HEADER HYDROLASE 26-FEB-90 3CMS
TITLE ENGINEERING ENZYME SUB-SITE SPECIFICITY: PREPARATION, KINETIC
TITLE 2 CHARACTERIZATION AND X-RAY ANALYSIS AT 2.0-ANGSTROMS RESOLUTION OF
TITLE 3 VAL111PHE SITE-MUTATED CALF CHYMOSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHYMOSIN B;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.23.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE, ACID PROTEINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NEWMAN,C.FRAZAO,A.SHEARER,I.J.TICKLE,T.L.BLUNDELL
REVDAT 5 29-NOV-17 3CMS 1 HELIX
REVDAT 4 29-FEB-12 3CMS 1 VERSN
REVDAT 3 24-FEB-09 3CMS 1 VERSN
REVDAT 2 01-APR-03 3CMS 1 JRNL
REVDAT 1 15-OCT-92 3CMS 0
JRNL AUTH P.STROP,J.SEDLACEK,J.STYS,Z.KADERABKOVA,I.BLAHA,
JRNL AUTH 2 L.PAVLICKOVA,J.POHL,M.FABRY,V.KOSTKA,M.NEWMAN
JRNL TITL ENGINEERING ENZYME SUBSITE SPECIFICITY: PREPARATION, KINETIC
JRNL TITL 2 CHARACTERIZATION, AND X-RAY ANALYSIS AT 2.0-A RESOLUTION OF
JRNL TITL 3 VAL111PHE SITE-MUTATED CALF CHYMOSIN.
JRNL REF BIOCHEMISTRY V. 29 9863 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2271625
JRNL DOI 10.1021/BI00494A016
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.NEWMAN,M.SAFRO,C.FRAZAO,G.KAHN,A.ZDANOV,I.J.TICKLE,
REMARK 1 AUTH 2 T.L.BLUNDELL,N.ANDREEVA
REMARK 1 TITL X-RAY ANALYSES OF ASPARTIC PROTEINASES IV: STRUCTURE AND
REMARK 1 TITL 2 REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN
REMARK 1 REF J.MOL.BIOL. V. 221 1295 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
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 : 21710
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) : 0.195
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 : 2490
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 145
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) : 0.022 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.050 ; 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 PRESENTED IN THE TEMPERATURE FACTOR FIELD IS
REMARK 3 U.
REMARK 3
REMARK 3 RESIDUES 72 TO 79 HAVE BEEN REFINED IN TWO ALTERNATE
REMARK 3 CONFORMATIONS. TURN 5 WITH THE A CONFORMATION IS
REMARK 3 CLASSIFED TYPE II' 2:2 DISTORTED. TURN 5 WITH THE B
REMARK 3 CONFORMATION IS UNCLASSIFIED 2:2.
REMARK 3
REMARK 3 INVARIANT RESIDUE TYR 14 HAS BEEN BUILT INTO A CONFORMATION
REMARK 3 THAT DIFFERS FROM THE WILD-TYPE CHYMOSIN STRUCTURE.
REMARK 3 HOWEVER, THIS RESIDUE BELONGS TO THE POORLY DEFINED SURFACE
REMARK 3 REGION BETWEEN STRANDS AN AND BN, AND THUS THE ASSIGNMENT
REMARK 3 OF ITS POSITION MUST BE REGARDED AS TENTATIVE.
REMARK 4
REMARK 4 3CMS 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_1000178915.
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 (%): 47.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 40.10500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.28000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.21500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.10500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.28000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.21500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.10500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.28000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.21500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.10500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.28000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 36.21500
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 THE SPECIFIC GENE MUTATION V111F IS SITUATED BETWEEN THE
REMARK 400 PRIMARY SPECIFICITY BINDING POCKET S1 AND THE SECONDARY
REMARK 400 SPECIFICITY POCKET S3, EFFECTING THE BINDING OF LARGE
REMARK 400 HYDROPHOBIC RESIDUES IN BOTH THESE POCKETS. THIS MUTATION
REMARK 400 IS RESPONSIBLE FOR THE REARRANGEMENT OF RESIDUES 72 TO 79
REMARK 400 KNOWN AS THE ACTIVE SITE FLAP, A FLEXIBLE BETA-HAIRPIN TURN
REMARK 400 ABOVE THE ACTIVE SITE.
