Header list of 1aw6.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSCRIPTION REGULATION 10-OCT-97 1AW6
TITLE GAL4 (CD), NMR, 24 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAL4 (CD);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XA-90
KEYWDS TRANSCRIPTION REGULATION, DNA-BINDING
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR J.D.BALEJA,G.WAGNER
REVDAT 3 16-FEB-22 1AW6 1 REMARK LINK
REVDAT 2 24-FEB-09 1AW6 1 VERSN
REVDAT 1 15-APR-98 1AW6 0
SPRSDE 15-APR-98 1AW6 125D
JRNL AUTH J.D.BALEJA,V.THANABAL,G.WAGNER
JRNL TITL REFINED SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF GAL4
JRNL TITL 2 AND USE OF 3J(113CD,1H) IN STRUCTURE DETERMINATION.
JRNL REF J.BIOMOL.NMR V. 10 397 1997
JRNL REFN ISSN 0925-2738
JRNL PMID 9460244
JRNL DOI 10.1023/A:1018332327565
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION.
REMARK 4
REMARK 4 1AW6 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_1000171331.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BIOSYM
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
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 HB3 GLN A 9 HD3 LYS A 23 1.26
REMARK 500 HG3 GLU A 24 HA CYS A 28 1.27
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 2 GLU A 8 CD GLU A 8 OE1 -0.126
REMARK 500 2 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 2 GLU A 37 CD GLU A 37 OE1 -0.125
REMARK 500 2 GLU A 37 CD GLU A 37 OE2 0.110
REMARK 500 3 GLU A 8 CD GLU A 8 OE1 0.109
REMARK 500 3 GLU A 24 CD GLU A 24 OE1 0.109
REMARK 500 3 GLU A 24 CD GLU A 24 OE2 -0.126
REMARK 500 5 GLU A 8 CD GLU A 8 OE1 -0.132
REMARK 500 5 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 5 GLU A 24 CD GLU A 24 OE1 0.113
REMARK 500 5 GLU A 24 CD GLU A 24 OE2 -0.127
REMARK 500 6 GLU A 8 CD GLU A 8 OE1 -0.126
REMARK 500 6 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 6 GLU A 24 CD GLU A 24 OE1 0.113
REMARK 500 6 GLU A 24 CD GLU A 24 OE2 -0.126
REMARK 500 7 GLU A 8 CD GLU A 8 OE1 -0.127
REMARK 500 7 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 7 GLU A 24 CD GLU A 24 OE1 0.113
REMARK 500 7 GLU A 24 CD GLU A 24 OE2 -0.126
REMARK 500 7 GLU A 37 CD GLU A 37 OE1 -0.126
REMARK 500 7 GLU A 37 CD GLU A 37 OE2 0.110
REMARK 500 8 GLU A 8 CD GLU A 8 OE1 -0.126
REMARK 500 8 GLU A 8 CD GLU A 8 OE2 0.109
REMARK 500 8 GLU A 37 CD GLU A 37 OE1 -0.126
REMARK 500 8 GLU A 37 CD GLU A 37 OE2 0.110
REMARK 500 9 GLU A 8 CD GLU A 8 OE1 -0.127
REMARK 500 9 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 9 GLU A 24 CD GLU A 24 OE1 0.111
REMARK 500 9 GLU A 24 CD GLU A 24 OE2 -0.125
REMARK 500 9 GLU A 37 CD GLU A 37 OE1 -0.125
REMARK 500 9 GLU A 37 CD GLU A 37 OE2 0.110
REMARK 500 10 GLU A 24 CD GLU A 24 OE1 0.113
REMARK 500 10 GLU A 24 CD GLU A 24 OE2 -0.127
REMARK 500 10 GLU A 37 CD GLU A 37 OE1 -0.126
REMARK 500 10 GLU A 37 CD GLU A 37 OE2 0.110
REMARK 500 11 GLU A 8 CD GLU A 8 OE1 -0.126
REMARK 500 11 GLU A 8 CD GLU A 8 OE2 0.111
REMARK 500 11 GLU A 24 CD GLU A 24 OE1 0.110
REMARK 500 11 GLU A 24 CD GLU A 24 OE2 -0.122
REMARK 500 12 GLU A 24 CD GLU A 24 OE1 0.114
REMARK 500 12 GLU A 24 CD GLU A 24 OE2 -0.126
REMARK 500 12 GLU A 37 CD GLU A 37 OE1 -0.126
REMARK 500 12 GLU A 37 CD GLU A 37 OE2 0.110
REMARK 500 13 GLU A 8 CD GLU A 8 OE1 -0.126
REMARK 500 13 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 13 GLU A 24 CD GLU A 24 OE1 0.109
REMARK 500 13 GLU A 24 CD GLU A 24 OE2 -0.126
REMARK 500 14 GLU A 24 CD GLU A 24 OE1 0.112
REMARK 500 14 GLU A 24 CD GLU A 24 OE2 -0.127
REMARK 500 15 GLU A 8 CD GLU A 8 OE1 -0.125
REMARK 500
