HEADER HYDROLASE/HYDROLASE INHIBITOR 05-JAN-91 3ER5
TITLE THE ACTIVE SITE OF ASPARTIC PROTEINASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHIAPEPSIN;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.23.6;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: H-189;
COMPND 8 CHAIN: I;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPHONECTRIA PARASITICA;
SOURCE 3 ORGANISM_TAXID: 5116;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES
KEYWDS ACID PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR, HYDROLASE-HYDROLASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BAILEY,B.VEERAPANDIAN,J.COOPER,M.SZELKE,T.L.BLUNDELL
REVDAT 5 29-NOV-17 3ER5 1 HELIX
REVDAT 4 13-JUL-11 3ER5 1 VERSN
REVDAT 3 24-FEB-09 3ER5 1 VERSN
REVDAT 2 15-JUL-92 3ER5 1 AUTHOR
REVDAT 1 15-APR-91 3ER5 0
JRNL AUTH D.BAILEY,J.B.COOPER,B.VEERAPANDIAN,T.L.BLUNDELL,B.ATRASH,
JRNL AUTH 2 D.M.JONES,M.SZELKE
JRNL TITL X-RAY-CRYSTALLOGRAPHIC STUDIES OF COMPLEXES OF PEPSTATIN A
JRNL TITL 2 AND A STATINE-CONTAINING HUMAN RENIN INHIBITOR WITH
JRNL TITL 3 ENDOTHIAPEPSIN.
JRNL REF BIOCHEM.J. V.T 2) 363 1993
JRNL REFN ISSN 0264-6021
JRNL PMID 8424781
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.L.BLUNDELL,H.B.JONES,G.KHAN,G.TAYLOR,T.S.SEWELL,L.H.PEARL,
REMARK 1 AUTH 2 S.P.WOOD
REMARK 1 TITL ACTIVE SITE OF ACID PROTEINASES
REMARK 1 REF PROC.FEBS MEET. V. 60 281 1979
REMARK 1 REFN ISSN 0071-4402
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.L.BLUNDELL,J.A.JENKINS,G.KHAN,P.ROYCHOWDHURY,T.SEWELL,
REMARK 1 AUTH 2 I.J.TICKLE,E.A.WOOD
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF ACID PROTEINASES
REMARK 1 REF PROC.FEBS MEET. V. 52 81 1979
REMARK 1 REFN ISSN 0071-4402
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.L.BLUNDELL,B.T.SEWELL,A.D.MCLACHLAN
REMARK 1 TITL FOUR-FOLD STRUCTURAL REPEAT IN THE ACID PROTEASES
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V. 580 24 1979
REMARK 1 REFN ISSN 0006-3002
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.TANG,M.N.G.JAMES,I.N.HSU,J.A.JENKINS,T.L.BLUNDELL
REMARK 1 TITL STRUCTURAL EVIDENCE FOR GENE DUPLICATION IN THE EVOLUTION OF
REMARK 1 TITL 2 ACID PROTEASES
REMARK 1 REF NATURE V. 271 618 1978
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 5
REMARK 1 AUTH E.SUBRAMANIAN,I.D.A.SWAN,M.LIU,D.R.DAVIES,J.A.JENKINS,
REMARK 1 AUTH 2 I.J.TICKLE,T.L.BLUNDELL
REMARK 1 TITL HOMOLOGY AMONG ACID PROTEASES. COMPARISON OF CRYSTAL
REMARK 1 TITL 2 STRUCTURES AT 3 ANGSTROMS RESOLUTION OF ACID PROTEASES FROM
REMARK 1 TITL 3 RHIZOPUS CHINENSIS AND ENDOTHIA PARASITICA
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 74 556 1977
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 6
REMARK 1 AUTH J.JENKINS,I.TICKLE,T.SEWELL,L.UNGARETTI,A.WOLLMER,T.BLUNDELL
REMARK 1 TITL X-RAY ANALYSIS AND CIRCULAR DICHROISM OF THE ACID PROTEASE
REMARK 1 TITL 2 FROM ENDOTHIA PARASITICA AND CHYMOSIN
REMARK 1 EDIT J.TANG
REMARK 1 REF ADV.EXP.MED.BIOL. V. 95 43 1977
REMARK 1 PUBL PLENUM,NEW YORK
REMARK 1 REFN ISSN 0065-2598
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) : 10.00
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) : 0.150
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 : 2480
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 223
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:
REMARK 3 THE QUANTITY GIVEN IN THE TEMPERATURE FACTOR FIELD OF THE
REMARK 3 *ATOM* AND *HETATM* RECORDS BELOW IS U**2, WHICH IS THE
REMARK 3 MEAN-SQUARE AMPLITUDE OF ATOMIC VIBRATION. THE TEMPERATURE
REMARK 3 FACTOR, B, CAN BE DERIVED BY THE FOLLOWING RELATION -
REMARK 3 B = 8 * (PI)**2 * U**2. IT IS AN INDICATION OF POSSIBLE
REMARK 3 ERRORS IN THE REFINEMENT THAT SOME ARE SLIGHTLY NEGATIVE.
