HEADER HYDROLASE (SERINE PROTEINASE) 06-APR-90 6GCH
TITLE STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR
TITLE 2 COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING
TITLE 3 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA-CHYMOTRYPSIN A;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.21.1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: GAMMA-CHYMOTRYPSIN A;
COMPND 7 CHAIN: F;
COMPND 8 EC: 3.4.21.1;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: GAMMA-CHYMOTRYPSIN A;
COMPND 11 CHAIN: G;
COMPND 12 EC: 3.4.21.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: CATTLE;
SOURCE 8 ORGANISM_TAXID: 9913;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 11 ORGANISM_COMMON: CATTLE;
SOURCE 12 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE (SERINE PROTEINASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BRADY,A.WEI,D.RINGE,R.H.ABELES
REVDAT 2 24-FEB-09 6GCH 1 VERSN
REVDAT 1 15-OCT-90 6GCH 0
JRNL AUTH K.BRADY,A.Z.WEI,D.RINGE,R.H.ABELES
JRNL TITL STRUCTURE OF CHYMOTRYPSIN-TRIFLUOROMETHYL KETONE
JRNL TITL 2 INHIBITOR COMPLEXES: COMPARISON OF SLOWLY AND
JRNL TITL 3 RAPIDLY EQUILIBRATING INHIBITORS.
JRNL REF BIOCHEMISTRY V. 29 7600 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2271520
JRNL DOI 10.1021/BI00485A009
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.L.STODDARD,J.BRUHNKE,N.PORTER,D.RINGE,G.A.PETSKO
REMARK 1 TITL STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE
REMARK 1 TITL 2 CINNAMATES BOUND TO CHYMOTRYPSIN
REMARK 1 REF BIOCHEMISTRY V. 29 4871 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.L.STODDARD,J.BRUHNKE,P.KOENIG,N.PORTER,D.RINGE,
REMARK 1 AUTH 2 G.A.PETSKO
REMARK 1 TITL PHOTOLYSIS AND DEACYLATION OF INHIBITED
REMARK 1 TITL 2 CHYMOTRYPSIN
REMARK 1 REF BIOCHEMISTRY V. 29 8042 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.BRADY,R.H.ABELES
REMARK 1 TITL INHIBITION OF CHYMOTRYPSIN BY PEPTIDYL
REMARK 1 TITL 2 TRIFLUOROMETHY KETONES. DETERMINANTS OF
REMARK 1 TITL 3 SLOW-BINDING KINETICS
REMARK 1 REF BIOCHEMISTRY V. 29 7608 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH K.BRADY.T.-C.LIANG,R.H.ABELES
REMARK 1 TITL PH DEPENDENCE OF THE INHIBITION OF CHYMOTRYPSIN BY
REMARK 1 TITL 2 A PEPTIDYL TRIFLUOROMETHYL KETONE
REMARK 1 REF BIOCHEMISTRY V. 28 9066 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 9255
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) : 0.180
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 : 1738
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 188
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) : 0.012 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.029 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.032 ; 0.040
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 6GCH PHASES WERE CALCULATED FROM THE MODEL OF G.COHEN ET AL.
