HEADER HYDROLASE(SERINE PROTEINASE) 17-SEP-92 2PF1
TITLE STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTHROMBIN FRAGMENT 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE(SERINE PROTEINASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.SESHADRI,A.TULINSKY,E.SKRZYPCZAK-JANKUN,C.H.PARK
REVDAT 4 29-NOV-17 2PF1 1 HELIX
REVDAT 3 24-FEB-09 2PF1 1 VERSN
REVDAT 2 01-APR-03 2PF1 1 JRNL
REVDAT 1 31-JAN-94 2PF1 0
JRNL AUTH T.P.SESHADRI,A.TULINSKY,E.SKRZYPCZAK-JANKUN,C.H.PARK
JRNL TITL STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25 A
JRNL TITL 2 RESOLUTION.
JRNL REF J.MOL.BIOL. V. 220 481 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 1856869
JRNL DOI 10.1016/0022-2836(91)90025-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.TULINSKY,C.H.PARK,E.SKRZYPCZAK-JANKUN
REMARK 1 TITL STRUCTURE OF PROTHROMBIN FRAGMENT 1 REFINED AT 2.8 ANGSTROMS
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 202 885 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.H.PARK,A.TULINSKY
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE KRINGLE SEQUENCE:
REMARK 1 TITL 2 STRUCTURE OF PROTHROMBIN FRAGMENT 1
REMARK 1 REF BIOCHEMISTRY V. 25 3977 1986
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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) : 0.175
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 : 947
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 164
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) : 0.020 ; 0.014
REMARK 3 ANGLE DISTANCE (A) : 0.040 ; 0.053
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.050 ; 0.054
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.020 ; 0.011
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.150 ; 0.207
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.500 ; 0.280
REMARK 3 MULTIPLE TORSION (A) : 0.500 ; 0.380
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.500 ; 0.320
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 3.000 ; 1.900
REMARK 3 STAGGERED (DEGREES) : 15.000; 27.800
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.000 ; 0.590
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.500 ; 1.070
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.000 ; 0.790
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.500 ; 1.120
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PF1 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_1000178458.
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 (%): 65.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 42.60500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.81000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.81000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 63.90750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.81000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.81000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.30250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.81000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.81000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 63.90750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.81000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.81000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 21.30250
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 42.60500
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 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 ALA A 1
REMARK 465 ASN A 2
REMARK 465 LYS A 3
REMARK 465 GLY A 4
REMARK 465 PHE A 5
REMARK 465 LEU A 6
REMARK 465 CGU A 7
REMARK 465 CGU A 8
REMARK 465 VAL A 9
REMARK 465 ARG A 10
REMARK 465 LYS A 11
REMARK 465 GLY A 12
REMARK 465 ASN A 13
REMARK 465 LEU A 14
REMARK 465 CGU A 15
REMARK 465 ARG A 16
REMARK 465 CGU A 17
REMARK 465 CYS A 18
REMARK 465 LEU A 19
REMARK 465 CGU A 20
REMARK 465 CGU A 21
REMARK 465 PRO A 22
REMARK 465 CYS A 23
REMARK 465 SER A 24
REMARK 465 ARG A 25
REMARK 465 CGU A 26
REMARK 465 CGU A 27
REMARK 465 ALA A 28
REMARK 465 PHE A 29
REMARK 465 CGU A 30
REMARK 465 ALA A 31
REMARK 465 LEU A 32
REMARK 465 CGU A 33
REMARK 465 SER A 34
REMARK 465 LEU A 35
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 ARG A 111 O GLU A 112 1.57
REMARK 500 OD1 ASN A 101 CB THR A 103 2.04
REMARK 500 O VAL A 143 OD2 ASP A 147 2.09
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 OE1 GLU A 138 NH2 ARG A 156 3554 2.01
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 GLY A 71 N GLY A 71 CA 0.090
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 A 50 CA - C - N ANGL. DEV. = 13.9 DEGREES
REMARK 500 SER A 50 O - C - N ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 52 CD - NE - CZ ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 55 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 GLU A 56 OE1 - CD - OE2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 LEU A 58 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ALA A 67 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 MET A 72 CB - CA - C ANGL. DEV. = 18.8 DEGREES
