Header list of 2da8.pdb file
Complete list - 1 20 Bytes
HEADER DNA/ANTIBIOTIC 09-APR-93 2DA8
TITLE SOLUTION STRUCTURE OF A COMPLEX BETWEEN (N-MECYS3,N-MECYS7)TANDEM AND
TITLE 2 (D(GATATC))2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSTIN A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: VALINE AT POSITIONS 4 AND 8;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*GP*AP*TP*AP*TP*C)-3');
COMPND 9 CHAIN: C, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: STREPTOMYCINEAE;
SOURCE 4 ORGANISM_TAXID: 1931;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES
KEYWDS BISINTERCALATOR, DEPSIPEPTIDE, QUINOXALINE, ANTIBIOTIC, ANTITUMOR,
KEYWDS 2 DNA-ANTIBIOTIC COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 8
AUTHOR K.J.ADDESS,J.S.SINSHEIMER,J.FEIGON
REVDAT 7 01-NOV-17 2DA8 1 REMARK
REVDAT 6 27-JUL-11 2DA8 1 HETATM KEYWDS REMARK
REVDAT 5 13-JUL-11 2DA8 1 VERSN
REVDAT 4 24-FEB-09 2DA8 1 VERSN
REVDAT 3 01-APR-03 2DA8 1 JRNL
REVDAT 2 15-JAN-95 2DA8 1 SEQRES
REVDAT 1 31-JAN-94 2DA8 0
JRNL AUTH K.J.ADDESS,J.S.SINSHEIMER,J.FEIGON
JRNL TITL SOLUTION STRUCTURE OF A COMPLEX BETWEEN
JRNL TITL 2 [N-MECYS3,N-MECYS7]TANDEM AND [D(GATATC)]2.
JRNL REF BIOCHEMISTRY V. 32 2498 1993
JRNL REFN ISSN 0006-2960
JRNL PMID 8448108
JRNL DOI 10.1021/BI00061A006
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: EIGHT STRUCTURES WERE GENERATED BY
REMARK 3 DISTANCE GEOMETRY. TWO DIMENSIONAL DERIVED NOE AND DIHEDRAL BOND
REMARK 3 ANGLE CONSTRAINTS WERE USED THROUGHOUT ALL STAGES OF THE
REMARK 3 STRUCTURE CALCULATIONS. AVERAGE R VALUE FOR 8 STRUCTURES 0.21
REMARK 4
REMARK 4 2DA8 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_1000177981.
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 : DSPACE
REMARK 210 METHOD USED : ENERGY MINIMIZATION, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS, NOE BASED
REMARK 210 RELAXATION REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 8
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 8
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: FOR DISTANCE GEOMETRY, FULL STRUCTURE EMBEDS WERE DONE
REMARK 210 USING THE PROGRAM DSPACE (HARE RESEARCH, INC.) AND SUBSTRUCTURE
REMARK 210 EMBEDS WERE DONE USING X-PLOR (A. T. BRUNGER, YALE UNIVERSITY).
REMARK 210 ALL REFINEMENT STEPS WERE DONE USING X-PLOR.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
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 1 VAL A 4 CB VAL A 4 CG2 0.150
REMARK 500 1 VAL A 8 CA VAL A 8 CB 0.140
REMARK 500 1 VAL A 8 CB VAL A 8 CG1 0.154
REMARK 500 1 VAL A 8 CB VAL A 8 CG2 0.127
REMARK 500 1 DT C 3 C5 DT C 3 C7 0.054
REMARK 500 1 DT C 5 C5 DT C 5 C7 0.064
REMARK 500 1 DT D 3 C5 DT D 3 C7 0.054
REMARK 500 1 DT D 5 C5 DT D 5 C7 0.062
REMARK 500 2 VAL A 4 CB VAL A 4 CG1 0.135
REMARK 500 2 VAL A 4 CB VAL A 4 CG2 0.144
REMARK 500 2 VAL A 8 CA VAL A 8 CB 0.144
REMARK 500 2 VAL A 8 CB VAL A 8 CG1 0.159
REMARK 500 2 VAL A 8 CB VAL A 8 CG2 0.134
REMARK 500 2 DT C 3 C5 DT C 3 C7 0.053
REMARK 500 2 DT C 5 C5 DT C 5 C7 0.065
REMARK 500 2 DT D 3 C5 DT D 3 C7 0.055
REMARK 500 2 DT D 5 C5 DT D 5 C7 0.062
REMARK 500 3 VAL A 4 CA VAL A 4 CB 0.136
REMARK 500 3 VAL A 4 CB VAL A 4 CG1 0.157
REMARK 500 3 VAL A 4 CB VAL A 4 CG2 0.134
REMARK 500 3 VAL A 8 CB VAL A 8 CG1 0.140
REMARK 500 3 VAL A 8 CB VAL A 8 CG2 0.179
REMARK 500 3 DT C 3 C5 DT C 3 C7 0.053
REMARK 500 3 DT C 5 C5 DT C 5 C7 0.067
REMARK 500 3 DT D 3 C5 DT D 3 C7 0.048
REMARK 500 3 DT D 5 C5 DT D 5 C7 0.066
REMARK 500 4 VAL A 4 CB VAL A 4 CG1 0.133