REMARK 3 6GCH (PROTEIN DATA BANK ENTRY 2GCH) AND APPLIED TO STRUCTURE
REMARK 3 6GCH FACTORS COLLATED FROM ALPHA-CHYMOTRYPSIN CRYSTALS WHICH
REMARK 3 HAD 6GCH BEEN SOAKED IN A SOLUTION CONTAINING THE INHIBITOR
REMARK 3 6GCH N-ACETYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE. ALL 6GCH
REMARK 3 SECONDARY STRUCTURAL FEATURES AND SEQUENCE ARE IDENTICAL TO
REMARK 3 6GCH PROTEIN DATA BANK ENTRY 2GCH. 6GCH
REMARK 4
REMARK 4 6GCH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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 (%): 46.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
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 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.85049
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.85049
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.60031
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.85049
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.85049
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 48.60031
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.85049
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.85049
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.60031
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.85049
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.85049
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 48.60031
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G
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 -1.000000 0.000000 0.000000 69.70098
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 139.40197
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 GLY E 12
REMARK 465 LEU E 13
REMARK 465 ALA G 149
REMARK 465 ASN G 150
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 SER E 11 CA C O CB OG
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 ND2 ASN F 18 O GLY G 187 1.85
REMARK 500 NE2 GLN F 116 O HOH F 321 2.16
REMARK 500 CB ALA F 56 O HOH F 430 2.17
REMARK 500 N CYS G 191 OD2 ASP G 194 2.18
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 F 424 O HOH G 307 2675 0.47
REMARK 500 CA SER F 127 O HOH F 451 6576 0.81
REMARK 500 C SER F 127 O HOH F 451 6576 0.85
REMARK 500 O HOH F 318 O HOH F 326 6476 1.01
REMARK 500 OG SER F 63 O HOH F 465 2675 1.30
REMARK 500 CB SER F 63 O HOH F 465 2675 1.31
REMARK 500 O HOH G 381 O HOH G 381 7557 1.44
REMARK 500 O HOH F 498 O HOH G 379 8777 1.47
REMARK 500 SD MET G 192 O HOH F 386 2675 1.47
REMARK 500 O HOH F 302 O HOH F 437 2675 1.50
REMARK 500 OD1 ASN G 204 O HOH F 440 6576 1.51
REMARK 500 O HOH F 337 O HOH G 520 8777 1.57
REMARK 500 OG SER F 96 O HOH F 369 2675 1.69
REMARK 500 O HOH F 318 O HOH F 390 6476 1.76
REMARK 500 O SER F 127 O HOH F 451 6576 1.77
REMARK 500 O HOH F 499 O HOH G 549 8777 1.78
REMARK 500 O THR F 37 O HOH E 489 6476 1.79
REMARK 500 N ASP F 128 O HOH F 451 6576 1.85
REMARK 500 N SER F 127 O HOH F 451 6576 1.88
REMARK 500 CB SER G 159 O HOH G 517 8777 1.90
REMARK 500 O HOH F 302 O HOH F 434 2675 1.97
REMARK 500 OG SER F 96 O HOH F 433 2675 2.03
REMARK 500 OD1 ASP F 35 O HOH F 308 2675 2.04
REMARK 500 O SER G 159 O HOH G 516 8777 2.07
REMARK 500 OH TYR G 171 O HOH F 499 8777 2.10
REMARK 500 CE MET G 192 O HOH F 386 2675 2.14
REMARK 500 CD2 LEU F 97 O HOH G 375 2675 2.14
REMARK 500 CB SER F 127 O HOH F 451 6576 2.14
REMARK 500 CA HIS F 57 O HOH F 432 2675 2.15
REMARK 500 O LEU F 97 O HOH F 443 2675 2.18
REMARK 500 CG ASN G 204 O HOH F 440 6576 2.18
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 ASN G 245 C ASN G 245 OXT 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 F 145 NE - CZ - NH1 ANGL. DEV. = 3.5 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 ASN F 18 20.10 91.18
REMARK 500 PHE F 71 -43.56 -141.06
REMARK 500 SER F 115 -168.13 -163.12
REMARK 500 CYS F 136 -168.27 -115.55
REMARK 500 THR G 174 22.52 -63.18
REMARK 500 SER G 214 -70.27 -111.40
REMARK 500 SER G 217 127.47 -38.01
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 F 145 0.12 SIDE_CHAIN
REMARK 500 ARG G 154 0.16 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, 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 LEU E 10 20.74
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 E 406 DISTANCE = 5.70 ANGSTROMS
REMARK 525 HOH F 311 DISTANCE = 5.65 ANGSTROMS
