HEADER HYDROLASE/HYDROLASE INHIBITOR 27-JUL-94 1EPM
TITLE A STRUCTURAL COMPARISON OF 21 INHIBITOR COMPLEXES OF THE ASPARTIC
TITLE 2 PROTEINASE FROM ENDOTHIA PARASITICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHIAPEPSIN;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.23.22;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PS2, THR-PHE-GLN-ALA-PSA-LEU-ARG-GLU;
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
KEYWDS ACID PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CRAWFORD,J.B.COOPER,P.STROP,T.L.BLUNDELL
REVDAT 4 29-NOV-17 1EPM 1 HELIX
REVDAT 3 13-JUL-11 1EPM 1 VERSN
REVDAT 2 24-FEB-09 1EPM 1 VERSN
REVDAT 1 20-DEC-94 1EPM 0
JRNL AUTH D.BAILEY,J.B.COOPER
JRNL TITL A STRUCTURAL COMPARISON OF 21 INHIBITOR COMPLEXES OF THE
JRNL TITL 2 ASPARTIC PROTEINASE FROM ENDOTHIA PARASITICA.
JRNL REF PROTEIN SCI. V. 3 2129 1994
JRNL REFN ISSN 0961-8368
JRNL PMID 7703859
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.L.BLUNDELL,J.JENKINS,B.T.SEWELL,L.H.PEARL,J.B.COOPER,
REMARK 1 AUTH 2 I.J.TICKLE,B.VEERAPANDIAN,S.P.WOOD
REMARK 1 TITL THE 3D STRUCTURE AT 2 ANGSTROMS RESOLUTION OF ENDOTHIAPEPSIN
REMARK 1 REF J.MOL.BIOL. V. 211 919 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : RESTRAIN
REMARK 3 AUTHORS : MOSS,DRIESSEN,HANEEF,HOWLIN,HARRIS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) : 0.170
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 : 2463
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 281
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 1EPM 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_1000173117.
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 (%): 38.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
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 37.94000
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: 1930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 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 O LEU I 2A CB ARG I 3A 1.76
REMARK 500 O HOH E 531 O HOH E 586 2.00
REMARK 500
REMARK 500 REMARK: 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 HOH E 564 O HOH E 575 2555 0.29
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 E 49 CD GLU E 49 OE2 0.067
REMARK 500 GLN E 134A CD GLN E 134A OE1 0.159
REMARK 500 HIS E 158 CG HIS E 158 CD2 0.055
REMARK 500 GLY E 188 N GLY E 188 CA 0.101
REMARK 500 TYR E 246 CD1 TYR E 246 CE1 0.106
REMARK 500 SER E 282 CB SER E 282 OG 0.085
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 SER E 9 O - C - N ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP E 11 CB - CG - OD1 ANGL. DEV. = -8.4 DEGREES
REMARK 500 PRO E 17 CA - N - CD ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP E 30 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP E 30 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 PHE E 31 CB - CG - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 PHE E 31 CG - CD2 - CE2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP E 37 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 TRP E 39 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TRP E 39 CB - CG - CD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 TRP E 39 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP E 51 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 ASP E 51 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP E 51 CA - C - O ANGL. DEV. = 33.5 DEGREES
REMARK 500 ASP E 51 CA - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP E 51 O - C - N ANGL. DEV. = -20.1 DEGREES
REMARK 500 SER E 67 O - C - N ANGL. DEV. = 16.0 DEGREES
REMARK 500 TRP E 71 NE1 - CE2 - CZ2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP E 71 CG - CD2 - CE3 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TYR E 75 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR E 75 CD1 - CE1 - CZ ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP E 77 CB - CG - OD1 ANGL. DEV. = 10.5 DEGREES
REMARK 500 ASP E 77 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 SER E 80A O - C - N ANGL. DEV. = -13.0 DEGREES
REMARK 500 GLY E 82 C - N - CA ANGL. DEV. = -12.7 DEGREES
REMARK 500 TYR E 85 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR E 85 CD1 - CG - CD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 TYR E 85 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR E 85 CG - CD2 - CE2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLY E 98 O - C - N ANGL. DEV. = 13.1 DEGREES
REMARK 500 PHE E 111 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 PHE E 138 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 PHE E 139 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 PHE E 139 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 PHE E 151 N - CA - CB ANGL. DEV. = 11.4 DEGREES
REMARK 500 TYR E 157 CB - CG - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TYR E 157 CB - CG - CD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TYR E 157 CG - CD1 - CE1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 TYR E 157 CG - CD2 - CE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 TYR E 157 CD1 - CE1 - CZ ANGL. DEV. = -13.5 DEGREES
REMARK 500 TYR E 165 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TYR E 165 CB - CG - CD1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 TYR E 165 CG - CD2 - CE2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 TYR E 165 CZ - CE2 - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 PHE E 167 CB - CG - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 PHE E 167 CD1 - CG - CD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 PHE E 167 CG - CD2 - CE2 ANGL. DEV. = -12.1 DEGREES
REMARK 500 PHE E 167 CD1 - CE1 - CZ ANGL. DEV. = -8.5 DEGREES
REMARK 500 PHE E 167 CZ - CE2 - CD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 PHE E 169 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 103 ANGLE DEVIATIONS.
