Header list of 1rgd.pdb file
Complete list - 2 20 Bytes
HEADER DNA BINDING PROTEIN 06-JAN-95 1RGD
TITLE STRUCTURE REFINEMENT OF THE GLUCOCORTICOID RECEPTOR-DNA BINDING DOMAIN
TITLE 2 FROM NMR DATA BY RELAXATION MATRIX CALCULATIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOCORTICOID RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116
KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR M.A.A.VAN TILBORG,A.M.J.J.BONVIN,K.HARD,A.DAVIS,B.MALER,R.BOELENS,
AUTHOR 2 K.R.YAMAMOTO,R.KAPTEIN
REVDAT 3 02-MAR-22 1RGD 1 KEYWDS REMARK LINK
REVDAT 2 24-FEB-09 1RGD 1 VERSN
REVDAT 1 14-FEB-95 1RGD 0
JRNL AUTH M.A.VAN TILBORG,A.M.BONVIN,K.HARD,A.L.DAVIS,B.MALER,
JRNL AUTH 2 R.BOELENS,K.R.YAMAMOTO,R.KAPTEIN
JRNL TITL STRUCTURE REFINEMENT OF THE GLUCOCORTICOID RECEPTOR-DNA
JRNL TITL 2 BINDING DOMAIN FROM NMR DATA BY RELAXATION MATRIX
JRNL TITL 3 CALCULATIONS.
JRNL REF J.MOL.BIOL. V. 247 689 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7723024
JRNL DOI 10.1006/JMBI.1995.0173
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.F.LUISI,W.X.XU,Z.OTWINOWSKI,L.P.FREEDMAN,K.R.YAMAMOTO,
REMARK 1 AUTH 2 P.B.SIGLER
REMARK 1 TITL CRYSTALLOGRAPHIC ANALYSIS OF THE INTERACTION OF THE
REMARK 1 TITL 2 GLUCOCORTICOID RECEPTOR WITH DNA
REMARK 1 REF NATURE V. 352 497 1991
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.HARD,E.KELLENBACH,R.BOELENS,B.A.MALER,K.DAHLMAN,
REMARK 1 AUTH 2 L.P.FREEDMAN,J.CARLSTEDT-DUKE,K.R.YAMAMOTO,J.-A.GUSTAFSSON,
REMARK 1 AUTH 3 R.KAPTEIN
REMARK 1 TITL SOLUTION STRUCTURE OF THE GLUCOCORTICOID RECEPTOR
REMARK 1 TITL 2 DNA-BINDING DOMAIN
REMARK 1 REF SCIENCE V. 249 157 1990
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.HARD,E.KELLENBACH,R.BOELENS,R.KAPTEIN,K.DAHLMAN,
REMARK 1 AUTH 2 J.CARLSTEDT-DUKE,L.P.FREEDMAN,B.A.MALER,E.HYDE,
REMARK 1 AUTH 3 J.-A.GUSTAFSSON,K.R.YAMAMOTO
REMARK 1 TITL 1H NMR STUDIES OF THE GLUCOCORTICOID RECEPTOR DNA-BINDING
REMARK 1 TITL 2 DOMAIN: SEQUENTIAL ASSIGNMENTS AND IDENTIFICATION OF
REMARK 1 TITL 3 SECONDARY STRUCTURE ELEMENTS
REMARK 1 REF BIOCHEMISTRY V. 29 9015 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : IRMA, DINOSAUR
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RGD 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_1000176072.
