Header list of 1apo.pdb file
Complete list - 29 20 Bytes
HEADER COAGULATION FACTOR 21-APR-92 1APO
TITLE THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE N-TERMINAL EGF-LIKE
TITLE 2 MODULE OF BLOOD COAGULATION FACTOR X AS DETERMINED BY NMR
TITLE 3 SPECTROSCOPY AND SIMULATED FOLDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X;
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 COAGULATION FACTOR
EXPDTA SOLUTION NMR
NUMMDL 13
AUTHOR M.ULLNER,M.SELANDER,E.PERSSON,J.STENFLO,T.DRAKENBERG,O.TELEMAN
REVDAT 3 29-NOV-17 1APO 1 REMARK HELIX
REVDAT 2 24-FEB-09 1APO 1 VERSN
REVDAT 1 31-JAN-94 1APO 0
JRNL AUTH M.ULLNER,M.SELANDER,E.PERSSON,J.STENFLO,T.DRAKENBERG,
JRNL AUTH 2 O.TELEMAN
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE
JRNL TITL 2 N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X AS
JRNL TITL 3 DETERMINED BY NMR SPECTROSCOPY AND SIMULATED FOLDING.
JRNL REF BIOCHEMISTRY V. 31 5974 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1627540
JRNL DOI 10.1021/BI00141A004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.SELANDER,E.PERSSON,J.STENFLO,T.DRAKENBERG
REMARK 1 TITL 1H NMR ASSIGNMENT AND SECONDARY STRUCTURE OF THE CA2+-FREE
REMARK 1 TITL 2 FORM OF THE AMINO-TERMINAL EPIDERMAL GROWTH FACTOR LIKE
REMARK 1 TITL 3 DOMAIN IN COAGULATION FACTOR X
REMARK 1 REF BIOCHEMISTRY V. 29 8111 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.PERSSON,M.SELANDER,S.LINSE,T.DRAKENBERG,A.-K.OHLIN
REMARK 1 TITL CALCIUM BINDING TO THE ISOLATED BETA-HYDROXYASPARTIC
REMARK 1 TITL 2 ACID-CONTAINING EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF
REMARK 1 TITL 3 BOVINE FACTOR X
REMARK 1 REF J.BIOL.CHEM. V. 264 16897 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1APO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171103.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HG3 GLU A 77 HE1 PHE A 83 0.92
REMARK 500 CG GLU A 77 HE1 PHE A 83 1.19
REMARK 500 HG3 GLU A 77 CE1 PHE A 83 1.20
REMARK 500 CB GLU A 77 HE1 PHE A 83 1.52
REMARK 500 CG GLU A 77 CE1 PHE A 83 2.09
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 1 PHE A 83 CB PHE A 83 CG -0.113
REMARK 500 1 PHE A 83 CG PHE A 83 CD1 -0.168
REMARK 500 2 HIS A 53 CG HIS A 53 ND1 -0.094
REMARK 500 2 HIS A 60 CG HIS A 60 ND1 -0.094
REMARK 500 3 HIS A 53 CG HIS A 53 ND1 -0.123
REMARK 500 3 HIS A 60 CG HIS A 60 ND1 -0.099
REMARK 500 4 HIS A 53 CG HIS A 53 ND1 -0.096
REMARK 500 4 HIS A 60 CG HIS A 60 ND1 -0.114
REMARK 500 5 HIS A 60 CG HIS A 60 ND1 -0.097
REMARK 500 5 PHE A 83 CG PHE A 83 CD1 -0.171
REMARK 500 6 HIS A 53 CG HIS A 53 ND1 -0.103
REMARK 500 6 HIS A 60 CG HIS A 60 ND1 -0.096
REMARK 500 7 HIS A 53 CG HIS A 53 ND1 -0.103
REMARK 500 7 HIS A 60 CG HIS A 60 ND1 -0.100
REMARK 500 7 GLU A 82 CD GLU A 82 OE2 -0.070
REMARK 500 8 HIS A 53 CG HIS A 53 ND1 -0.098
REMARK 500 8 HIS A 60 CG HIS A 60 ND1 -0.105
REMARK 500 9 HIS A 53 CG HIS A 53 ND1 -0.107
REMARK 500 10 HIS A 53 CG HIS A 53 ND1 -0.099
REMARK 500 10 PHE A 83 CB PHE A 83 CG -0.133
REMARK 500 10 PHE A 83 CG PHE A 83 CD1 -0.227
REMARK 500 11 GLY A 47 N GLY A 47 CA -0.100
REMARK 500 11 HIS A 53 CG HIS A 53 ND1 -0.105
REMARK 500 11 HIS A 60 CG HIS A 60 ND1 -0.112
REMARK 500 11 PHE A 83 CB PHE A 83 CG -0.125
REMARK 500 11 PHE A 83 CG PHE A 83 CD1 -0.191
REMARK 500 12 HIS A 53 CG HIS A 53 ND1 -0.093
REMARK 500 12 HIS A 60 CG HIS A 60 ND1 -0.091
REMARK 500 12 PHE A 83 CG PHE A 83 CD1 -0.189
REMARK 500 13 HIS A 53 CG HIS A 53 ND1 -0.093
REMARK 500 13 ARG A 86 NE ARG A 86 CZ -0.107
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 1 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 1 HIS A 60 ND1 - CG - CD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 PHE A 83 CB - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 1 PHE A 83 CB - CG - CD1 ANGL. DEV. = -14.0 DEGREES
REMARK 500 2 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 HIS A 60 ND1 - CG - CD2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 HIS A 60 CB - CG - ND1 ANGL. DEV. = -9.0 DEGREES
