Header list of 1hcp.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION REGULATION 23-NOV-93 1HCP
TITLE DNA RECOGNITION BY THE OESTROGEN RECEPTOR: FROM SOLUTION TO THE
TITLE 2 CRYSTAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN/CHICKEN ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 OTHER_DETAILS: CHICKEN PROTEIN HAS IDENTICAL AMINO ACID SEQUENCE
KEYWDS TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR J.W.R.SCHWABE,D.RHODES,D.NEUHAUS
REVDAT 3 23-FEB-22 1HCP 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1HCP 1 VERSN
REVDAT 1 23-NOV-95 1HCP 0
JRNL AUTH J.W.SCHWABE,L.CHAPMAN,J.T.FINCH,D.RHODES,D.NEUHAUS
JRNL TITL DNA RECOGNITION BY THE OESTROGEN RECEPTOR: FROM SOLUTION TO
JRNL TITL 2 THE CRYSTAL.
JRNL REF STRUCTURE V. 1 187 1993
JRNL REFN ISSN 0969-2126
JRNL PMID 16100953
JRNL DOI 10.1016/0969-2126(93)90020-H
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.W.R.SCHWABE,D.RHODES
REMARK 1 TITL BEYOND ZINC FINGERS: STEROID HORMONE RECEPTORS HAVE A NOVEL
REMARK 1 TITL 2 MOTIF FOR DNA RECOGNITION
REMARK 1 REF TRENDS BIOCHEM.SCI. V. 16 291 1991
REMARK 1 REFN ISSN 0968-0004
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.W.R.SCHWABE,D.NEUHAUS,D.RHODES
REMARK 1 TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF THE
REMARK 1 TITL 2 OESTROGEN RECEPTOR
REMARK 1 REF NATURE V. 348 450 1990
REMARK 1 REFN ISSN 0028-0836
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 1HCP 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_1000173781.
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 : 30
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 76
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 H GLY A 20 H VAL A 21 1.31
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 HIS A 18 CG HIS A 18 ND1 -0.118
REMARK 500 1 TRP A 22 CG TRP A 22 CD2 -0.119
REMARK 500 1 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 2 HIS A 18 CG HIS A 18 ND1 -0.111
REMARK 500 2 TRP A 22 CG TRP A 22 CD2 -0.122
REMARK 500 2 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 3 HIS A 18 CG HIS A 18 ND1 -0.120
REMARK 500 3 TRP A 22 CG TRP A 22 CD2 -0.125
REMARK 500 3 HIS A 38 CG HIS A 38 ND1 -0.121
REMARK 500 4 HIS A 18 CG HIS A 18 ND1 -0.118
REMARK 500 4 TRP A 22 CG TRP A 22 CD2 -0.123
REMARK 500 4 HIS A 38 CG HIS A 38 ND1 -0.122
REMARK 500 5 HIS A 18 CG HIS A 18 ND1 -0.111
REMARK 500 5 TRP A 22 CG TRP A 22 CD2 -0.123
REMARK 500 5 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 6 HIS A 18 CG HIS A 18 ND1 -0.116
REMARK 500 6 TRP A 22 CG TRP A 22 CD2 -0.123
REMARK 500 6 HIS A 38 CG HIS A 38 ND1 -0.122
REMARK 500 7 HIS A 18 CG HIS A 18 ND1 -0.121
REMARK 500 7 TRP A 22 CG TRP A 22 CD2 -0.118
REMARK 500 7 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 8 HIS A 18 CG HIS A 18 ND1 -0.118
REMARK 500 8 TRP A 22 CG TRP A 22 CD2 -0.124
REMARK 500 8 HIS A 38 CG HIS A 38 ND1 -0.119
REMARK 500 9 HIS A 18 CG HIS A 18 ND1 -0.120
REMARK 500 9 TRP A 22 CG TRP A 22 CD2 -0.125
REMARK 500 9 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 10 HIS A 18 CG HIS A 18 ND1 -0.103
REMARK 500 10 TRP A 22 CG TRP A 22 CD2 -0.126
