Header list of 1rpv.pdb file
Complete list - 2 20 Bytes
HEADER TRANSCRIPTION REGULATION PROTEIN 04-MAY-95 1RPV
TITLE HIV-1 REV PROTEIN (RESIDUES 34-50)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 REV PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (CLONE 12);
SOURCE 3 ORGANISM_TAXID: 11679
KEYWDS HUMAN IMMUNODEFICIENCY VIRUS-1, REV RESPONSE ELEMENT, TRANSCRIPTION
KEYWDS 2 REGULATION PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.J.SCANLON,D.P.FAIRLIE,D.J.CRAIK,D.R.ENGLEBRETSEN,M.L.WEST
REVDAT 3 02-MAR-22 1RPV 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1RPV 1 VERSN
REVDAT 1 15-OCT-95 1RPV 0
JRNL AUTH M.J.SCANLON,D.P.FAIRLIE,D.J.CRAIK,D.R.ENGLEBRETSEN,M.L.WEST
JRNL TITL NMR SOLUTION STRUCTURE OF THE RNA-BINDING PEPTIDE FROM HUMAN
JRNL TITL 2 IMMUNODEFICIENCY VIRUS (TYPE 1) REV.
JRNL REF BIOCHEMISTRY V. 34 8242 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7599117
JRNL DOI 10.1021/BI00026A005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.D.PETERSON,D.P.BARTEL,J.W.SZOSTAK,S.J.HORVATH,J.FEIGON
REMARK 1 TITL 1H NMR STUDIES OF THE HIGH-AFFINITY REV BINDING SITE OF THE
REMARK 1 TITL 2 REV RESPONSIVE ELEMENT OF HIV-1 MRNA: BASE PAIRING IN THE
REMARK 1 TITL 3 CORE BINDING ELEMENT
REMARK 1 REF BIOCHEMISTRY V. 33 5357 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.L.BATTISTE,R.TAN,A.D.FRANKEL,J.R.WILLIAMSON
REMARK 1 TITL BINDING OF AN HIV REV PEPTIDE TO REV RESPONSIVE ELEMENT RNA
REMARK 1 TITL 2 INDUCES FORMATION OF PURINE-PURINE BASE PAIRS
REMARK 1 REF BIOCHEMISTRY V. 33 2741 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.LECLERC,R.CEDERGREN,A.D.ELLINGTON
REMARK 1 TITL A THREE-DIMENSIONAL MODEL OF THE REV BINDING ELEMENT OF
REMARK 1 TITL 2 HIV-1 DERIVED FROM ANALYSES OF APTAMERS
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 293 1994
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 4
REMARK 1 AUTH R.TAN,L.CHEN,J.A.BUETTNER,D.HUDSON,A.D.FRANKEL
REMARK 1 TITL RNA RECOGNITION BY AN ISOLATED ALPHA HELIX
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 73 1031 1993
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 5
REMARK 1 AUTH T.J.DALY,K.S.COOK,G.S.GRAY,T.E.MAIONE,J.R.RUSCHE
REMARK 1 TITL SPECIFIC BINDING OF HIV-1 RECOMBINANT REV PROTEIN TO THE
REMARK 1 TITL 2 REV-RESPONSIVE ELEMENT IN VITRO
REMARK 1 REF NATURE V. 342 816 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RPV 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_1000176184.