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 ASN A 294
REMARK 465 HIS A 295
REMARK 465 SER A 296
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 LEU A 6 C THR A 7 N -0.188
REMARK 500 ASP A 11 C SER A 12 N 0.174
REMARK 500 SER A 12 N SER A 12 CA 0.137
REMARK 500 PHE A 15 C GLY A 16 N 0.175
REMARK 500 ASN A 66 C LEU A 67 N -0.203
REMARK 500 VAL A 202 C VAL A 203 N -0.213
REMARK 500 GLY A 243 C GLU A 244 N -0.142
REMARK 500 VAL A 258 C VAL A 259 N 0.237
REMARK 500 ALA A 273 C TYR A 274 N 0.228
REMARK 500 PHE A 305 C ILE A 306 N 0.243
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 A 9 O - C - N ANGL. DEV. = 11.5 DEGREES
REMARK 500 ASP A 11 O - C - N ANGL. DEV. = -12.3 DEGREES
REMARK 500 TYR A 19 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLU A 26 CB - CG - CD ANGL. DEV. = -16.7 DEGREES
REMARK 500 GLU A 26 OE1 - CD - OE2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLU A 26 O - C - N ANGL. DEV. = 11.5 DEGREES
REMARK 500 ASP A 32 CB - CG - OD2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP A 37 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 VAL A 40 CA - CB - CG2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG A 55 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 96 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 LEU A 103 CB - CG - CD2 ANGL. DEV. = 14.3 DEGREES
REMARK 500 GLY A 122 C - N - CA ANGL. DEV. = 19.6 DEGREES
REMARK 500 MET A 123 CG - SD - CE ANGL. DEV. = 18.2 DEGREES
REMARK 500 MET A 140 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 MET A 141 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 143 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 149 CB - CG - OD1 ANGL. DEV. = 10.9 DEGREES
REMARK 500 MET A 155 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 MET A 164 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 TYR A 189 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 TYR A 189 CG - CD1 - CE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 SER A 200 CB - CA - C ANGL. DEV. = -12.0 DEGREES
REMARK 500 CYS A 206 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 GLU A 207 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 GLY A 208 C - N - CA ANGL. DEV. = -12.8 DEGREES
REMARK 500 GLN A 232 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 MET A 255 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 VAL A 259 C - N - CA ANGL. DEV. = -15.3 DEGREES
REMARK 500 MET A 266 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 VAL A 304 CA - CB - CG2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 ILE A 306 C - N - CA ANGL. DEV. = -15.3 DEGREES