REMARK 500 10 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 11 HIS A 18 CG HIS A 18 ND1 -0.120
REMARK 500 11 TRP A 22 CG TRP A 22 CD2 -0.112
REMARK 500 11 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 12 HIS A 18 CG HIS A 18 ND1 -0.113
REMARK 500 12 TRP A 22 CG TRP A 22 CD2 -0.113
REMARK 500 12 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 13 HIS A 18 CG HIS A 18 ND1 -0.116
REMARK 500 13 TRP A 22 CG TRP A 22 CD2 -0.124
REMARK 500 13 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 14 HIS A 18 CG HIS A 18 ND1 -0.107
REMARK 500 14 TRP A 22 CG TRP A 22 CD2 -0.120
REMARK 500 14 HIS A 38 CG HIS A 38 ND1 -0.121
REMARK 500 15 HIS A 18 CG HIS A 18 ND1 -0.105
REMARK 500 15 TRP A 22 CG TRP A 22 CD2 -0.127
REMARK 500 15 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 16 HIS A 18 CG HIS A 18 ND1 -0.119
REMARK 500 16 TRP A 22 CG TRP A 22 CD2 -0.119
REMARK 500 16 HIS A 38 CG HIS A 38 ND1 -0.120
REMARK 500 17 HIS A 18 CG HIS A 18 ND1 -0.119
REMARK 500 17 TRP A 22 CG TRP A 22 CD2 -0.116
REMARK 500
REMARK 500 THIS ENTRY HAS 90 BOND DEVIATIONS.
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 10 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 1 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 1 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 1 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 2 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 2 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 2 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 3 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 3 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 3 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 4 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 4 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 4 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 5 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 5 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 5 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 6 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 6 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 6 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 6 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 7 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 7 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 7 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 7 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 8 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 8 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 8 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 8 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 9 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 9 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 9 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 9 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 10 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 10 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 10 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 10 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 