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 : 20
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 8 ARG A 7 CD ARG A 7 NE 0.110
REMARK 500 8 ARG A 9 CD ARG A 9 NE 0.102
REMARK 500 8 ARG A 11 CD ARG A 11 NE 0.108
REMARK 500 8 ARG A 12 CD ARG A 12 NE 0.103
REMARK 500 8 ARG A 14 CD ARG A 14 NE 0.105
REMARK 500 8 ARG A 16 CD ARG A 16 NE 0.109
REMARK 500 14 ARG A 3 CD ARG A 3 NE 0.149
REMARK 500 14 ARG A 6 CD ARG A 6 NE 0.154
REMARK 500 14 ARG A 7 CD ARG A 7 NE 0.150
REMARK 500 14 ARG A 9 CD ARG A 9 NE 0.139
REMARK 500 14 ARG A 11 CD ARG A 11 NE 0.140
REMARK 500 14 ARG A 12 CD ARG A 12 NE 0.144
REMARK 500 14 ARG A 14 CD ARG A 14 NE 0.154
REMARK 500 14 ARG A 16 CD ARG A 16 NE 0.139
REMARK 500 14 ARG A 18 CD ARG A 18 NE 0.158
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 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 2 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 2 TRP A 13 NE1 - CE2 - CZ2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 3 ARG A 3 CD - NE - CZ ANGL. DEV. = -19.1 DEGREES
REMARK 500 3 ARG A 6 CD - NE - CZ ANGL. DEV. = -18.6 DEGREES
REMARK 500 3 ARG A 7 CD - NE - CZ ANGL. DEV. = -19.2 DEGREES
REMARK 500 3 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 9 CD - NE - CZ ANGL. DEV. = -18.9 DEGREES
REMARK 500 3 ARG A 11 CD - NE - CZ ANGL. DEV. = -19.0 DEGREES
REMARK 500 3 ARG A 12 CD - NE - CZ ANGL. DEV. = -17.4 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 3 TRP A 13 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 TRP A 13 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 3 ARG A 14 CD - NE - CZ ANGL. DEV. = -19.8 DEGREES
REMARK 500 3 ARG A 16 CD - NE - CZ ANGL. DEV. = -19.0 DEGREES
REMARK 500 3 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 ARG A 18 CD - NE - CZ ANGL. DEV. = -18.1 DEGREES
REMARK 500 3 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 4 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 4 TRP A 13 NE1 - CE2 - CZ2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 5 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 5 TRP A 13 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 6 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 7 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 7 TRP A 13 NE1 - CE2 - CZ2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 8 ARG A 3 CD - NE - CZ ANGL. DEV. = -18.1 DEGREES
REMARK 500 8 ARG A 6 CD - NE - CZ ANGL. DEV. = -18.4 DEGREES
REMARK 500 8 ARG A 6 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 8 ARG A 7 CD - NE - CZ ANGL. DEV. = -17.7 DEGREES
REMARK 500 8 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 8 ARG A 7 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 8 ARG A 9 CD - NE - CZ ANGL. DEV. = -18.8 DEGREES
REMARK 500 8 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 8 ARG A 11 CD - NE - CZ ANGL. DEV. = -18.9 DEGREES
REMARK 500 8 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 8 ARG A 12 CD - NE - CZ ANGL. DEV. = -18.6 DEGREES
REMARK 500 8 TRP A 13 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 8 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 8 TRP A 13 NE1 - CE2 - CZ2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 8 ARG A 14 CD - NE - CZ ANGL. DEV. = -18.2 DEGREES
REMARK 500 8 ARG A 16 CD - NE - CZ ANGL. DEV. = -19.2 DEGREES
REMARK 500 8 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 8 ARG A 18 CD - NE - CZ ANGL. DEV. = -18.4 DEGREES