REMARK 500 THIS ENTRY HAS 81 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 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 TYR A 40 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 2 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 2 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ASP A 12 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 TYR A 40 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 5 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 6 ASP A 12 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 6 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 6 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 7 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 7 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 8 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 8 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 9 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 9 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 9 ASN A 35 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 9 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 9 TYR A 40 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 10 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 10 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 10 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 11 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 11 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ASP A 12 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 12 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 13 ASP A 12 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 13 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 13 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 14 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 14 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 14 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 15 ASP A 12 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 15 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 15 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 16 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 16 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 16 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 17 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 17 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 17 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 70 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 LYS A 2 118.08 -160.31
REMARK 500 1 LEU A 3 139.07 73.43
REMARK 500 1 LEU A 4 -48.70 -147.06
REMARK 500 1 SER A 6 -156.62 -67.40
REMARK 500 1 ILE A 7 25.51 -148.79
REMARK 500 1 ALA A 10 123.14 177.04
REMARK 500 1 LYS A 18 72.90 60.42
REMARK 500 1 LYS A 23 9.19 84.89
REMARK 500 1 GLU A 24 152.91 -46.29
REMARK 500 1 CYS A 28 -174.18 -57.35
REMARK 500 1 LYS A 30 -71.64 -45.86
REMARK 500 1 ASN A 35 82.37 51.43
REMARK 500 1 GLU A 37 64.23 -106.02
REMARK 500 1 CYS A 38 97.99 -44.96
REMARK 500 1 TYR A 40 55.05 -99.07
REMARK 500 1 SER A 41 83.01 -154.74
REMARK 500 1 PRO A 42 -81.80 -41.81
REMARK 500 2 LYS A 2 -83.30 -41.51
REMARK 500 2 LEU A 4 26.91 114.93
REMARK 500 2 SER A 5 -50.84 -138.73
REMARK 500 2 ILE A 7 135.55 162.49
REMARK 500 2 GLU A 8 54.96 -96.29
REMARK 500 2 ALA A 10 128.83 69.63
REMARK 500 2 LYS A 18 74.95 56.18
REMARK 500 2 SER A 22 -29.86 -39.47
REMARK 500 2 LYS A 23 7.52 87.64
REMARK 500 2 GLU A 24 159.56 -44.66
REMARK 500 2 CYS A 28 -172.20 -56.25
REMARK 500 2 LYS A 30 -72.57 -46.78
REMARK 500 2 GLU A 37 71.24 -108.24
REMARK 500 2 CYS A 38 107.05 -45.67
REMARK 500 2 SER A 41 -175.55 59.01
REMARK 500 2 PRO A 42 -83.01 -59.27
REMARK 500 3 LEU A 4 29.50 -153.64
REMARK 500 3 SER A 6 -166.61 72.20
REMARK 500 3 ILE A 7 65.98 -173.50
REMARK 500 3 ALA A 10 114.92 70.07
REMARK 500 3 LYS A 18 71.54 61.08
REMARK 500 3 SER A 22 -29.54 -39.90
REMARK 500 3 LYS A 23 11.80 86.02
REMARK 500 3 CYS A 28 178.74 -54.19
REMARK 500 3 LYS A 30 -73.58 -45.73
REMARK 500 3 ASN A 35 81.40 45.35
REMARK 500 3 CYS A 38 91.81 -63.07
REMARK 500 3 SER A 41 -168.05 64.91
REMARK 500 3 PRO A 42 -58.88 -28.80