11 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 11 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 11 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 11 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 12 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 12 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 12 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 12 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 13 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 122 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 CYS A 7 89.08 -52.28
REMARK 500 1 ALA A 8 -16.32 -47.13
REMARK 500 1 CYS A 10 55.47 -167.46
REMARK 500 1 ASN A 11 -91.83 -164.46
REMARK 500 1 ASP A 12 -157.63 -173.25
REMARK 500 1 TYR A 13 103.22 -33.81
REMARK 500 1 HIS A 18 -47.96 -138.96
REMARK 500 1 CYS A 24 -169.55 -55.39
REMARK 500 1 GLU A 25 -66.48 -107.94
REMARK 500 1 ILE A 35 166.26 -41.02
REMARK 500 1 GLN A 36 142.80 72.27
REMARK 500 1 HIS A 38 99.56 -30.99
REMARK 500 1 ASN A 39 143.43 -171.99
REMARK 500 1 ASP A 40 30.65 -76.68
REMARK 500 1 MET A 42 142.79 -171.70
REMARK 500 1 PRO A 44 20.07 -60.26
REMARK 500 1 ALA A 45 -30.41 -160.72
REMARK 500 1 THR A 46 11.04 51.64
REMARK 500 1 ASN A 47 -90.35 -87.37
REMARK 500 1 CYS A 49 134.22 175.01
REMARK 500 1 ASP A 52 -89.23 -151.22
REMARK 500 1 LYS A 53 169.34 -44.42
REMARK 500 1 ASN A 54 -92.17 -91.70
REMARK 500 1 ARG A 55 -26.33 68.15
REMARK 500 1 ARG A 56 40.71 36.52
REMARK 500 1 LYS A 57 24.84 -160.38
REMARK 500 1 SER A 58 -99.94 -131.54
REMARK 500 1 MET A 73 121.59 -171.67
REMARK 500 1 LYS A 74 -42.28 -23.04
REMARK 500 2 LYS A 2 129.21 -171.54
REMARK 500 2 GLU A 3 99.59 51.67
REMARK 500 2 VAL A 9 -30.97 -165.42
REMARK 500 2 ASN A 11 -98.25 -165.78
REMARK 500 2 ASP A 12 -150.88 -176.10
REMARK 500 2 TYR A 13 100.08 -27.79
REMARK 500 2 HIS A 18 25.16 -143.29
REMARK 500 2 TYR A 19 13.47 -161.87
REMARK 500 2 TRP A 22 84.21 -68.14
REMARK 500 2 CYS A 24 -169.84 -51.70
REMARK 500 2 ILE A 35 -13.32 -43.46
REMARK 500 2 HIS A 38 58.54 -175.95
REMARK 500 2 ASP A 40 95.08 -66.25
REMARK 500 2 PRO A 44 31.66 -69.34
REMARK 500 2 ALA A 45 -22.56 -160.50
REMARK 500 2 THR A 46 9.56 58.75
REMARK 500 2 ASN A 47 42.34 -99.34
REMARK 500 2 GLN A 48 -74.59 61.52
REMARK 500 2 CYS A 49 144.14 68.84
REMARK 500 2 ASP A 52 145.01 159.63
REMARK 500 2 LYS A 53 -124.53 -176.46
REMARK 500
REMARK 500 THIS ENTRY HAS 748 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 ARG A 5 0.23 SIDE CHAIN
REMARK 500 1 ARG A 33 0.18 SIDE CHAIN
REMARK 500 1 ARG A 55 0.23 SIDE CHAIN
REMARK 500 1 ARG A 56 0.18 SIDE CHAIN
REMARK 500 1 ARG A 63 0.28 SIDE CHAIN
REMARK 500 1 ARG A 65 0.11 SIDE CHAIN
REMARK 500 2 ARG A 5 0.28 SIDE CHAIN
REMARK 500 2 ARG A 33 0.32 SIDE CHAIN
REMARK 500 2 ARG A 55 0.30 SIDE CHAIN
REMARK 500 2 ARG A 56 0.29 SIDE CHAIN
REMARK 500 2 ARG A 63 0.24 SIDE CHAIN
REMARK 500 2 ARG A 65 0.26 SIDE CHAIN
REMARK 500 3 ARG A 33 0.31 SIDE CHAIN
REMARK 500 3 ARG A 56 0.26 SIDE CHAIN
REMARK 500 3 ARG A 63 0.25 SIDE CHAIN
REMARK 500 3 ARG A 65 0.30 SIDE CHAIN
REMARK 500 4 ARG A 5 0.32 SIDE CHAIN
REMARK 500 4 ARG A 33 0.28 SIDE CHAIN
