HEADER HYDROLASE/HYDROLASE INHIBITOR 24-APR-97 2JXR
TITLE STRUCTURE OF YEAST PROTEINASE A
CAVEAT 2JXR THR A 16 HAS WRONG CHIRALITY AT ATOM CB ASN A 43 HAS WRONG
CAVEAT 2 2JXR CHIRALITY AT ATOM CA SER A 63 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 2JXR CA ASN A 161 HAS WRONG CHIRALITY AT ATOM CA TRP A 241 HAS
CAVEAT 4 2JXR WRONG CHIRALITY AT ATOM CA MAN B 5 HAS WRONG CHIRALITY AT
CAVEAT 5 2JXR ATOM C1 MAN B 5 HAS WRONG CHIRALITY AT ATOM C2 MAN B 5 HAS
CAVEAT 6 2JXR WRONG CHIRALITY AT ATOM C5 NAG A 337 HAS WRONG CHIRALITY AT
CAVEAT 7 2JXR ATOM C1 NAG A 337 HAS WRONG CHIRALITY AT ATOM C2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SACCHAROPEPSIN, YEAST ENDOPEPTIDASE A;
COMPND 5 EC: 3.4.23.25;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX, ASPARTYL PROTEASE,
KEYWDS 2 GLYCOPROTEIN, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.F.AGUILAR,M.BADASSO,T.DREYER,N.B.CRONIN,M.P.NEWMAN,J.B.COOPER,
AUTHOR 2 D.J.HOOVER,S.P.WOOD,M.S.JOHNSON,T.L.BLUNDELL
REVDAT 5 03-NOV-21 2JXR 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 2JXR 1 CAVEAT COMPND REMARK HET
REVDAT 4 2 1 HETNAM FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 13-JUL-11 2JXR 1 VERSN
REVDAT 2 24-FEB-09 2JXR 1 VERSN
REVDAT 1 29-OCT-97 2JXR 0
SPRSDE 29-OCT-97 2JXR 1JXR
JRNL AUTH C.F.AGUILAR,N.B.CRONIN,M.BADASSO,T.DREYER,M.P.NEWMAN,
JRNL AUTH 2 J.B.COOPER,D.J.HOOVER,S.P.WOOD,M.S.JOHNSON,T.L.BLUNDELL
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE AT 2.4 A RESOLUTION OF
JRNL TITL 2 GLYCOSYLATED PROTEINASE A FROM THE LYSOSOME-LIKE VACUOLE OF
JRNL TITL 3 SACCHAROMYCES CEREVISIAE.
JRNL REF J.MOL.BIOL. V. 267 899 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9135120
JRNL DOI 10.1006/JMBI.1996.0880
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
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 : 18013
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) : 0.193
REMARK 3 FREE R VALUE : 0.270
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 : 2528
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 121
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.01
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: LOOP RESIDUES A 140 - A 142 WERE
REMARK 3 MODELED STEREOCHEMICALLY.