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 : 11
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: 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 2 CYS A 56 CA CYS A 56 CB -0.083
REMARK 500 3 CYS A 1 CA CYS A 1 CB -0.085
REMARK 500 3 LYS A 26 CA LYS A 26 CB -0.162
REMARK 500 4 LYS A 26 CA LYS A 26 CB -0.151
REMARK 500 5 CYS A 1 CA CYS A 1 CB -0.111
REMARK 500 5 LYS A 26 CA LYS A 26 CB -0.168
REMARK 500 6 LYS A 26 CA LYS A 26 CB -0.154
REMARK 500 6 CYS A 43 CA CYS A 43 CB -0.079
REMARK 500 7 CYS A 1 CA CYS A 1 CB -0.090
REMARK 500 7 LYS A 26 CA LYS A 26 CB -0.183
REMARK 500 10 CYS A 56 CA CYS A 56 CB -0.081
REMARK 500 11 LYS A 26 CA LYS A 26 CB -0.134
REMARK 500 11 CYS A 56 CA CYS A 56 CB -0.091
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 CYS A 1 CB - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 1 CYS A 1 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 1 LEU A 2 CA - CB - CG ANGL. DEV. = -24.6 DEGREES
REMARK 500 1 VAL A 3 CA - CB - CG1 ANGL. DEV. = 15.7 DEGREES
REMARK 500 1 CYS A 4 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 1 GLU A 7 CA - C - N ANGL. DEV. = -15.8 DEGREES
REMARK 500 1 ALA A 8 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 1 TYR A 13 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 1 TYR A 13 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 VAL A 15 CB - CA - C ANGL. DEV. = 13.8 DEGREES
REMARK 500 1 CYS A 18 N - CA - CB ANGL. DEV. = 12.6 DEGREES
REMARK 500 1 PHE A 24 CB - CG - CD2 ANGL. DEV. = -16.6 DEGREES
REMARK 500 1 VAL A 29 C - N - CA ANGL. DEV. = 15.2 DEGREES
REMARK 500 1 VAL A 29 CA - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 1 HIS A 33 CB - CG - CD2 ANGL. DEV. = -14.1 DEGREES
REMARK 500 1 TYR A 35 N - CA - CB ANGL. DEV. = 12.5 DEGREES
REMARK 500 1 TYR A 35 CB - CG - CD2 ANGL. DEV. = -19.8 DEGREES
REMARK 500 1 TYR A 35 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 TYR A 35 CG - CD1 - CE1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 1 ARG A 40 CB - CA - C ANGL. DEV. = 18.5 DEGREES
REMARK 500 1 CYS A 43 CB - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 1 CYS A 43 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 GLN A 63 CB - CA - C ANGL. DEV. = 14.0 DEGREES
REMARK 500 2 CYS A 1 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 2 CYS A 1 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 LEU A 2 CA - CB - CG ANGL. DEV. = -23.8 DEGREES
REMARK 500 2 VAL A 3 CA - CB - CG1 ANGL. DEV. = 18.7 DEGREES
REMARK 500 2 CYS A 4 N - CA - CB ANGL. DEV. = 11.4 DEGREES
REMARK 500 2 GLU A 7 CA - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 2 ALA A 8 N - CA - CB ANGL. DEV. = -17.2 DEGREES
REMARK 500 2 TYR A 13 N - CA - CB ANGL. DEV. = 14.6 DEGREES
REMARK 500 2 TYR A 13 CB - CG - CD2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 2 TYR A 13 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 TYR A 13 CB - CG - CD1 ANGL. DEV. = -17.8 DEGREES
REMARK 500 2 TYR A 13 CG - CD2 - CE2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 2 TYR A 13 CD1 - CE1 - CZ ANGL. DEV. = -5.7 DEGREES
REMARK 500 2 VAL A 15 CB - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 2 PHE A 24 CB - CG - CD2 ANGL. DEV. = -17.8 DEGREES
REMARK 500 2 PHE A 25 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 LYS A 26 CB - CA - C ANGL. DEV. = 14.0 DEGREES
REMARK 500 2 LYS A 26 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 2 HIS A 33 CB - CG - CD2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 2 TYR A 35 CB - CG - CD2 ANGL. DEV. = -11.9 DEGREES