REMARK 4
REMARK 4 3ER5 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_1000178952.
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 (%): 37.45
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 37.70000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE H 189 IS PEPTIDE-LIKE, A MEMBER OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: H 189
REMARK 400 CHAIN: I
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLY E 281 CG LYS I 10 2546 2.16
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 VAL E 18 C GLN E 19 N 0.165
REMARK 500 ILE E 268 C PRO E 269 N 0.124
REMARK 500 PRO E 269 CD PRO E 269 N 0.120
REMARK 500 ASP E 274 C PHE E 275 N 0.195
REMARK 500 PRO I 3 CD PRO I 3 N 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 TYR E 14 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 VAL E 18 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 ASP E 30 CB - CG - OD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLU E 44 OE1 - CD - OE2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 TYR E 75 CB - CG - CD1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP E 83 CB - CG - OD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP E 114 OD1 - CG - OD2 ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASP E 114 CB - CG - OD2 ANGL. DEV. = -12.4 DEGREES
REMARK 500 LEU E 121 CB - CG - CD2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 PRO E 149 O - C - N ANGL. DEV. = -10.5 DEGREES
REMARK 500 VAL E 150 CA - CB - CG1 ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP E 171 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 PHE E 189 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 GLU E 191 OE1 - CD - OE2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 TYR E 246 CB - CG - CD1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 TYR E 246 CG - CD2 - CE2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 PRO E 269 C - N - CA ANGL. DEV. = -12.8 DEGREES
REMARK 500 PRO E 269 C - N - CD ANGL. DEV. = 17.5 DEGREES
REMARK 500 TYR E 272 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 PHE E 275 C - N - CA ANGL. DEV. = -22.4 DEGREES
REMARK 500 PHE E 323 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 PRO I 3 C - N - CA ANGL. DEV. = -19.2 DEGREES
REMARK 500 PRO I 3 C - N - CD ANGL. DEV. = 27.7 DEGREES
REMARK 500 PRO I 3 CA - N - CD ANGL. DEV. = -9.5 DEGREES
REMARK 500 PRO I 3 N - CD - CG ANGL. DEV. = -9.1 DEGREES
REMARK 500 STA I 6 CA - C - N ANGL. DEV. = 16.1 DEGREES
REMARK 500 HIS I 9 CA - CB - CG ANGL. DEV. = -11.5 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 HIS I 9 -62.20 -107.53
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 PRO I 1 HIS I 2 -79.65
REMARK 500 STA I 6 VAL I 7 -117.49
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 E 265 0.09 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 VAL E 18 20.69
REMARK 500 STA I 6 31.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
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 CHAIN I OF H-189
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE COMPLETE SEQUENCE WAS DETERMINED BY V. PEDERSEN AS
REMARK 999 TRYPTIC FRAGMENTS WHICH WERE ALIGNED IN THE ELECTRON
REMARK 999 DENSITY. HOMOLOGY WITH OTHER ASPARTIC PROTEINASES WAS USED
REMARK 999 TO RESOLVE ALIGNMENT AMBIGUITIES. THE RESIDUE NUMBERING IS
REMARK 999 BASED ON THAT OF PORCINE PEPSIN.