REMARK 4
REMARK 4 2JXR 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_1000178279.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NOV-93
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AGROVATA, WEIS
REMARK 200 DATA SCALING SOFTWARE : AGROVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18325
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 (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07000
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 (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.60000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.80000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.80000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 73.60000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 25.0 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 73.60000
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 PHE A 260 CZ PHE A 260 CE2 0.120
REMARK 500 VAL A 301 CB VAL A 301 CG1 -0.128
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 HIS A 2 CA - CB - CG ANGL. DEV. = -10.2 DEGREES
REMARK 500 ASP A 3 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 VAL A 4 CA - CB - CG2 ANGL. DEV. = 22.9 DEGREES
REMARK 500 TYR A 14 CG - CD2 - CE2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR A 15 CG - CD1 - CE1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ASP A 17 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ILE A 30 CB - CG1 - CD1 ANGL. DEV. = 17.6 DEGREES
REMARK 500 SER A 35 C - N - CA ANGL. DEV. = 24.4 DEGREES
REMARK 500 LEU A 38 CB - CG - CD1 ANGL. DEV. = 14.8 DEGREES
REMARK 500 ASN A 43 N - CA - CB ANGL. DEV. = 12.7 DEGREES
REMARK 500 TYR A 56 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 57 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ALA A 60 O - C - N ANGL. DEV. = 12.6 DEGREES
REMARK 500 SER A 63 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 LEU A 80 CA - CB - CG ANGL. DEV. = 20.0 DEGREES
REMARK 500 ILE A 91 CA - C - N ANGL. DEV. = 13.4 DEGREES
REMARK 500 GLY A 92 C - N - CA ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASP A 93 CB - CG - OD1 ANGL. DEV. = -10.2 DEGREES
REMARK 500 LEU A 94 CB - CG - CD2 ANGL. DEV. = -14.1 DEGREES
REMARK 500 PRO A 108 C - N - CA ANGL. DEV. = -13.7 DEGREES
REMARK 500 PRO A 108 C - N - CD ANGL. DEV. = 16.3 DEGREES
REMARK 500 LEU A 121 CB - CG - CD2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 GLY A 122 C - N - CA ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASP A 126 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ILE A 128 CB - CG1 - CD1 ANGL. DEV. = -19.9 DEGREES
REMARK 500 ASP A 131 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LYS A 132 CD - CE - NZ ANGL. DEV. = 20.6 DEGREES
REMARK 500 VAL A 133 CA - CB - CG1 ANGL. DEV. = -10.9 DEGREES
REMARK 500 VAL A 134 CG1 - CB - CG2 ANGL. DEV. = -11.9 DEGREES
REMARK 500 LEU A 145 CB - CG - CD2 ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG A 150 CB - CG - CD ANGL. DEV. = -16.2 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 PHE A 153 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 TYR A 154 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 159B CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASN A 161 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASP A 171 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 PHE A 175 CG - CD1 - CE1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 PHE A 175 CD1 - CE1 - CZ ANGL. DEV. = -9.6 DEGREES