REMARK 500 2 TYR A 35 CB - CG - CD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 2 CYS A 43 CB - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 2 CYS A 43 CA - CB - SG ANGL. DEV. = 10.7 DEGREES
REMARK 500 2 ILE A 44 N - CA - CB ANGL. DEV. = 14.3 DEGREES
REMARK 500 2 ASP A 46 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 2 CYS A 56 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 2 CYS A 56 CB - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 306 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 1 VAL A 3 -74.95 -102.72
REMARK 500 1 SER A 5 12.51 87.00
REMARK 500 1 GLU A 7 124.55 -18.46
REMARK 500 1 CYS A 11 -168.38 48.62
REMARK 500 1 ASN A 34 116.56 73.55
REMARK 500 1 TYR A 35 72.89 -119.48
REMARK 500 1 LEU A 36 55.37 -69.52
REMARK 500 1 CYS A 37 179.63 38.41
REMARK 500 1 ALA A 38 20.26 -77.53
REMARK 500 1 ARG A 40 73.45 -116.03
REMARK 500 1 ASN A 41 65.61 16.46
REMARK 500 1 ASP A 42 70.07 69.21
REMARK 500 1 ASP A 46 -153.39 -140.39
REMARK 500 1 LYS A 47 -37.21 25.65
REMARK 500 1 ARG A 49 61.01 65.25
REMARK 500 1 CYS A 53 96.88 -175.78
REMARK 500 1 LEU A 68 -81.09 -9.40
REMARK 500 1 ALA A 70 82.92 18.13
REMARK 500 2 VAL A 3 -74.41 -95.42
REMARK 500 2 GLU A 7 134.56 -8.47
REMARK 500 2 CYS A 11 -73.66 142.96
REMARK 500 2 VAL A 15 140.38 -36.53
REMARK 500 2 LYS A 26 -74.60 -38.79
REMARK 500 2 LEU A 36 -101.70 70.40
REMARK 500 2 CYS A 37 80.79 -24.28
REMARK 500 2 ARG A 40 -89.73 -99.50
REMARK 500 2 ASN A 41 -12.12 89.70
REMARK 500 2 ILE A 44 86.02 -59.03
REMARK 500 2 ILE A 45 23.62 -70.04
REMARK 500 2 LYS A 47 -3.73 -57.07
REMARK 500 2 ARG A 49 -93.88 -124.83
REMARK 500 2 LYS A 51 -32.62 -147.32
REMARK 500 2 GLU A 69 47.68 -93.03
REMARK 500 2 ALA A 70 -58.03 63.86
REMARK 500 3 VAL A 3 -72.14 -95.79
REMARK 500 3 SER A 5 -9.01 81.34
REMARK 500 3 GLU A 7 140.64 -9.99
REMARK 500 3 CYS A 11 -76.34 61.08
REMARK 500 3 TYR A 13 -22.02 111.93
REMARK 500 3 LEU A 16 58.67 -68.77
REMARK 500 3 LEU A 36 112.01 62.02
REMARK 500 3 ALA A 38 17.87 56.50
REMARK 500 3 ASN A 41 56.13 -98.93
REMARK 500 3 ILE A 45 -43.87 80.42
REMARK 500 3 LYS A 47 -17.83 -33.72
REMARK 500 3 ARG A 50 167.75 91.88
REMARK 500 3 LYS A 51 81.15 -61.06
REMARK 500 3 ASN A 52 -66.95 -93.83
REMARK 500 3 LEU A 68 -8.17 -43.47
REMARK 500 3 ALA A 70 124.24 -30.56
REMARK 500
REMARK 500 THIS ENTRY HAS 184 RAMACHANDRAN OUTLIERS.
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 TYR A 13 0.24 SIDE CHAIN
REMARK 500 1 PHE A 24 0.21 SIDE CHAIN
REMARK 500 1 TYR A 35 0.18 SIDE CHAIN
REMARK 500 1 TYR A 58 0.07 SIDE CHAIN
REMARK 500 2 PHE A 24 0.25 SIDE CHAIN
REMARK 500 2 TYR A 35 0.10 SIDE CHAIN
REMARK 500 2 TYR A 58 0.09 SIDE CHAIN
REMARK 500 3 TYR A 13 0.12 SIDE CHAIN
REMARK 500 3 PHE A 24 0.30 SIDE CHAIN
REMARK 500 3 TYR A 35 0.14 SIDE CHAIN
REMARK 500 4 PHE A 24 0.26 SIDE CHAIN
REMARK 500 4 TYR A 35 0.12 SIDE CHAIN
REMARK 500 5 TYR A 13 0.13 SIDE CHAIN
REMARK 500 5 PHE A 24 0.27 SIDE CHAIN
REMARK 500 5 TYR A 35 0.12 SIDE CHAIN
REMARK 500 5 TYR A 58 0.12 SIDE CHAIN
REMARK 500 6 TYR A 13 0.09 SIDE CHAIN
REMARK 500 6 PHE A 24 0.28 SIDE CHAIN
REMARK 500 6 TYR A 35 0.13 SIDE CHAIN
REMARK 500 6 TYR A 58 0.08 SIDE CHAIN
REMARK 500 7 PHE A 24 0.27 SIDE CHAIN
REMARK 500 7 TYR A 35 0.10 SIDE CHAIN
REMARK 500 8 TYR A 13 0.06 SIDE CHAIN
REMARK 500 8 PHE A 24 0.27 SIDE CHAIN
REMARK 500 8 PHE A 25 0.13 SIDE CHAIN
REMARK 500 8 TYR A 35 0.10 SIDE CHAIN
REMARK 500 8 TYR A 58 0.09 SIDE CHAIN