DBREF 3ER5 E -2 326 UNP P11838 CARP_CRYPA 90 419
DBREF 3ER5 I 2 5 UNP P01017 ANGT_BOVIN 6 9
SEQRES 1 E 330 SER THR GLY SER ALA THR THR THR PRO ILE ASP SER LEU
SEQRES 2 E 330 ASP ASP ALA TYR ILE THR PRO VAL GLN ILE GLY THR PRO
SEQRES 3 E 330 ALA GLN THR LEU ASN LEU ASP PHE ASP THR GLY SER SER
SEQRES 4 E 330 ASP LEU TRP VAL PHE SER SER GLU THR THR ALA SER GLU
SEQRES 5 E 330 VAL ASP GLY GLN THR ILE TYR THR PRO SER LYS SER THR
SEQRES 6 E 330 THR ALA LYS LEU LEU SER GLY ALA THR TRP SER ILE SER
SEQRES 7 E 330 TYR GLY ASP GLY SER SER SER SER GLY ASP VAL TYR THR
SEQRES 8 E 330 ASP THR VAL SER VAL GLY GLY LEU THR VAL THR GLY GLN
SEQRES 9 E 330 ALA VAL GLU SER ALA LYS LYS VAL SER SER SER PHE THR
SEQRES 10 E 330 GLU ASP SER THR ILE ASP GLY LEU LEU GLY LEU ALA PHE
SEQRES 11 E 330 SER THR LEU ASN THR VAL SER PRO THR GLN GLN LYS THR
SEQRES 12 E 330 PHE PHE ASP ASN ALA LYS ALA SER LEU ASP SER PRO VAL
SEQRES 13 E 330 PHE THR ALA ASP LEU GLY TYR HIS ALA PRO GLY THR TYR
SEQRES 14 E 330 ASN PHE GLY PHE ILE ASP THR THR ALA TYR THR GLY SER
SEQRES 15 E 330 ILE THR TYR THR ALA VAL SER THR LYS GLN GLY PHE TRP
SEQRES 16 E 330 GLU TRP THR SER THR GLY TYR ALA VAL GLY SER GLY THR
SEQRES 17 E 330 PHE LYS SER THR SER ILE ASP GLY ILE ALA ASP THR GLY
SEQRES 18 E 330 THR THR LEU LEU TYR LEU PRO ALA THR VAL VAL SER ALA
SEQRES 19 E 330 TYR TRP ALA GLN VAL SER GLY ALA LYS SER SER SER SER
SEQRES 20 E 330 VAL GLY GLY TYR VAL PHE PRO CYS SER ALA THR LEU PRO
SEQRES 21 E 330 SER PHE THR PHE GLY VAL GLY SER ALA ARG ILE VAL ILE
SEQRES 22 E 330 PRO GLY ASP TYR ILE ASP PHE GLY PRO ILE SER THR GLY
SEQRES 23 E 330 SER SER SER CYS PHE GLY GLY ILE GLN SER SER ALA GLY
SEQRES 24 E 330 ILE GLY ILE ASN ILE PHE GLY ASP VAL ALA LEU LYS ALA
SEQRES 25 E 330 ALA PHE VAL VAL PHE ASN GLY ALA THR THR PRO THR LEU
SEQRES 26 E 330 GLY PHE ALA SER LYS
SEQRES 1 I 10 PRO HIS PRO PHE HIS STA VAL ILE HIS LYS
HET STA I 6 11
HETNAM STA STATINE
FORMUL 2 STA C8 H17 N O3
FORMUL 3 HOH *223(H2 O)
HELIX 1 H1 THR E 57 SER E 61 1 5
HELIX 2 H2 SER E 108 GLU E 113 1 6
HELIX 3 H3 THR E 137 LYS E 143 1 7
HELIX 4 H4 PRO E 224 GLN E 234 1 11
HELIX 5 H5 GLY E 303 LYS E 308 1 6
SHEET 1 N1 8 THR E -1 ILE E 7 0
SHEET 2 N1 8 ALA E 13 GLY E 21 -1 N ILE E 15 O THR E 5