REMARK 500 4 LYS A 2 30.79 -163.73
REMARK 500 4 LEU A 4 -96.30 52.83
REMARK 500 4 SER A 5 -153.95 44.89
REMARK 500 4 ILE A 7 -20.33 159.04
REMARK 500
REMARK 500 THIS ENTRY HAS 355 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 40 0.20 SIDE CHAIN
REMARK 500 2 TYR A 40 0.10 SIDE CHAIN
REMARK 500 3 TYR A 40 0.13 SIDE CHAIN
REMARK 500 4 TYR A 40 0.09 SIDE CHAIN
REMARK 500 5 TYR A 40 0.17 SIDE CHAIN
REMARK 500 6 TYR A 40 0.13 SIDE CHAIN
REMARK 500 9 TYR A 40 0.10 SIDE CHAIN
REMARK 500 10 TYR A 40 0.19 SIDE CHAIN
REMARK 500 11 TYR A 40 0.11 SIDE CHAIN
REMARK 500 12 TYR A 40 0.07 SIDE CHAIN
REMARK 500 13 TYR A 40 0.14 SIDE CHAIN
REMARK 500 14 TYR A 40 0.13 SIDE CHAIN
REMARK 500 16 TYR A 40 0.09 SIDE CHAIN
REMARK 500 17 TYR A 40 0.09 SIDE CHAIN
REMARK 500 18 TYR A 40 0.22 SIDE CHAIN
REMARK 500 19 TYR A 40 0.12 SIDE CHAIN
REMARK 500 20 TYR A 40 0.17 SIDE CHAIN
REMARK 500 21 TYR A 40 0.31 SIDE CHAIN
REMARK 500 22 TYR A 40 0.16 SIDE CHAIN
REMARK 500 23 TYR A 40 0.09 SIDE CHAIN
REMARK 500 24 TYR A 40 0.34 SIDE CHAIN
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 CD A 44 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 14 SG 91.8
REMARK 620 3 CYS A 21 SG 109.4 105.9
REMARK 620 4 CYS A 28 SG 98.8 120.8 124.0
REMARK 620 5 CD A 45 CD 50.0 115.5 132.7 48.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 45 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 28 SG 102.7
REMARK 620 3 CYS A 31 SG 129.4 104.6
REMARK 620 4 CYS A 38 SG 95.0 117.1 108.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CD4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CADMIUM BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CD5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CADMIUM BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 44
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 45
DBREF 1AW6 A 1 43 UNP P04386 GAL4_YEAST 1 43
SEQRES 1 A 43 MET LYS LEU LEU SER SER ILE GLU GLN ALA CYS ASP ILE
SEQRES 2 A 43 CYS ARG LEU LYS LYS LEU LYS CYS SER LYS GLU LYS PRO
SEQRES 3 A 43 LYS CYS ALA LYS CYS LEU LYS ASN ASN TRP GLU CYS ARG
SEQRES 4 A 43 TYR SER PRO LYS
HET CD A 44 1
HET CD A 45 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 2(CD 2+)
HELIX 1 A ASP A 12 LYS A 17 1 6
HELIX 2 B ALA A 29 ASN A 34 1 6
LINK SG CYS A 11 CD CD A 44 1555 1555 2.44
LINK SG CYS A 11 CD CD A 45 1555 1555 2.44
LINK SG CYS A 14 CD CD A 44 1555 1555 2.56
LINK SG CYS A 21 CD CD A 44 1555 1555 2.47
LINK SG CYS A 28 CD CD A 44 1555 1555 2.55
LINK SG CYS A 28 CD CD A 45 1555 1555 2.41
LINK SG CYS A 31 CD CD A 45 1555 1555 2.45
LINK SG CYS A 38 CD CD A 45 1555 1555 2.44
LINK CD CD A 44 CD CD A 45 1555 1555 3.14
CISPEP 1 LYS A 25 PRO A 26 1 -3.39
CISPEP 2 LYS A 25 PRO A 26 2 -3.56
CISPEP 3 LYS A 25 PRO A 26 3 -3.91
CISPEP 4 LYS A 25 PRO A 26 4 -3.51
CISPEP 5 LYS A 25 PRO A 26 5 -3.15
CISPEP 6 LYS A 25 PRO A 26 6 -3.19
CISPEP 7 LYS A 25 PRO A 26 7 -3.12
CISPEP 8 LYS A 25 PRO A 26 8 -3.46
CISPEP 9 LYS A 25 PRO A 26 9 -3.33
CISPEP 10 LYS A 25 PRO A 26 10 -3.11
CISPEP 11 LYS A 25 PRO A 26 11 -3.64
CISPEP 12 LYS A 25 PRO A 26 12 -3.64
CISPEP 13 LYS A 25 PRO A 26 13 -3.45
CISPEP 14 LYS A 25 PRO A 26 14 -3.36
CISPEP 15 LYS A 25 PRO A 26 15 -3.21
CISPEP 16 LYS A 25 PRO A 26 16 -3.35
CISPEP 17 LYS A 25 PRO A 26 17 -3.41
CISPEP 18 LYS A 25 PRO A 26 18 -2.93
CISPEP 19 LYS A 25 PRO A 26 19 -3.24
CISPEP 20 LYS A 25 PRO A 26 20 -3.06
CISPEP 21 LYS A 25 PRO A 26 21 -3.43
CISPEP 22 LYS A 25 PRO A 26 22 -3.48
CISPEP 23 LYS A 25 PRO A 26 23 -2.62
CISPEP 24 LYS A 25 PRO A 26 24 -3.37
SITE 1 CD4 4 CYS A 11 CYS A 14 CYS A 21 CYS A 28
SITE 1 CD5 4 CYS A 11 CYS A 28 CYS A 31 CYS A 38
SITE 1 AC1 5 CYS A 11 CYS A 14 CYS A 21 CYS A 28
SITE 2 AC1 5 CD A 45
SITE 1 AC2 5 CYS A 11 CYS A 28 CYS A 31 CYS A 38
SITE 2 AC2 5 CD A 44
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 16 2 Bytes