REMARK 500 4 ARG A 55 0.22 SIDE CHAIN
REMARK 500 4 ARG A 56 0.29 SIDE CHAIN
REMARK 500 5 ARG A 5 0.27 SIDE CHAIN
REMARK 500 5 ARG A 55 0.10 SIDE CHAIN
REMARK 500 5 ARG A 56 0.31 SIDE CHAIN
REMARK 500 5 ARG A 63 0.13 SIDE CHAIN
REMARK 500 5 ARG A 65 0.12 SIDE CHAIN
REMARK 500 6 ARG A 5 0.26 SIDE CHAIN
REMARK 500 6 ARG A 33 0.29 SIDE CHAIN
REMARK 500 6 ARG A 55 0.12 SIDE CHAIN
REMARK 500 6 ARG A 56 0.28 SIDE CHAIN
REMARK 500 6 ARG A 63 0.32 SIDE CHAIN
REMARK 500 6 ARG A 65 0.20 SIDE CHAIN
REMARK 500 7 ARG A 5 0.12 SIDE CHAIN
REMARK 500 7 ARG A 33 0.19 SIDE CHAIN
REMARK 500 7 ARG A 56 0.24 SIDE CHAIN
REMARK 500 7 ARG A 63 0.28 SIDE CHAIN
REMARK 500 7 ARG A 65 0.10 SIDE CHAIN
REMARK 500 8 ARG A 5 0.31 SIDE CHAIN
REMARK 500 8 TYR A 19 0.08 SIDE CHAIN
REMARK 500 8 ARG A 33 0.32 SIDE CHAIN
REMARK 500 8 ARG A 55 0.22 SIDE CHAIN
REMARK 500 8 ARG A 56 0.13 SIDE CHAIN
REMARK 500 8 ARG A 63 0.08 SIDE CHAIN
REMARK 500 8 ARG A 65 0.30 SIDE CHAIN
REMARK 500 9 ARG A 5 0.21 SIDE CHAIN
REMARK 500 9 ARG A 33 0.29 SIDE CHAIN
REMARK 500 9 ARG A 55 0.28 SIDE CHAIN
REMARK 500 9 ARG A 56 0.30 SIDE CHAIN
REMARK 500 9 ARG A 65 0.31 SIDE CHAIN
REMARK 500 10 ARG A 5 0.31 SIDE CHAIN
REMARK 500 10 TYR A 19 0.11 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 172 PLANE 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 98 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 7 SG
REMARK 620 2 CYS A 10 SG 112.7
REMARK 620 3 CYS A 24 SG 96.2 126.8
REMARK 620 4 CYS A 27 SG 131.9 97.8 93.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 99 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 43 SG
REMARK 620 2 CYS A 49 SG 103.1
REMARK 620 3 CYS A 59 SG 108.1 112.9
REMARK 620 4 CYS A 62 SG 106.9 106.6 118.0
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 98
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 99
DBREF 1HCP A 1 76 UNP P03372 ESR1_HUMAN 176 254
SEQADV 1HCP A UNP P03372 GLU 177 DELETION
SEQADV 1HCP A UNP P03372 SER 178 DELETION
SEQADV 1HCP A UNP P03372 ALA 179 DELETION
SEQRES 1 A 76 MET LYS GLU THR ARG TYR CYS ALA VAL CYS ASN ASP TYR
SEQRES 2 A 76 ALA SER GLY TYR HIS TYR GLY VAL TRP SER CYS GLU GLY
SEQRES 3 A 76 CYS LYS ALA PHE PHE LYS ARG SER ILE GLN GLY HIS ASN
SEQRES 4 A 76 ASP TYR MET CYS PRO ALA THR ASN GLN CYS THR ILE ASP
SEQRES 5 A 76 LYS ASN ARG ARG LYS SER CYS GLN ALA CYS ARG LEU ARG
SEQRES 6 A 76 LYS CYS TYR GLU VAL GLY MET MET LYS GLY GLY
HET ZN A 98 1
HET ZN A 99 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLU A 25 ILE A 35 1 11
HELIX 2 2 CYS A 59 GLY A 71 1 13
SHEET 1 A 2 GLY A 16 TYR A 17 0
SHEET 2 A 2 TRP A 22 SER A 23 -1 O SER A 23 N GLY A 16
LINK SG CYS A 7 ZN ZN A 98 1555 1555 2.30
LINK SG CYS A 10 ZN ZN A 98 1555 1555 2.32
LINK SG CYS A 24 ZN ZN A 98 1555 1555 2.29
LINK SG CYS A 27 ZN ZN A 98 1555 1555 2.29
LINK SG CYS A 43 ZN ZN A 99 1555 1555 2.30
LINK SG CYS A 49 ZN ZN A 99 1555 1555 2.30
LINK SG CYS A 59 ZN ZN A 99 1555 1555 2.31
LINK SG CYS A 62 ZN ZN A 99 1555 1555 2.30
SITE 1 AC1 4 CYS A 7 CYS A 10 CYS A 24 CYS A 27
SITE 1 AC2 4 CYS A 43 CYS A 49 CYS A 59 CYS A 62
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 - b 23 2 Bytes