Header list of 1nk3.pdb file
Complete list - 23 20 Bytes
HEADER DNA BINDING PROTEIN/DNA 06-MAY-98 1NK3
TITLE VND/NK-2 HOMEODOMAIN/DNA COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*TP*GP*TP*GP*TP*CP*AP*AP*GP*TP*GP*GP*CP*TP*GP*T)-
COMPND 3 3');
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(*AP*CP*AP*GP*CP*CP*AP*CP*TP*TP*GP*AP*CP*AP*CP*A)-
COMPND 8 3');
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HOMEOBOX PROTEIN VND;
COMPND 13 CHAIN: P;
COMPND 14 FRAGMENT: HOMEODOMAIN;
COMPND 15 SYNONYM: VND/NK-2 HOMEODOMAIN, VENTRAL NERVOUS SYSTEM DEFECTIVE
COMPND 16 PROTEIN, HOMEOBOX PROTEIN NK-2;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 7 ORGANISM_COMMON: FRUIT FLY;
SOURCE 8 ORGANISM_TAXID: 7227;
SOURCE 9 ORGAN: FRUIT;
SOURCE 10 GENE: POTENTIAL;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS HOMEODOMAIN, HOMEOBOX, DNA-BINDING PROTEIN, EMBRYONIC DEVELOPMENT,
KEYWDS 2 COMPLEX (HOMEODOMAIN-DNA), DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
AUTHOR J.M.GRUSCHUS,D.H.H.TSAO,L.-H.WANG,M.NIRENBERG,J.A.FERRETTI
REVDAT 4 23-FEB-22 1NK3 1 REMARK
REVDAT 3 24-FEB-09 1NK3 1 VERSN
REVDAT 2 23-FEB-99 1NK3 3 COMPND REMARK TITLE DBREF
REVDAT 2 2 3 HEADER TER ATOM SEQRES
REVDAT 2 3 3 JRNL KEYWDS HELIX
REVDAT 1 09-DEC-98 1NK3 0
JRNL AUTH J.M.GRUSCHUS,D.H.TSAO,L.H.WANG,M.NIRENBERG,J.A.FERRETTI
JRNL TITL INTERACTIONS OF THE VND/NK-2 HOMEODOMAIN WITH DNA BY NUCLEAR
JRNL TITL 2 MAGNETIC RESONANCE SPECTROSCOPY: BASIS OF BINDING
JRNL TITL 3 SPECIFICITY.
JRNL REF BIOCHEMISTRY V. 36 5372 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9154919
JRNL DOI 10.1021/BI9620060
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.M.GRUSCHUS,D.H.TSAO,L.H.WANG,M.NIRENBERG,J.A.FERRETTI
REMARK 1 TITL INTERACTIONS OF THE VND/NK-2 HOMEODOMAIN WITH DNA BY NUCLEAR
REMARK 1 TITL 2 MAGNETIC RESONANCE SPECTROSCOPY: BASIS OF BINDING
REMARK 1 TITL 3 SPECIFICITY
REMARK 1 REF BIOCHEMISTRY V. 36 5372 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.H.TSAO,J.M.GRUSCHUS,L.H.WANG,M.NIRENBERG,J.A.FERRETTI
REMARK 1 TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE NK-2
REMARK 1 TITL 2 HOMEODOMAIN FROM DROSOPHILA
REMARK 1 REF J.MOL.BIOL. V. 251 297 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.H.TSAO,J.M.GRUSCHUS,L.H.WANG,M.NIRENBERG,J.A.FERRETTI
REMARK 1 TITL ELONGATION OF HELIX III OF THE NK-2 HOMEODOMAIN UPON BINDING
REMARK 1 TITL 2 TO DNA: A SECONDARY STRUCTURE STUDY BY NMR
REMARK 1 REF BIOCHEMISTRY V. 33 15053 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INSIGHT II 97 AUTHOR : MSI MSI
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NMR REFINE/INSIGHT II 97
REMARK 4
REMARK 4 1NK3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175317.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 60MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED 3D NOESY H2O; 13C
REMARK 210 -EDITED 3D NOESY D2O; 12C-