REMARK 500 9 TYR A 13 0.13 SIDE CHAIN
REMARK 500 9 PHE A 24 0.27 SIDE CHAIN
REMARK 500 9 TYR A 35 0.10 SIDE CHAIN
REMARK 500 9 ARG A 50 0.08 SIDE CHAIN
REMARK 500 10 PHE A 24 0.07 SIDE CHAIN
REMARK 500 10 TYR A 35 0.10 SIDE CHAIN
REMARK 500 11 TYR A 13 0.20 SIDE CHAIN
REMARK 500 11 PHE A 24 0.10 SIDE CHAIN
REMARK 500 11 TYR A 35 0.23 SIDE CHAIN
REMARK 500 11 ARG A 71 0.09 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 ASP A 6 11.18
REMARK 500 1 GLU A 7 10.50
REMARK 500 1 VAL A 15 -14.65
REMARK 500 1 LEU A 16 11.06
REMARK 500 1 SER A 20 -12.83
REMARK 500 1 PHE A 25 -14.57
REMARK 500 1 VAL A 29 10.74
REMARK 500 1 CYS A 37 10.91
REMARK 500 1 GLY A 39 -12.64
REMARK 500 1 ARG A 40 18.56
REMARK 500 1 ASN A 41 12.71
REMARK 500 1 CYS A 43 12.52
REMARK 500 1 ILE A 45 -15.95
REMARK 500 1 ASP A 46 -13.32
REMARK 500 1 ALA A 55 -11.52
REMARK 500 1 ARG A 57 -11.41
REMARK 500 1 ARG A 59 -12.69
REMARK 500 1 CYS A 61 -15.04
REMARK 500 1 ALA A 64 10.31
REMARK 500 1 GLU A 69 11.07
REMARK 500 2 SER A 5 -11.41
REMARK 500 2 SER A 20 -11.29
REMARK 500 2 PHE A 24 -14.08
REMARK 500 2 PHE A 25 -11.25
REMARK 500 2 ALA A 28 -10.72
REMARK 500 2 ARG A 40 16.04
REMARK 500 2 CYS A 43 12.25
REMARK 500 2 ALA A 55 -15.29
REMARK 500 2 ARG A 57 -11.29
REMARK 500 2 ARG A 59 -13.22
REMARK 500 2 CYS A 61 -14.88
REMARK 500 2 ALA A 64 11.01
REMARK 500 3 CYS A 4 10.55
REMARK 500 3 ASP A 6 11.54
REMARK 500 3 TYR A 13 11.00
REMARK 500 3 SER A 20 -11.03
REMARK 500 3 LYS A 22 -10.15
REMARK 500 3 PHE A 25 -12.50
REMARK 500 3 ARG A 40 -13.98
REMARK 500 3 ILE A 44 14.79
REMARK 500 3 ARG A 49 12.99
REMARK 500 3 ARG A 50 10.10
REMARK 500 3 ARG A 57 -16.45
REMARK 500 3 ARG A 59 -12.88
REMARK 500 3 CYS A 61 -16.87
REMARK 500 3 ALA A 64 11.37
REMARK 500 3 LEU A 68 -10.31
REMARK 500 3 GLU A 69 11.80
REMARK 500 4 SER A 5 -14.50
REMARK 500 4 ASP A 6 10.08
REMARK 500
REMARK 500 THIS ENTRY HAS 173 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 72 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 1 SG
REMARK 620 2 CYS A 4 SG 89.0
REMARK 620 3 CYS A 18 SG 133.0 107.4
REMARK 620 4 CYS A 21 SG 110.2 137.5 87.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 73 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 37 SG
REMARK 620 2 CYS A 43 SG 129.4
REMARK 620 3 CYS A 53 SG 93.5 108.1
REMARK 620 4 CYS A 56 SG 105.8 90.3 135.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 73
DBREF 1RGD A 1 71 UNP P06536 GCR_RAT 440 510
SEQRES 1 A 71 CYS LEU VAL CYS SER ASP GLU ALA SER GLY CYS HIS TYR
SEQRES 2 A 71 GLY VAL LEU THR CYS GLY SER CYS LYS VAL PHE PHE LYS
SEQRES 3 A 71 ARG ALA VAL GLU GLY GLN HIS ASN TYR LEU CYS ALA GLY
SEQRES 4 A 71 ARG ASN ASP CYS ILE ILE ASP LYS ILE ARG ARG LYS ASN
SEQRES 5 A 71 CYS PRO ALA CYS ARG TYR ARG LYS CYS LEU GLN ALA GLY
SEQRES 6 A 71 MET ASN LEU GLU ALA ARG
HET ZN A 72 1
HET ZN A 73 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLY A 19 GLU A 30 1 12
HELIX 2 2 PRO A 54 ALA A 64 1 11
LINK SG CYS A 1 ZN ZN A 72 1555 1555 2.42
LINK SG CYS A 4 ZN ZN A 72 1555 1555 2.57
LINK SG CYS A 18 ZN ZN A 72 1555 1555 2.29
LINK SG CYS A 21 ZN ZN A 72 1555 1555 2.61
LINK SG CYS A 37 ZN ZN A 73 1555 1555 2.50
LINK SG CYS A 43 ZN ZN A 73 1555 1555 2.50
LINK SG CYS A 53 ZN ZN A 73 1555 1555 2.87
LINK SG CYS A 56 ZN ZN A 73 1555 1555 2.74
SITE 1 AC1 5 CYS A 1 CYS A 4 CYS A 18 CYS A 21
SITE 2 AC1 5 ARG A 57
SITE 1 AC2 4 CYS A 37 CYS A 43 CYS A 53 CYS A 56
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 - 2 20 Bytes