REMARK 500 4 VAL A 4 CB VAL A 4 CG2 0.159
REMARK 500 4 VAL A 8 CB VAL A 8 CG2 0.165
REMARK 500 4 DT C 3 C5 DT C 3 C7 0.055
REMARK 500 4 DT C 5 C5 DT C 5 C7 0.064
REMARK 500 4 DT D 3 C5 DT D 3 C7 0.052
REMARK 500 4 DT D 5 C5 DT D 5 C7 0.063
REMARK 500 5 DT C 3 C5 DT C 3 C7 0.046
REMARK 500 5 DT C 5 C5 DT C 5 C7 0.060
REMARK 500 5 DT D 3 C5 DT D 3 C7 0.045
REMARK 500 5 DT D 5 C5 DT D 5 C7 0.060
REMARK 500 6 VAL A 4 CB VAL A 4 CG1 0.151
REMARK 500 6 VAL A 4 CB VAL A 4 CG2 0.173
REMARK 500 6 DT C 3 C5 DT C 3 C7 0.053
REMARK 500 6 DT C 5 C5 DT C 5 C7 0.050
REMARK 500 6 DT D 3 C5 DT D 3 C7 0.051
REMARK 500 6 DT D 5 C5 DT D 5 C7 0.069
REMARK 500 7 DT C 3 C5 DT C 3 C7 0.049
REMARK 500 7 DT C 5 C5 DT C 5 C7 0.063
REMARK 500 7 DT D 3 C5 DT D 3 C7 0.049
REMARK 500 7 DT D 5 C5 DT D 5 C7 0.061
REMARK 500 8 VAL A 4 CA VAL A 4 CB 0.139
REMARK 500 8 VAL A 4 CB VAL A 4 CG1 0.158
REMARK 500 8 VAL A 4 CB VAL A 4 CG2 0.132
REMARK 500
REMARK 500 THIS ENTRY HAS 56 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 VAL A 4 CG1 - CB - CG2 ANGL. DEV. = -11.4 DEGREES
REMARK 500 1 VAL A 4 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 VAL A 8 CG1 - CB - CG2 ANGL. DEV. = -13.1 DEGREES
REMARK 500 1 VAL A 8 CA - CB - CG1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 1 DG C 1 C4' - C3' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 DG C 1 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 DG C 1 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DG C 1 C3' - O3' - P ANGL. DEV. = 9.1 DEGREES
REMARK 500 1 DA C 2 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT C 3 O4' - C1' - N1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 1 DA C 4 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 1 DC C 6 C4' - C3' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 1 DC C 6 O4' - C1' - N1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 DG D 1 C4' - C3' - C2' ANGL. DEV. = -4.4 DEGREES
REMARK 500 1 DG D 1 N7 - C8 - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 DG D 1 C8 - N9 - C4 ANGL. DEV. = -2.4 DEGREES
REMARK 500 1 DG D 1 C3' - O3' - P ANGL. DEV. = 10.0 DEGREES
REMARK 500 1 DA D 2 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DT D 3 O4' - C1' - N1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 1 DA D 4 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 1 DT D 5 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 DC D 6 C4' - C3' - C2' ANGL. DEV. = -4.7 DEGREES
REMARK 500 1 DC D 6 O4' - C1' - N1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 2 VAL A 4 CG1 - CB - CG2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 2 VAL A 4 CA - CB - CG1 ANGL. DEV. = 11.2 DEGREES
REMARK 500 2 VAL A 8 CG1 - CB - CG2 ANGL. DEV. = -13.2 DEGREES
REMARK 500 2 VAL A 8 CA - CB - CG1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 2 DG C 1 C4' - C3' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 DG C 1 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 DG C 1 N7 - C8 - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 DG C 1 C3' - O3' - P ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 DA C 2 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 2 DT C 3 O4' - C1' - N1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 DC C 6 C4' - C3' - C2' ANGL. DEV. = -5.3 DEGREES
REMARK 500 2 DC C 6 O4' - C1' - N1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 2 DG D 1 C4' - C3' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 DG D 1 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DG D 1 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 DA D 2 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 DT D 5 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 DC D 6 C4' - C3' - C2' ANGL. DEV. = -4.7 DEGREES