REMARK 500 LYS A 176 CA - CB - CG ANGL. DEV. = 23.9 DEGREES
REMARK 500 THR A 180 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 VAL A 184 CA - CB - CG1 ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 186 CA - CB - CG ANGL. DEV. = 22.8 DEGREES
REMARK 500 ARG A 186 CG - CD - NE ANGL. DEV. = 21.0 DEGREES
REMARK 500 LYS A 187 CD - CE - NZ ANGL. DEV. = -15.8 DEGREES
REMARK 500 LYS A 193 CA - CB - CG ANGL. DEV. = 20.4 DEGREES
REMARK 500 LYS A 193 CG - CD - CE ANGL. DEV. = 20.5 DEGREES
REMARK 500 TYR A 203 CB - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 215 CB - CG - OD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 215 CB - CG - OD2 ANGL. DEV. = -9.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 ASN A 67 -30.13 -155.39
REMARK 500 ASP A 87 176.76 174.40
REMARK 500 ASP A 159B -151.12 -114.46
REMARK 500 THR A 159C -85.97 -172.63
REMARK 500 ASN A 161 99.40 -48.82
REMARK 500 ALA A 188 -59.45 -148.40
REMARK 500 LEU A 220 -150.97 -112.37
REMARK 500 LYS A 239 99.06 -63.63
REMARK 500 TRP A 241 -85.17 -3.06
REMARK 500 ASN A 263 8.06 58.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N-(MORPHOLIN-4-YLCARBONYL)-L-PHENYLALANYL-N-[(1R)-1-
REMARK 630 (CYCLOHEXYLMETHYL)-3,3-DIFLUORO-2,2-DIHYDROXY-4-(METHYLAMINO)-4-
REMARK 630 OXOBUTYL]-L-NORLEUCINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 2Z3 A 327
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: MOR PHE NLE CHF NME
REMARK 630 DETAILS: NULL
DBREF 2JXR A 0 326 UNP P07267 CARP_YEAST 77 405
SEQADV 2JXR ILE A 315 UNP P07267 LEU 394 ENGINEERED MUTATION
SEQRES 1 A 329 GLY GLY HIS ASP VAL PRO LEU THR ASN TYR LEU ASN ALA
SEQRES 2 A 329 GLN TYR TYR THR ASP ILE THR LEU GLY THR PRO PRO GLN
SEQRES 3 A 329 ASN PHE LYS VAL ILE LEU ASP THR GLY SER SER ASN LEU
SEQRES 4 A 329 TRP VAL PRO SER ASN GLU CYS GLY SER LEU ALA CYS PHE
SEQRES 5 A 329 LEU HIS SER LYS TYR ASP HIS GLU ALA SER SER SER TYR
SEQRES 6 A 329 LYS ALA ASN GLY THR GLU PHE ALA ILE GLN TYR GLY THR
SEQRES 7 A 329 GLY SER LEU GLU GLY TYR ILE SER GLN ASP THR LEU SER
SEQRES 8 A 329 ILE GLY ASP LEU THR ILE PRO LYS GLN ASP PHE ALA GLU
SEQRES 9 A 329 ALA THR SER GLU PRO GLY LEU THR PHE ALA PHE GLY LYS
SEQRES 10 A 329 PHE ASP GLY ILE LEU GLY LEU GLY TYR ASP THR ILE SER
SEQRES 11 A 329 VAL ASP LYS VAL VAL PRO PRO PHE TYR ASN ALA ILE GLN
SEQRES 12 A 329 GLN ASP LEU LEU ASP GLU LYS ARG PHE ALA PHE TYR LEU
SEQRES 13 A 329 GLY ASP THR SER LYS ASP THR GLU ASN GLY GLY GLU ALA
SEQRES 14 A 329 THR PHE GLY GLY ILE ASP GLU SER LYS PHE LYS GLY ASP
SEQRES 15 A 329 ILE THR TRP LEU PRO VAL ARG ARG LYS ALA TYR TRP GLU
SEQRES 16 A 329 VAL LYS PHE GLU GLY ILE GLY LEU GLY ASP GLU TYR ALA
SEQRES 17 A 329 GLU LEU GLU SER HIS GLY ALA ALA ILE ASP THR GLY THR
SEQRES 18 A 329 SER LEU ILE THR LEU PRO SER GLY LEU ALA GLU MET ILE
SEQRES 19 A 329 ASN ALA GLU ILE GLY ALA LYS LYS GLY TRP THR GLY GLN
SEQRES 20 A 329 TYR THR LEU ASP CYS ASN THR ARG ASP ASN LEU PRO ASP
SEQRES 21 A 329 LEU ILE PHE ASN PHE ASN GLY TYR ASN PHE THR ILE GLY
SEQRES 22 A 329 PRO TYR ASP TYR THR LEU GLU VAL SER GLY SER CYS ILE