REMARK 500 ARG A 307 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 TYR A 310 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 ASP A 314 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 315 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 315 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 VAL A 320 O - C - N ANGL. DEV. = -11.1 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 LEU A 10 60.63 30.32
REMARK 500 ASP A 11 -1.95 68.75
REMARK 500 ILE A 43 -19.68 -45.72
REMARK 500 THR A 77 -66.67 -29.65
REMARK 500 SER A 92 -125.39 57.84
REMARK 500 GLN A 98 57.77 37.02
REMARK 500 TYR A 132 -0.01 76.63
REMARK 500 GLN A 161 -15.08 -153.98
REMARK 500 GLN A 188 -72.24 -150.13
REMARK 500 GLN A 279 -152.25 44.59
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 MET A 80 10.42
REMARK 500 LEU A 128 11.29
REMARK 500 GLU A 261 14.64
REMARK 500 ASP A 278 12.21
REMARK 500 TYR A 310 16.02
REMARK 500 ALA A 323 11.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: active site
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: active site
DBREF 3CMS A -2 326 UNP P00794 CHYM_BOVIN 59 381
SEQADV 3CMS PHE A 111 UNP P00794 VAL 171 CONFLICT
SEQRES 1 A 323 GLY GLU VAL ALA SER VAL PRO LEU THR ASN TYR LEU ASP
SEQRES 2 A 323 SER GLN TYR PHE GLY LYS ILE TYR LEU GLY THR PRO PRO
SEQRES 3 A 323 GLN GLU PHE THR VAL LEU PHE ASP THR GLY SER SER ASP
SEQRES 4 A 323 PHE TRP VAL PRO SER ILE TYR CYS LYS SER ASN ALA CYS
SEQRES 5 A 323 LYS ASN HIS GLN ARG PHE ASP PRO ARG LYS SER SER THR
SEQRES 6 A 323 PHE GLN ASN LEU GLY LYS PRO LEU SER ILE HIS TYR GLY
SEQRES 7 A 323 THR GLY SER MET GLN GLY ILE LEU GLY TYR ASP THR VAL
SEQRES 8 A 323 THR VAL SER ASN ILE VAL ASP ILE GLN GLN THR VAL GLY
SEQRES 9 A 323 LEU SER THR GLN GLU PRO GLY ASP PHE PHE THR TYR ALA
SEQRES 10 A 323 GLU PHE ASP GLY ILE LEU GLY MET ALA TYR PRO SER LEU
SEQRES 11 A 323 ALA SER GLU TYR SER ILE PRO VAL PHE ASP ASN MET MET
SEQRES 12 A 323 ASN ARG HIS LEU VAL ALA GLN ASP LEU PHE SER VAL TYR
SEQRES 13 A 323 MET ASP ARG ASN GLY GLN GLU SER MET LEU THR LEU GLY
SEQRES 14 A 323 ALA ILE ASP PRO SER TYR TYR THR GLY SER LEU HIS TRP
SEQRES 15 A 323 VAL PRO VAL THR VAL GLN GLN TYR TRP GLN PHE THR VAL
SEQRES 16 A 323 ASP SER VAL THR ILE SER GLY VAL VAL VAL ALA CYS GLU
SEQRES 17 A 323 GLY GLY CYS GLN ALA ILE LEU ASP THR GLY THR SER LYS
SEQRES 18 A 323 LEU VAL GLY PRO SER SER ASP ILE LEU ASN ILE GLN GLN
SEQRES 19 A 323 ALA ILE GLY ALA THR GLN ASN GLN TYR GLY GLU PHE ASP
SEQRES 20 A 323 ILE ASP CYS ASP ASN LEU SER TYR MET PRO THR VAL VAL
SEQRES 21 A 323 PHE GLU ILE ASN GLY LYS MET TYR PRO LEU THR PRO SER
SEQRES 22 A 323 ALA TYR THR SER GLN ASP GLN GLY PHE CYS THR SER GLY
SEQRES 23 A 323 PHE GLN SER GLU ASN HIS SER GLN LYS TRP ILE LEU GLY
SEQRES 24 A 323 ASP VAL PHE ILE ARG GLU TYR TYR SER VAL PHE ASP ARG