SHEET 3 N1 8 ALA E 24 THR E 33 -1 N LEU E 29 O THR E 16
SHEET 4 N1 8 ILE E 117 ALA E 124 1 N LEU E 121 O ASP E 30
SHEET 5 N1 8 SER E 36 GLU E 44 -1 N TRP E 39 O LEU E 120
SHEET 6 N1 8 GLN E 99 LYS E 105 1 N ALA E 104 O VAL E 40
SHEET 7 N1 8 GLY E 78 ASP E 87 -1 N ASP E 83 O SER E 103
SHEET 8 N1 8 TRP E 71 GLY E 76 -1 N TRP E 71 O GLY E 82
SHEET 1 C1 8 SER E 178 LYS E 186 0
SHEET 2 C1 8 PHE E 189 THR E 195 -1 N GLU E 191 O SER E 184A
SHEET 3 C1 8 ASP E 211 THR E 216 -1 N GLY E 212 O TRP E 192
SHEET 4 C1 8 ILE E 299 PHE E 302 1 N PHE E 302 O ILE E 213
SHEET 5 C1 8 THR E 219 PRO E 224 -1 N TYR E 222 O ILE E 301
SHEET 6 C1 8 SER E 282 SER E 294 1 N GLN E 288 O LEU E 221
SHEET 7 C1 8 GLY E 244 CYS E 250 -1 N PHE E 248 O CYS E 283
SHEET 8 C1 8 ALA E 238 SER E 241 -1 N LYS E 238A O VAL E 247
SHEET 1 N2 4 ALA E 24 ASN E 28 0
SHEET 2 N2 4 PRO E 17 GLY E 21 -1 N ILE E 20 O GLN E 25
SHEET 3 N2 4 VAL E 89 VAL E 91 -1 N SER E 90 O GLN E 19
SHEET 4 N2 4 LEU E 94 VAL E 96 -1 N VAL E 96 O VAL E 89
SHEET 1 C2 4 GLY E 202 LYS E 204 0
SHEET 2 C2 4 GLY E 196 VAL E 199 -1 N TYR E 197 O LYS E 204
SHEET 3 C2 4 SER E 256 VAL E 261 -1 N GLY E 260 O GLY E 196
SHEET 4 C2 4 ALA E 264 ILE E 268 -1 N ILE E 266 O PHE E 259
SHEET 1 NC 6 THR E -1 ILE E 7 0
SHEET 2 NC 6 PRO E 162 THR E 172 -1 N TYR E 165 O ALA E 2
SHEET 3 NC 6 SER E 148 TYR E 157 -1 N ASP E 154 O THR E 164
SHEET 4 NC 6 ALA E 310 GLY E 316 -1 N VAL E 312 O ALA E 153
SHEET 5 NC 6 THR E 319 LYS E 326 -1 N GLY E 322 O VAL E 313
SHEET 6 NC 6 SER E 178 LYS E 186 -1 N THR E 182 O LEU E 321
SSBOND 1 CYS E 250 CYS E 283 1555 1555 2.04
LINK C HIS I 5 N STA I 6 1555 1555 1.33
LINK C STA I 6 N VAL I 7 1555 1555 1.34
CISPEP 1 THR E 22 PRO E 23 0 1.30
CISPEP 2 SER E 132 PRO E 133 0 -1.67
SITE 1 CAT 2 ASP E 32 ASP E 215
SITE 1 AC1 11 ASP E 12 TYR E 75 GLY E 76 ASP E 77
SITE 2 AC1 11 ASP E 114 GLY E 217 THR E 218 THR E 219
SITE 3 AC1 11 ILE E 301 HOH I 11 HOH I 16
CRYST1 43.100 75.400 42.800 90.00 97.00 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 0.023202 0.000000 0.002849 0.00000
SCALE2 0.000000 0.013263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023540 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
