X,Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.31500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.31500
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 APPLY THE FOLLOWING TO CHAINS: A, B
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 281 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 295 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 252 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 357 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE INHIBITOR CHYMOSTATIN A HAS LAST RESIDUE PHENYLALANINAL
REMARK 400 REPRESENTED WITH ALTERNATE CONFORMATIONS ON ITS TERMINAL OXYGEN.
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 ARG A 221 CG CD NE CZ NH1 NH2
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 GLY A 202 N GLY A 202 CA 0.119
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 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG A 41 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 HIS A 57 ND1 - CE1 - NE2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 HIS A 57 CE1 - NE2 - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 115 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 117 CD - NE - CZ ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ASP A 123 CB - CG - OD1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 PHE A 131 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 138 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 SER A 141 CA - CB - OG ANGL. DEV. = 20.7 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 TYR A 171 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 194 CB - CG - OD2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 GLY A 197 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 PHE A 200 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 CYS A 220 CB - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 THR A 232 CA - CB - OG1 ANGL. DEV. = -12.6 DEGREES
REMARK 500 GLU A 233 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 TYR A 237 CG - CD2 - CE2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 LEU A 242 CB - CG - CD1 ANGL. DEV. = -10.7 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 PRO A 99A -154.01 -77.91
REMARK 500 ASN A 100 -69.12 81.18
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 PHE B 1 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 456 DISTANCE = 5.61 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF CHYMOSTATIN A
DBREF 1SGC A 16 242 UNP P00776 PRTA_STRGR 117 297
DBREF 1SGC B 1 4 PDB 1SGC 1SGC 1 4
SEQADV 1SGC GLN A 192A UNP P00776 GLU 249 CONFLICT
SEQRES 1 A 181 ILE ALA GLY GLY GLU ALA ILE THR THR GLY GLY SER ARG
SEQRES 2 A 181 CYS SER LEU GLY PHE ASN VAL SER VAL ASN GLY VAL ALA
SEQRES 3 A 181 HIS ALA LEU THR ALA GLY HIS CYS THR ASN ILE SER ALA
SEQRES 4 A 181 SER TRP SER ILE GLY THR ARG THR GLY THR SER PHE PRO
SEQRES 5 A 181 ASN ASN ASP TYR GLY ILE ILE ARG HIS SER ASN PRO ALA
SEQRES 6 A 181 ALA ALA ASP GLY ARG VAL TYR LEU TYR ASN GLY SER TYR
SEQRES 7 A 181 GLN ASP ILE THR THR ALA GLY ASN ALA PHE VAL GLY GLN
SEQRES 8 A 181 ALA VAL GLN ARG SER GLY SER THR THR GLY LEU ARG SER
SEQRES 9 A 181 GLY SER VAL THR GLY LEU ASN ALA THR VAL ASN TYR GLY
SEQRES 10 A 181 SER SER GLY ILE VAL TYR GLY MET ILE GLN THR ASN VAL
SEQRES 11 A 181 CYS ALA GLN PRO GLY ASP SER GLY GLY SER LEU PHE ALA
SEQRES 12 A 181 GLY SER THR ALA LEU GLY LEU THR SER GLY GLY SER GLY
SEQRES 13 A 181 ASN CYS ARG THR GLY GLY THR THR PHE TYR GLN PRO VAL
SEQRES 14 A 181 THR GLU ALA LEU SER ALA TYR GLY ALA THR VAL LEU
SEQRES 1 B 4 PHE CSI LEU PHA
MODRES 1SGC PHA B 4 PHE PHENYLALANINAL
HET CSI B 2 13
HET PHA B 4 12
HETNAM CSI AMINO-(2-IMINO-HEXAHYDRO-PYRIMIDIN-4-YL)-ACETIC ACID
HETNAM PHA PHENYLALANINAL
FORMUL 2 CSI C7 H12 N4 O4
FORMUL 2 PHA C9 H11 N O
FORMUL 3 HOH *217(H2 O)
HELIX 1 H1 GLY A 56 ILE A 63 1 6
HELIX 2 H2 PRO A 230 ALA A 236 1 8
SHEET 1 S1 3 ILE A 16 GLY A 18 0
SHEET 2 S1 3 ASP A 115 LEU A 120 1
SHEET 3 S1 3 SER A 120D ILE A 124 -1
SHEET 1 S2 2 GLY A 19 THR A 33 0
SHEET 2 S2 2 GLY A 39 LEU A 44 -1
SHEET 1 S3 5 GLY A 45 VAL A 48B 0
SHEET 2 S3 5 VAL A 49 THR A 54 -1
SHEET 3 S3 5 GLY A 104 HIS A 108 -1
SHEET 4 S3 5 GLY A 86 SER A 93 -1
SHEET 5 S3 5 ALA A 65 TRP A 66 -1
SHEET 1 S4 3 THR A 126 GLY A 128 0
SHEET 2 S4 3 SER A 207 ALA A 209 1
SHEET 3 S4 3 PHE A 200 ALA A 201 -1
SHEET 1 S5 6 GLY A 197 LEU A 199 0
SHEET 2 S5 6 LEU A 210 ASN A 219 -1
SHEET 3 S5 6 GLY A 223 GLN A 229 -1
SHEET 4 S5 6 ILE A 181 THR A 183 -1
SHEET 5 S5 6 SER A 161 ASN A 166 -1
SHEET 6 S5 6 GLN A 134 GLY A 140 -1
SHEET 1 S6 2 ALA A 167 TYR A 171 0
SHEET 2 S6 2 GLY A 175 MET A 180 -1
SSBOND 1 CYS A 42 CYS A 58 1555 1555 1.99
SSBOND 2 CYS A 191 CYS A 220 1555 1555 2.01
LINK N PHE B 1 C7 CSI B 2 1555 1555 1.31
LINK C CSI B 2 N LEU B 3 1555 1555 1.34
LINK OG SER A 195 C PHA B 4 1555 1555 1.62
LINK C LEU B 3 N PHA B 4 1555 1555 1.32
CISPEP 1 PHE A 94 PRO A 99A 0 -7.14
SITE 1 AC1 18 HIS A 57 VAL A 169 TYR A 171 SER A 174
SITE 2 AC1 18 ALA A 192 GLY A 193 ASP A 194 SER A 195
SITE 3 AC1 18 SER A 214 GLY A 215 GLY A 216 SER A 217
SITE 4 AC1 18 PHE A 227 HOH B 386 HOH B 442 HOH B 443
SITE 5 AC1 18 HOH B 453 HOH B 454
CRYST1 55.050 55.050 54.630 90.00 90.00 90.00 P 42 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 0.018165 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018165 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018305 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