REMARK 500 3 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 5 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 5 HIS A 53 CB - CG - ND1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 5 HIS A 60 CB - CG - ND1 ANGL. DEV. = -7.9 DEGREES
REMARK 500 5 PHE A 83 CB - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 5 PHE A 83 CB - CG - CD1 ANGL. DEV. = -14.2 DEGREES
REMARK 500 6 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 6 HIS A 53 CB - CG - ND1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 6 HIS A 60 ND1 - CG - CD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 7 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 7 HIS A 60 ND1 - CG - CD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 8 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 8 ARG A 86 CD - NE - CZ ANGL. DEV. = -8.7 DEGREES
REMARK 500 8 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 9 HIS A 53 CB - CG - ND1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 9 HIS A 60 ND1 - CG - CD2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 10 HIS A 53 ND1 - CG - CD2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 10 HIS A 60 ND1 - CG - CD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 10 PHE A 83 CB - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 10 PHE A 83 CB - CG - CD1 ANGL. DEV. = -16.1 DEGREES
REMARK 500 10 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 11 HIS A 60 ND1 - CG - CD2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 11 PHE A 83 CB - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 11 PHE A 83 CB - CG - CD1 ANGL. DEV. = -14.0 DEGREES
REMARK 500 12 PHE A 83 CB - CG - CD1 ANGL. DEV. = -13.7 DEGREES
REMARK 500 13 ASP A 46 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 13 ARG A 86 NH1 - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 13 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 13 ARG A 86 NE - CZ - NH2 ANGL. DEV. = 3.3 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 1 GLN A 49 7.05 46.53
REMARK 500 1 HIS A 53 91.99 9.25
REMARK 500 1 GLN A 58 26.86 46.83
REMARK 500 1 LYS A 62 -141.60 -90.00
REMARK 500 1 ILE A 65 30.08 -88.76
REMARK 500 1 ASP A 67 137.21 73.81
REMARK 500 1 TYR A 68 -165.16 -78.25
REMARK 500 1 GLU A 77 -146.31 -155.03
REMARK 500 2 ASP A 48 52.56 -97.15
REMARK 500 2 CYS A 50 19.88 -143.22
REMARK 500 2 HIS A 53 90.33 51.29
REMARK 500 2 GLN A 58 29.20 49.73
REMARK 500 2 TYR A 68 -166.19 -77.40
REMARK 500 2 CYS A 81 18.67 86.48
REMARK 500 2 THR A 85 19.95 43.87
REMARK 500 3 ASP A 48 58.73 -110.64
REMARK 500 3 HIS A 53 92.63 10.61
REMARK 500 3 CYS A 81 17.44 82.51
REMARK 500 4 HIS A 53 96.67 -173.12
REMARK 500 4 LYS A 62 -144.35 -123.30
REMARK 500 4 ASP A 67 141.14 -176.58
REMARK 500 5 HIS A 53 94.48 -172.30
REMARK 500 5 GLU A 77 -146.72 -155.84
REMARK 500 5 THR A 85 28.55 37.14
REMARK 500 6 GLN A 49 6.78 42.21
REMARK 500 6 HIS A 53 84.20 44.48
REMARK 500 6 ILE A 65 36.49 36.27
REMARK 500 6 ASP A 67 116.78 67.57
REMARK 500 6 TYR A 68 -169.90 -76.70
REMARK 500 6 THR A 85 20.87 40.03
REMARK 500 7 HIS A 53 88.47 13.98
REMARK 500 7 THR A 85 22.95 46.10
REMARK 500 8 GLN A 49 4.91 43.29
REMARK 500 8 CYS A 50 54.97 -112.53
REMARK 500 8 GLU A 51 163.93 -40.61
REMARK 500 8 HIS A 53 93.03 -174.26
REMARK 500 8 LYS A 62 -132.75 -103.29
REMARK 500 8 THR A 85 16.15 44.29
REMARK 500 9 ASP A 48 29.73 -166.43
REMARK 500 9 CYS A 50 14.32 -163.87
REMARK 500 9 HIS A 53 91.50 39.65
REMARK 500 9 ASP A 63 146.28 63.22
REMARK 500 9 ALA A 73 162.28 115.88
REMARK 500 9 CYS A 81 26.94 94.10
REMARK 500 9 THR A 85 5.33 47.54
REMARK 500 10 ASP A 48 66.67 -119.44
REMARK 500 10 CYS A 50 -22.75 -145.23
REMARK 500 10 HIS A 53 82.18 44.30
REMARK 500 10 ASP A 67 153.51 68.08
REMARK 500 10 GLU A 77 -145.86 -143.20
REMARK 500
REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS.