REMARK 525 HOH G 333 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH G 361 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH F 370 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH F 371 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH G 378 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH G 381 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH G 382 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH F 415 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH G 398 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH F 424 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH G 511 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH G 516 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH G 517 DISTANCE = 5.44 ANGSTROMS
REMARK 525 HOH F 443 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH G 525 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH G 535 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH F 451 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH F 460 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH F 469 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH F 484 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH F 485 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH F 499 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH F 515 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH F 538 DISTANCE = 5.23 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APF G 246
DBREF 6GCH E 1 13 UNP P00766 CTRA_BOVIN 1 13
DBREF 6GCH F 16 146 UNP P00766 CTRA_BOVIN 16 146
DBREF 6GCH G 149 245 UNP P00766 CTRA_BOVIN 149 245
SEQRES 1 E 13 CYS GLY VAL PRO ALA ILE GLN PRO VAL LEU SER GLY LEU
SEQRES 1 F 131 ILE VAL ASN GLY GLU GLU ALA VAL PRO GLY SER TRP PRO
SEQRES 2 F 131 TRP GLN VAL SER LEU GLN ASP LYS THR GLY PHE HIS PHE
SEQRES 3 F 131 CYS GLY GLY SER LEU ILE ASN GLU ASN TRP VAL VAL THR
SEQRES 4 F 131 ALA ALA HIS CYS GLY VAL THR THR SER ASP VAL VAL VAL
SEQRES 5 F 131 ALA GLY GLU PHE ASP GLN GLY SER SER SER GLU LYS ILE
SEQRES 6 F 131 GLN LYS LEU LYS ILE ALA LYS VAL PHE LYS ASN SER LYS
SEQRES 7 F 131 TYR ASN SER LEU THR ILE ASN ASN ASP ILE THR LEU LEU
SEQRES 8 F 131 LYS LEU SER THR ALA ALA SER PHE SER GLN THR VAL SER
SEQRES 9 F 131 ALA VAL CYS LEU PRO SER ALA SER ASP ASP PHE ALA ALA
SEQRES 10 F 131 GLY THR THR CYS VAL THR THR GLY TRP GLY LEU THR ARG
SEQRES 11 F 131 TYR
SEQRES 1 G 97 ALA ASN THR PRO ASP ARG LEU GLN GLN ALA SER LEU PRO
SEQRES 2 G 97 LEU LEU SER ASN THR ASN CYS LYS LYS TYR TRP GLY THR
SEQRES 3 G 97 LYS ILE LYS ASP ALA MET ILE CYS ALA GLY ALA SER GLY
SEQRES 4 G 97 VAL SER SER CYS MET GLY ASP SER GLY GLY PRO LEU VAL
SEQRES 5 G 97 CYS LYS LYS ASN GLY ALA TRP THR LEU VAL GLY ILE VAL
SEQRES 6 G 97 SER TRP GLY SER SER THR CYS SER THR SER THR PRO GLY
SEQRES 7 G 97 VAL TYR ALA ARG VAL THR ALA LEU VAL ASN TRP VAL GLN
SEQRES 8 G 97 GLN THR LEU ALA ALA ASN
HET APF G 246 18
HETNAM APF 1,1,1-TRIFLUORO-3-ACETAMIDO-4-PHENYL BUTAN-2-ONE(N-
HETNAM 2 APF ACETYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE)
FORMUL 4 APF C12 H12 F3 N O2
FORMUL 5 HOH *188(H2 O)
HELIX 1 H1 VAL G 231 ASN G 245 1 15
SHEET 1 S1 7 PRO F 28 ASP F 35 0
SHEET 2 S1 7 CYS F 42 GLU F 49 -1
SHEET 3 S1 7 ASN F 50 ALA F 56 -1
SHEET 4 S1 7 ASN F 101 THR F 110 -1
SHEET 5 S1 7 GLN F 81 SER F 92 -1
SHEET 6 S1 7 SER F 63 GLY F 69 -1
SHEET 7 S1 7 PRO F 28 ASP F 35 -1
SHEET 1 S2 7 GLY F 133 TRP F 141 0
SHEET 2 S2 7 LEU G 155 LEU G 162 -1
SHEET 3 S2 7 ALA G 179 SER G 186 -1
SHEET 4 S2 7 SER G 223 ALA G 229 -1
SHEET 5 S2 7 ILE G 212 SER G 218 -1
SHEET 6 S2 7 GLY G 193 CYS G 201 -1
SHEET 7 S2 7 GLY F 133 TRP F 141 -1
SSBOND 1 CYS E 1 CYS F 122 1555 1555 2.02
SSBOND 2 CYS F 42 CYS F 58 1555 1555 2.07
SSBOND 3 CYS F 136 CYS G 201 1555 1555 2.03
SSBOND 4 CYS G 168 CYS G 182 1555 1555 1.99
SSBOND 5 CYS G 191 CYS G 220 1555 1555 2.05
LINK OG SER G 195 C2 APF G 246 1555 1555 1.54
SITE 1 AC1 19 PHE F 41 CYS F 42 HIS F 57 SER F 96
SITE 2 AC1 19 HOH F 369 HOH F 433 SER G 190 CYS G 191
SITE 3 AC1 19 MET G 192 GLY G 193 ASP G 194 SER G 195
SITE 4 AC1 19 SER G 214 GLY G 216 SER G 217 CYS G 220
SITE 5 AC1 19 HOH G 354 HOH G 366 HOH G 542
CRYST1 69.300 69.300 97.200 90.00 90.00 90.00 P 42 21 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 0.014347 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010288 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