SEQRES 25 A 323 ALA ASN ASN LEU VAL GLY LEU ALA LYS ALA ILE
FORMUL 2 HOH *145(H2 O)
HELIX 1 HN ASN A 48 LYS A 51 1 4
HELIX 2 HN1 PRO A 58 LYS A 60 5 3
HELIX 3 HN2 ASP A 110 TYR A 114 1DISTORTED 5
HELIX 4 HN3 PRO A 126 LEU A 128 5 3
HELIX 5 HNP VAL A 136 ASN A 142 1 7
HELIX 6 HC1 PRO A 172 TYR A 174 5 3
HELIX 7 HC SER A 225 ILE A 235 1 11
HELIX 8 HC2 LEU A 252 TYR A 254 5 3
HELIX 9 HC3 PRO A 271 TYR A 274 1 4
HELIX 10 HCP ASP A 303 ILE A 306 1 4
SHEET 1 1N 8 THR A 7 TYR A 9 0
SHEET 2 1N 8 GLN A 13 GLY A 16 -1 N THR A 7 O PHE A 15
SHEET 3 1N 8 THR A 28 ASP A 32 -1 N VAL A 29 O GLY A 16
SHEET 4 1N 8 GLY A 119 GLY A 122 1 N GLY A 119 O THR A 28
SHEET 5 1N 8 PHE A 38 PRO A 41 -1 N TRP A 39 O ILE A 120
SHEET 6 1N 8 GLN A 99 SER A 104 1 N GLY A 102 O PHE A 38
SHEET 7 1N 8 ILE A 83 ASP A 87 -1 N ILE A 83 O LEU A 103
SHEET 8 1N 8 GLN A 65 ASN A 66 -1 N GLN A 65 O TYR A 86
SHEET 1 1NP 3 THR A 105 GLN A 106 0
SHEET 2 1NP 3 GLY A 78 GLY A 82 -1 N GLN A 81 O GLN A 106
SHEET 3 1NP 3 PRO A 70 TYR A 75 -1 N TYR A 75 O GLY A 78
SHEET 1 1C 5 TRP A 190 VAL A 194 0
SHEET 2 1C 5 CYS A 210 LEU A 214 -1 N CYS A 210 O VAL A 194
SHEET 3 1C 5 TRP A 299 LEU A 301 1 N TRP A 299 O GLN A 211
SHEET 4 1C 5 LEU A 221 PRO A 224 -1 O VAL A 222 N ILE A 300
SHEET 5 1C 5 PHE A 286 GLU A 289 1 N GLN A 287 O LEU A 221
SHEET 1 1CP 4 THR A 275 ASP A 278 0
SHEET 2 1CP 4 PHE A 281 SER A 284 -1 N PHE A 281 O ASP A 278
SHEET 3 1CP 4 PHE A 245 ILE A 247 -1 N ILE A 247 O CYS A 282
SHEET 4 1CP 4 THR A 238 GLN A 239 -1 N THR A 238 O ASP A 246
SHEET 1 2N 4 GLN A 25 PHE A 27 0
SHEET 2 2N 4 LYS A 17 LEU A 20 -1 N ILE A 18 O PHE A 27
SHEET 3 2N 4 THR A 88 VAL A 91 -1 N THR A 90 O TYR A 19
SHEET 4 2N 4 ILE A 94 GLN A 98 -1 N ILE A 94 O VAL A 91
SHEET 1 2C 4 VAL A 202 ALA A 205 0
SHEET 2 2C 4 ASP A 195 ILE A 199 -1 N VAL A 197 O ALA A 205
SHEET 3 2C 4 VAL A 258 ILE A 262 -1 N VAL A 259 O THR A 198
SHEET 4 2C 4 LYS A 265 LEU A 269 -1 N LYS A 265 O ILE A 262
SHEET 1 3 6 ALA A 2 PRO A 5 0
SHEET 2 3 6 MET A 164 LEU A 167 -1 N LEU A 165 O VAL A 4
SHEET 3 3 6 LEU A 150 TYR A 154 -1 N SER A 152 O THR A 166
SHEET 4 3 6 TYR A 309 ASP A 314 -1 N SER A 311 O VAL A 153
SHEET 5 3 6 LEU A 319 ALA A 325 -1 N LEU A 319 O ASP A 314
SHEET 6 3 6 TYR A 175 PRO A 183 -1 N THR A 176 O LYS A 324
SSBOND 1 CYS A 45 CYS A 50 1555 1555 2.10
SSBOND 2 CYS A 206 CYS A 210 1555 1555 2.13
SSBOND 3 CYS A 249 CYS A 282 1555 1555 2.07
CISPEP 1 THR A 22 PRO A 23 0 -3.84
SITE 1 AC1 1 ASP A 32
SITE 1 AC2 1 ASP A 215
CRYST1 80.210 114.560 72.430 90.00 90.00 90.00 I 2 2 2 8
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 0.012467 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008729 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END