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 GLU A 82 PHE A 83 5 -148.03
REMARK 500 GLU A 82 PHE A 83 11 -149.73
REMARK 500 GLU A 82 PHE A 83 12 -149.55
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 1 HIS A 53 0.14 SIDE CHAIN
REMARK 500 1 HIS A 60 0.18 SIDE CHAIN
REMARK 500 1 TYR A 68 0.09 SIDE CHAIN
REMARK 500 1 PHE A 83 0.33 SIDE CHAIN
REMARK 500 2 HIS A 53 0.15 SIDE CHAIN
REMARK 500 2 HIS A 60 0.11 SIDE CHAIN
REMARK 500 2 TYR A 68 0.11 SIDE CHAIN
REMARK 500 3 HIS A 53 0.12 SIDE CHAIN
REMARK 500 3 HIS A 60 0.18 SIDE CHAIN
REMARK 500 3 TYR A 68 0.13 SIDE CHAIN
REMARK 500 4 HIS A 53 0.16 SIDE CHAIN
REMARK 500 4 HIS A 60 0.17 SIDE CHAIN
REMARK 500 4 TYR A 68 0.11 SIDE CHAIN
REMARK 500 5 HIS A 53 0.17 SIDE CHAIN
REMARK 500 5 HIS A 60 0.16 SIDE CHAIN
REMARK 500 5 TYR A 68 0.11 SIDE CHAIN
REMARK 500 5 PHE A 83 0.32 SIDE CHAIN
REMARK 500 6 HIS A 53 0.16 SIDE CHAIN
REMARK 500 6 HIS A 60 0.18 SIDE CHAIN
REMARK 500 6 TYR A 68 0.07 SIDE CHAIN
REMARK 500 7 HIS A 53 0.15 SIDE CHAIN
REMARK 500 7 HIS A 60 0.15 SIDE CHAIN
REMARK 500 7 TYR A 68 0.10 SIDE CHAIN
REMARK 500 8 HIS A 53 0.16 SIDE CHAIN
REMARK 500 8 HIS A 60 0.16 SIDE CHAIN
REMARK 500 8 TYR A 68 0.11 SIDE CHAIN
REMARK 500 9 HIS A 53 0.17 SIDE CHAIN
REMARK 500 9 HIS A 60 0.16 SIDE CHAIN
REMARK 500 9 TYR A 68 0.11 SIDE CHAIN
REMARK 500 10 HIS A 53 0.17 SIDE CHAIN
REMARK 500 10 HIS A 60 0.17 SIDE CHAIN
REMARK 500 10 TYR A 68 0.11 SIDE CHAIN
REMARK 500 10 PHE A 76 0.08 SIDE CHAIN
REMARK 500 10 PHE A 83 0.30 SIDE CHAIN
REMARK 500 11 HIS A 53 0.16 SIDE CHAIN
REMARK 500 11 HIS A 60 0.14 SIDE CHAIN
REMARK 500 11 TYR A 68 0.06 SIDE CHAIN
REMARK 500 11 PHE A 83 0.32 SIDE CHAIN
REMARK 500 12 HIS A 53 0.17 SIDE CHAIN
REMARK 500 12 HIS A 60 0.17 SIDE CHAIN
REMARK 500 12 TYR A 68 0.09 SIDE CHAIN
REMARK 500 12 PHE A 83 0.32 SIDE CHAIN
REMARK 500 13 HIS A 53 0.16 SIDE CHAIN
REMARK 500 13 HIS A 60 0.16 SIDE CHAIN
REMARK 500 13 TYR A 68 0.14 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 1 LYS A 45 10.17
REMARK 500 4 LYS A 45 10.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OH A 87
DBREF 1APO A 45 86 UNP P00743 FA10_BOVIN 85 126
SEQRES 1 A 42 LYS ASP GLY ASP GLN CYS GLU GLY HIS PRO CYS LEU ASN
SEQRES 2 A 42 GLN GLY HIS CYS LYS ASP GLY ILE GLY ASP TYR THR CYS
SEQRES 3 A 42 THR CYS ALA GLU GLY PHE GLU GLY LYS ASN CYS GLU PHE
SEQRES 4 A 42 SER THR ARG
HET OH A 87 2
HETNAM OH HYDROXIDE ION
FORMUL 2 OH H O 1-
SHEET 1 S1 2 GLY A 59 ASP A 63 0
SHEET 2 S1 2 TYR A 68 CYS A 72 -1
SHEET 1 S2 2 PHE A 76 GLU A 77 0
SHEET 2 S2 2 PHE A 83 SER A 84 -1
SSBOND 1 CYS A 50 CYS A 61 1555 1555 2.38
SSBOND 2 CYS A 55 CYS A 70 1555 1555 2.38
SSBOND 3 CYS A 72 CYS A 81 1555 1555 2.50
LINK CB ASP A 63 O OH A 87 1555 1555 1.46
SITE 1 AC1 2 ASP A 63 GLY A 64
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - 29 20 Bytes