REMARK 500 8 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 9 TRP A 13 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 9 TRP A 13 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 132 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 2 ALA A 5 57.52 -90.99
REMARK 500 3 ALA A 5 53.10 -95.99
REMARK 500 4 GLN A 4 63.52 -157.54
REMARK 500 4 ALA A 5 -80.78 -132.40
REMARK 500 4 GLN A 17 -66.64 -99.46
REMARK 500 5 GLN A 17 26.83 42.72
REMARK 500 7 GLN A 4 -55.11 -128.57
REMARK 500 8 GLN A 4 8.37 -156.38
REMARK 500 9 GLN A 17 24.43 42.95
REMARK 500 13 ALA A 5 31.22 -84.14
REMARK 500 14 GLN A 17 48.96 38.57
REMARK 500 17 ARG A 3 -34.33 -39.45
REMARK 500 19 ALA A 5 39.98 -86.03
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 3 ARG A 3 0.39 SIDE CHAIN
REMARK 500 3 ARG A 6 0.39 SIDE CHAIN
REMARK 500 3 ARG A 7 0.36 SIDE CHAIN
REMARK 500 3 ARG A 9 0.39 SIDE CHAIN
REMARK 500 3 ARG A 11 0.39 SIDE CHAIN
REMARK 500 3 ARG A 12 0.34 SIDE CHAIN
REMARK 500 3 ARG A 14 0.40 SIDE CHAIN
REMARK 500 3 ARG A 16 0.34 SIDE CHAIN
REMARK 500 3 ARG A 18 0.34 SIDE CHAIN
REMARK 500 8 ARG A 3 0.39 SIDE CHAIN
REMARK 500 8 ARG A 6 0.37 SIDE CHAIN
REMARK 500 8 ARG A 7 0.32 SIDE CHAIN
REMARK 500 8 ARG A 9 0.36 SIDE CHAIN
REMARK 500 8 ARG A 11 0.39 SIDE CHAIN
REMARK 500 8 ARG A 12 0.39 SIDE CHAIN
REMARK 500 8 ARG A 14 0.39 SIDE CHAIN
REMARK 500 8 ARG A 16 0.40 SIDE CHAIN
REMARK 500 8 ARG A 18 0.37 SIDE CHAIN
REMARK 500 10 ARG A 3 0.38 SIDE CHAIN
REMARK 500 10 ARG A 6 0.38 SIDE CHAIN
REMARK 500 10 ARG A 7 0.23 SIDE CHAIN
REMARK 500 10 ARG A 9 0.37 SIDE CHAIN
REMARK 500 10 ARG A 11 0.39 SIDE CHAIN
REMARK 500 10 ARG A 12 0.39 SIDE CHAIN
REMARK 500 10 ARG A 14 0.36 SIDE CHAIN
REMARK 500 10 ARG A 16 0.38 SIDE CHAIN
REMARK 500 10 ARG A 18 0.39 SIDE CHAIN
REMARK 500 14 ARG A 3 0.40 SIDE CHAIN
REMARK 500 14 ARG A 6 0.40 SIDE CHAIN
REMARK 500 14 ARG A 7 0.35 SIDE CHAIN
REMARK 500 14 ARG A 9 0.40 SIDE CHAIN
REMARK 500 14 ARG A 11 0.40 SIDE CHAIN
REMARK 500 14 ARG A 12 0.38 SIDE CHAIN
REMARK 500 14 ARG A 14 0.36 SIDE CHAIN
REMARK 500 14 ARG A 16 0.39 SIDE CHAIN
REMARK 500 14 ARG A 18 0.40 SIDE CHAIN
REMARK 500 19 ARG A 3 0.39 SIDE CHAIN
REMARK 500 19 ARG A 6 0.39 SIDE CHAIN
REMARK 500 19 ARG A 7 0.39 SIDE CHAIN
REMARK 500 19 ARG A 9 0.37 SIDE CHAIN
REMARK 500 19 ARG A 11 0.39 SIDE CHAIN
REMARK 500 19 ARG A 12 0.34 SIDE CHAIN
REMARK 500 19 ARG A 14 0.39 SIDE CHAIN
REMARK 500 19 ARG A 16 0.39 SIDE CHAIN
REMARK 500 19 ARG A 18 0.36 SIDE CHAIN
REMARK 500 20 ARG A 3 0.39 SIDE CHAIN
REMARK 500 20 ARG A 6 0.38 SIDE CHAIN
REMARK 500 20 ARG A 7 0.21 SIDE CHAIN
REMARK 500 20 ARG A 9 0.39 SIDE CHAIN
REMARK 500 20 ARG A 11 0.38 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 54 PLANE DEVIATIONS.
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 NH2 A 19
DBREF 1RPV A 2 18 UNP P12485 REV_HV1BN 35 51
SEQADV 1RPV ALA A 10 UNP P12485 ARG 43 CONFLICT
SEQRES 1 A 19 SIN THR ARG GLN ALA ARG ARG ASN ARG ALA ARG ARG TRP
SEQRES 2 A 19 ARG ALA ARG GLN ARG NH2
HET SIN A 1 11
HET NH2 A 19 3
HETNAM SIN SUCCINIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 SIN C4 H6 O4
FORMUL 1 NH2 H2 N
HELIX 1 1 ALA A 5 ARG A 16 1 12
LINK C1 SIN A 1 N THR A 2 1555 1555 1.31
LINK C ARG A 18 N NH2 A 19 1555 1555 1.30
SITE 1 AC1 1 ARG A 18
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