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 E 51 76.87 -153.93
REMARK 500 ARG I 3A 151.14 139.73
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 PSA I 1 LEU I 2A -120.09
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 I 3A 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 PSA I 1 31.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 RESIDUE I 5 IS A STANDARD THR.
REMARK 600 RESIDUE I 4 IS A STANDARD PHE.
REMARK 600 RESIDUE I 3 IS A STANDARD GLN.
REMARK 600 RESIDUE I 2 IS A STANDARD ALA.
REMARK 600 RESIDUE I 1 (PSA) IS A PHENYLSTATINE (I.E. IT HAS A PHE
REMARK 600 SIDE CHAIN BUT HAS A -CHOH-CH(2)-CO- INSTEAD OF MAIN
REMARK 600 CHAIN -CO- GROUP.
REMARK 600 RESIDUE I 2' IS A STANDARD LEU.
REMARK 600 RESIDUE I 3' IS A STANDARD ARG.
REMARK 600 RESIDUE I 4' IS A STANDARD GLU.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSA I 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 328
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 329
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF PS2, THR-PHE-GLN-ALA
REMARK 800 -PSA-LEU-ARG-GLU
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 63A, 80A, 134A, 184A, 203A, 204A, 238A, 282A,
REMARK 999 282B, AND 319A IN CHAIN E ARE INSERTIONS RELATIVE TO
REMARK 999 PORCINE PEPSIN.
DBREF 1EPM E -2 326 UNP P11838 CARP_CRYPA 90 419
DBREF 1EPM I 5 4A PDB 1EPM 1EPM 5 4
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 8 THR PHE GLN ALA PSA LEU ARG GLU
MODRES 1EPM PSA I 1 PHE
HET PSA I 1 14
HET SO4 E 327 5
HET SO4 E 328 5
HET SO4 E 329 5
HETNAM PSA 3-HYDROXY-4-AMINO-5-PHENYLPENTANOIC ACID
HETNAM SO4 SULFATE ION
FORMUL 2 PSA C11 H15 N O3
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 HOH *281(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 2.02
LINK N PSA I 1 C ALA I 2 1555 1555 1.35
LINK C PSA I 1 N LEU I 2A 1555 1555 1.33
CISPEP 1 THR E 22 PRO E 23 0 -3.38
CISPEP 2 SER E 132 PRO E 133 0 1.65
SITE 1 CAT 2 ASP E 32 ASP E 215
SITE 1 AC1 11 ASP E 30 ASP E 32 GLY E 34 TYR E 75
SITE 2 AC1 11 GLY E 76 ASP E 77 ASP E 215 GLY E 217
SITE 3 AC1 11 ALA I 2 LEU I 2A GLN I 3
SITE 1 AC2 4 LYS E 238A SER E 240 SER E 241 SER E 242
SITE 1 AC3 4 TYR E 175 SER E 178 ILE E 179 HOH E 589
SITE 1 AC4 8 SER E 108 SER E 109 THR E 318 THR E 319
SITE 2 AC4 8 HOH E 453 HOH E 500 HOH E 505 HOH E 538
SITE 1 AC5 10 ASP E 12 THR E 219 LEU E 220 PHE E 275
SITE 2 AC5 10 PHE E 284 GLN I 3 ARG I 3A HOH I 7
SITE 3 AC5 10 HOH I 10 HOH I 12
CRYST1 43.110 75.880 42.980 90.00 96.76 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 0.023196 0.000000 0.002750 0.00000
SCALE2 0.000000 0.013179 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023430 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