REMARK 500 2 DC D 6 O4' - C1' - N1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 3 VAL A 4 CG1 - CB - CG2 ANGL. DEV. = -14.4 DEGREES
REMARK 500 3 VAL A 4 CA - CB - CG1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 3 DG C 1 C4' - C3' - C2' ANGL. DEV. = -4.2 DEGREES
REMARK 500 3 DG C 1 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 DG C 1 N7 - C8 - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 DG C 1 C3' - O3' - P ANGL. DEV. = 8.7 DEGREES
REMARK 500 3 DT C 3 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 DA C 4 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 168 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 7 NCY A 3 58.02 -103.76
REMARK 500 7 NCY A 7 57.18 -105.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 QUI A 0
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF TRIOSTIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 185D RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF D(GACGTC) COMPLEXED WITH TRIOSTIN A
REMARK 900 RELATED ID: 193D RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF D(ACACGTGT) COMPLEXED WITH QUINOMYCIN UK-6305
REMARK 900 RELATED ID: 1PFE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(GCGTACG) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P6322
REMARK 900 RELATED ID: 1VS2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(GCGTACGC) COMPLEXED WITH TRIOSIN A
REMARK 900 RELATED ID: 1XVK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(GCGTACGC) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P632
REMARK 900 RELATED ID: 1XVN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(ACGTACGT) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P632
REMARK 900 RELATED ID: 1XVR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(CGTACG) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP C21
REMARK 900 RELATED ID: 2ADW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(ACGTACGT) COMPLEXED WITH ECHINOMYCIN - SPACE
REMARK 900 GROUP P42212
REMARK 900 RELATED ID: 3GO3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D(ACGTACGT) COMPLEXED WITH
DBREF 2DA8 A 1 8 NOR NOR01129 NOR01129 1 8
DBREF 2DA8 C 1 6 PDB 2DA8 2DA8 1 6
DBREF 2DA8 D 1 6 PDB 2DA8 2DA8 1 6
SEQADV 2DA8 VAL A 4 NOR NOR01129 MVA 4 ENGINEERED MUTATION
SEQADV 2DA8 VAL A 8 NOR NOR01129 MVA 8 ENGINEERED MUTATION
SEQRES 1 A 8 DSN ALA NCY VAL DSN ALA NCY VAL
SEQRES 1 C 6 DG DA DT DA DT DC
SEQRES 1 D 6 DG DA DT DA DT DC
HET DSN A 1 10
HET NCY A 3 13
HET DSN A 5 10
HET NCY A 7 13
HET QUI A 0 17
HET QUI A 9 17
HETNAM DSN D-SERINE
HETNAM NCY N-METHYLCYSTEINE
HETNAM QUI 2-CARBOXYQUINOXALINE
FORMUL 1 DSN 2(C3 H7 N O3)
FORMUL 1 NCY 2(C4 H9 N O2 S)
FORMUL 4 QUI 2(C9 H6 N2 O2)
SSBOND 1 NCY A 3 NCY A 7 1555 1555 2.02
LINK C QUI A 0 N DSN A 1 1555 1555 1.34
LINK C DSN A 1 N ALA A 2 1555 1555 1.31
LINK OG DSN A 1 C VAL A 8 1555 1555 1.33
LINK C ALA A 2 N NCY A 3 1555 1555 1.32
LINK C NCY A 3 N VAL A 4 1555 1555 1.31
LINK C VAL A 4 OG DSN A 5 1555 1555 1.33
LINK C DSN A 5 N ALA A 6 1555 1555 1.31
LINK N DSN A 5 C QUI A 9 1555 1555 1.34
LINK C ALA A 6 N NCY A 7 1555 1555 1.33
LINK C NCY A 7 N VAL A 8 1555 1555 1.31
SITE 1 AC1 8 DA C 2 DT C 3 DA C 4 DT C 5
SITE 2 AC1 8 DA D 2 DT D 3 DA D 4 DT D 5
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 - 1 20 Bytes