SEQRES 23 A 329 SER ALA ILE THR PRO MET ASP PHE PRO GLU PRO VAL GLY
SEQRES 24 A 329 PRO LEU ALA ILE VAL GLY ASP ALA PHE LEU ARG LYS TYR
SEQRES 25 A 329 TYR SER ILE TYR ASP ILE GLY ASN ASN ALA VAL GLY LEU
SEQRES 26 A 329 ALA LYS ALA ILE
MODRES 2JXR ASN A 67 ASN GLYCOSYLATION SITE
MODRES 2JXR ASN A 266 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET BMA B 4 11
HET MAN B 5 11
HET 2Z3 A 327 46
HET NAG A 337 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM 2Z3 N-(MORPHOLIN-4-YLCARBONYL)-L-PHENYLALANYL-N-[(1R)-1-
HETNAM 2 2Z3 (CYCLOHEXYLMETHYL)-3,3-DIFLUORO-2,2-DIHYDROXY-4-
HETNAM 3 2Z3 (METHYLAMINO)-4-OXOBUTYL]-L-NORLEUCINAMIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN 2Z3 CP-81,282
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 2 BMA 2(C6 H12 O6)
FORMUL 2 MAN C6 H12 O6
FORMUL 3 2Z3 C32 H49 F2 N5 O7
FORMUL 5 HOH *119(H2 O)
HELIX 1 A SER A 47 HIS A 53 1 7
HELIX 2 H2 ASP A 57 SER A 61 1 5
HELIX 3 H3 SER A 129 VAL A 133 1 5
HELIX 4 H4 PRO A 135 GLN A 143 1 9
HELIX 5 H5 PRO A 224 ILE A 235 1 12
HELIX 6 H6 ASP A 248 LEU A 255 1 8
HELIX 7 H7 GLY A 302 LYS A 308 1 7
SHEET 1 A 6 HIS A 2 PRO A 5 0
SHEET 2 A 6 GLY A 163 PHE A 167 -1 N PHE A 167 O HIS A 2
SHEET 3 A 6 ARG A 150 LEU A 155 -1 N TYR A 154 O GLU A 164
SHEET 4 A 6 TYR A 309 ASP A 314 -1 N TYR A 313 O PHE A 151
SHEET 5 A 6 ALA A 319 LYS A 324 -1 N ALA A 323 O TYR A 310
SHEET 6 A 6 THR A 180 PRO A 183 -1 N LEU A 182 O VAL A 320
SHEET 1 B 4 THR A 7 TYR A 9 0
SHEET 2 B 4 GLN A 13 THR A 19 -1 N TYR A 15 O THR A 7
SHEET 3 B 4 ASN A 26 ASP A 32 -1 N VAL A 29 O THR A 16
SHEET 4 B 4 GLY A 119 GLY A 122 1 N GLY A 119 O ILE A 30
SHEET 1 C 4 TRP A 39 PRO A 41 0
SHEET 2 C 4 PHE A 101 SER A 106 1 N ALA A 102 O VAL A 40
SHEET 3 C 4 SER A 79 SER A 85 -1 N SER A 85 O PHE A 101
SHEET 4 C 4 GLU A 70 GLN A 74 -1 N ILE A 73 O LEU A 80
SHEET 1 D 2 LEU A 89 ILE A 91 0
SHEET 2 D 2 LEU A 94 ILE A 96 -1 N ILE A 96 O LEU A 89
SHEET 1 E 3 GLU A 191 LYS A 193 0
SHEET 2 E 3 GLY A 210 ILE A 214 -1 N ALA A 212 O VAL A 192
SHEET 3 E 3 LEU A 298 VAL A 301 1 N ALA A 299 O GLY A 210
SHEET 1 F 4 GLU A 202 GLU A 205 0
SHEET 2 F 4 PHE A 194 LEU A 199 -1 N LEU A 199 O GLU A 202
SHEET 3 F 4 LEU A 258 PHE A 262 -1 N ASN A 261 O GLU A 195
SHEET 4 F 4 TYR A 265 ILE A 269 -1 N ILE A 269 O LEU A 258
SHEET 1 G 2 ILE A 221 LEU A 223 0
SHEET 2 G 2 ILE A 286 PRO A 288 1 N THR A 287 O ILE A 221
SHEET 1 H 2 THR A 275 VAL A 278 0
SHEET 2 H 2 SER A 281 SER A 284 -1 N ILE A 283 O LEU A 276
SSBOND 1 CYS A 45 CYS A 50 1555 1555 1.96
SSBOND 2 CYS A 249 CYS A 282 1555 1555 1.96
LINK ND2 ASN A 67 C1 NAG B 1 1555 1555 1.40
LINK ND2 ASN A 266 C1 NAG A 337 1555 1555 1.49
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.41
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45
LINK O3 BMA B 3 C1 BMA B 4 1555 1555 1.41
LINK O2 BMA B 4 C1 MAN B 5 1555 1555 1.46
CISPEP 1 THR A 22 PRO A 23 0 -1.06
CISPEP 2 GLU A 293 PRO A 294 0 7.77
CISPEP 3 GLY A 296 PRO A 297 0 -1.19
CRYST1 86.700 86.700 110.400 90.00 90.00 120.00 P 32 2 1 6
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 0.011534 0.006659 0.000000 0.00000
SCALE2 0.000000 0.013318 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009058 0.00000
(ATOM LINES ARE NOT SHOWN.)
END