REMARK 500 TYR A 74 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 75 CD - NE - CZ ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG A 75 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 VAL A 78 CB - CA - C ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG A 82 NH1 - CZ - NH2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 82 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 GLU A 86 OE1 - CD - OE2 ANGL. DEV. = -12.8 DEGREES
REMARK 500 GLU A 86 CG - CD - OE2 ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG A 91 N - CA - CB ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG A 91 CD - NE - CZ ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR A 94 CB - CG - CD2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 GLU A 99 N - CA - CB ANGL. DEV. = 12.2 DEGREES
REMARK 500 GLU A 99 OE1 - CD - OE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 GLU A 99 CG - CD - OE1 ANGL. DEV. = -15.1 DEGREES
REMARK 500 THR A 103 N - CA - CB ANGL. DEV. = -15.1 DEGREES
REMARK 500 GLY A 107 CA - C - O ANGL. DEV. = 11.3 DEGREES
REMARK 500 ALA A 108 C - N - CA ANGL. DEV. = 17.1 DEGREES
REMARK 500 ALA A 108 N - CA - CB ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP A 109 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 111 CD - NE - CZ ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASN A 117 C - N - CA ANGL. DEV. = 15.9 DEGREES
REMARK 500 ILE A 122 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 TYR A 128 CB - CG - CD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 THR A 129 CA - CB - OG1 ANGL. DEV. = -17.9 DEGREES
REMARK 500 ARG A 135 CD - NE - CZ ANGL. DEV. = -11.5 DEGREES
REMARK 500 ARG A 135 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 136 CD - NE - CZ ANGL. DEV. = 17.9 DEGREES
REMARK 500 GLU A 137 N - CA - CB ANGL. DEV. = 14.6 DEGREES
REMARK 500 GLU A 137 CA - CB - CG ANGL. DEV. = 18.8 DEGREES
REMARK 500 GLU A 137 OE1 - CD - OE2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 GLU A 137 CG - CD - OE2 ANGL. DEV. = 17.6 DEGREES
REMARK 500 VAL A 141 CB - CA - C ANGL. DEV. = 14.2 DEGREES
REMARK 500 VAL A 143 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ASP A 147 CB - CG - OD1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ASP A 147 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 55 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 ALA A 37 -80.44 151.40
REMARK 500 SER A 50 -93.42 -68.77
REMARK 500 ALA A 51 67.74 -48.29
REMARK 500 ASN A 53 -79.59 -64.02
REMARK 500 ASN A 65 -29.08 -162.25
REMARK 500 VAL A 70 143.06 -32.34
REMARK 500 TYR A 74 110.96 177.20
REMARK 500 ASN A 77 64.50 -177.03
REMARK 500 SER A 92 104.73 -51.50
REMARK 500 ARG A 93 65.02 -111.18
REMARK 500 SER A 102 2.39 -42.66
REMARK 500 THR A 104 -15.96 177.70
REMARK 500 ALA A 108 145.09 -35.57
REMARK 500 ASP A 109 78.20 -101.50
REMARK 500 GLU A 112 135.94 14.39
REMARK 500 ASN A 113 25.55 2.99
REMARK 500 ASN A 117 64.46 -164.23
REMARK 500 ASP A 119 -86.63 -88.42
REMARK 500 ARG A 148 -157.26 -159.67
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2PF1 A 1 156 UNP P00735 THRB_BOVIN 44 199
SEQADV 2PF1 CGU A 7 UNP P00735 GLU 50 CONFLICT
SEQADV 2PF1 CGU A 8 UNP P00735 GLU 51 CONFLICT
SEQADV 2PF1 CGU A 15 UNP P00735 GLU 58 CONFLICT
SEQADV 2PF1 CGU A 17 UNP P00735 GLU 60 CONFLICT
SEQADV 2PF1 CGU A 20 UNP P00735 GLU 63 CONFLICT
SEQADV 2PF1 CGU A 21 UNP P00735 GLU 64 CONFLICT
SEQADV 2PF1 CGU A 26 UNP P00735 GLU 69 CONFLICT
SEQADV 2PF1 CGU A 27 UNP P00735 GLU 70 CONFLICT
SEQADV 2PF1 CGU A 30 UNP P00735 GLU 73 CONFLICT
SEQADV 2PF1 CGU A 33 UNP P00735 GLU 76 CONFLICT
SEQRES 1 A 156 ALA ASN LYS GLY PHE LEU CGU CGU VAL ARG LYS GLY ASN
SEQRES 2 A 156 LEU CGU ARG CGU CYS LEU CGU CGU PRO CYS SER ARG CGU
SEQRES 3 A 156 CGU ALA PHE CGU ALA LEU CGU SER LEU SER ALA THR ASP
SEQRES 4 A 156 ALA PHE TRP ALA LYS TYR THR ALA CYS GLU SER ALA ARG
SEQRES 5 A 156 ASN PRO ARG GLU LYS LEU ASN GLU CYS LEU GLU GLY ASN
SEQRES 6 A 156 CYS ALA GLU GLY VAL GLY MET ASN TYR ARG GLY ASN VAL
SEQRES 7 A 156 SER VAL THR ARG SER GLY ILE GLU CYS GLN LEU TRP ARG
SEQRES 8 A 156 SER ARG TYR PRO HIS LYS PRO GLU ILE ASN SER THR THR
SEQRES 9 A 156 HIS PRO GLY ALA ASP LEU ARG GLU ASN PHE CYS ARG ASN
SEQRES 10 A 156 PRO ASP GLY SER ILE THR GLY PRO TRP CYS TYR THR THR
SEQRES 11 A 156 SER PRO THR LEU ARG ARG GLU GLU CYS SER VAL PRO VAL
SEQRES 12 A 156 CYS GLY GLN ASP ARG VAL THR VAL GLU VAL ILE PRO ARG
FORMUL 2 HOH *164(H2 O)
HELIX 1 A1 ASP A 39 ALA A 47 1 9
HELIX 2 A2 ARG A 55 LEU A 62 1 8
SHEET 1 B1 2 SER A 79 THR A 81 0
SHEET 2 B1 2 ILE A 85 CYS A 87 -1
SHEET 1 B2 2 GLN A 88 TRP A 90 0
SHEET 2 B2 2 ARG A 111 ASN A 113 -1
SHEET 1 B3 2 CYS A 127 THR A 129 0
SHEET 2 B3 2 ARG A 136 GLU A 138 -1
SHEET 1 B4 2 VAL A 141 PRO A 142 0
SHEET 2 B4 2 VAL A 149 THR A 150 -1
SSBOND 1 CYS A 48 CYS A 61 1555 1555 2.05
SSBOND 2 CYS A 66 CYS A 144 1555 1555 2.07
SSBOND 3 CYS A 87 CYS A 127 1555 1555 1.96
SSBOND 4 CYS A 115 CYS A 139 1555 1555 1.96
CISPEP 1 TYR A 94 PRO A 95 0 0.19
CRYST1 77.620 77.620 85.210 90.00 90.00 90.00 P 43 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 0.012883 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012883 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