REMARK 210 FILTERED 2D NOESY D2O; 1-1
REMARK 210 SEMISELECTIVE 2D NOESY H2O;
REMARK 210 DEUTERIUM EXCHANGE 15N 2D HMQC
REMARK 210 H2O; QUANTITATIVE HN-HALPHA J-
REMARK 210 COUPLING
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMR REFINE REFINE
REMARK 210 METHOD USED : DISTANCE GEOMETRY/ SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS MODEL IS THE AVERAGE STRUCTURE OF THE ENSEMBLE OF 20
REMARK 210 STRUCTURES (1NK2). THE UNSTRUCTURED N-TERMINAL AND C-TERMINAL
REMARK 210 AMINO ACIDS (P 101-P 107 AND P 171-P 177 IN PDB ENTRY 1NK2) WERE
REMARK 210 REMOVED PRIOR TO MINIMIZATION OF THE AVERAGE STRUCTURE BY THE MD_
REMARK 210 SCHE DULE PROGRAM OF INSIGHTII/NMR REFINE, SUBJECT TO ALL
REMARK 210 EXPERIMENTAL RESTRAINTS FOR THE DNA AND REMAINING PROTEIN
REMARK 210 RESIDUES. THE REMAINING PROTEIN RESIDUES ARE RENUMBERED STARTING
REMARK 210 WITH P 100 SO THAT THE RESIDUE NUMBERING FOLLOWS THE STANDARD,
REMARK 210 CANONICAL NUMBER ING SCHEME FOR HOMEODOMAINS.
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P
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 RES C SSSEQI
REMARK 465 ALA P 93
REMARK 465 SER P 94
REMARK 465 ASP P 95
REMARK 465 GLY P 96
REMARK 465 LEU P 97
REMARK 465 PRO P 98
REMARK 465 ASN P 99
REMARK 465 LYS P 163
REMARK 465 GLY P 164
REMARK 465 TYR P 165
REMARK 465 GLU P 166
REMARK 465 GLY P 167
REMARK 465 HIS P 168
REMARK 465 PRO P 169
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 H2' DG A 15 H71 DT A 16 1.05
REMARK 500 H2'' DC B 24 H5'' DT B 25 1.29
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 DT A 1 C2' DT A 1 C1' 0.060
REMARK 500 DG A 9 C6 DG A 9 N1 0.046
REMARK 500 DG A 11 C6 DG A 11 N1 0.046
REMARK 500 DC A 13 C4 DC A 13 C5 0.049
REMARK 500 DG A 15 C6 DG A 15 N1 0.042
REMARK 500 DC B 18 C4 DC B 18 C5 0.049
REMARK 500 DA B 32 O3' DA B 32 C3' -0.038
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 DT A 1 O4' - C4' - C3' ANGL. DEV. = -2.6 DEGREES
REMARK 500 DT A 1 C3' - O3' - P ANGL. DEV. = 10.8 DEGREES
REMARK 500 DG A 2 C5 - C6 - N1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 DG A 2 N1 - C6 - O6 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DT A 3 P - O5' - C5' ANGL. DEV. = -16.9 DEGREES
REMARK 500 DG A 4 C5 - C6 - N1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DG A 4 C6 - C5 - N7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 DG A 4 N1 - C6 - O6 ANGL. DEV. = 5.8 DEGREES
REMARK 500 DT A 5 N3 - C4 - O4 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT A 5 C4 - C5 - C7 ANGL. DEV. = -4.1 DEGREES
REMARK 500 DC A 6 C2 - N3 - C4 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DA A 8 P - O5' - C5' ANGL. DEV. = -12.3 DEGREES
REMARK 500 DA A 8 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DA A 8 C6 - N1 - C2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DA A 8 C2 - N3 - C4 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DA A 8 C5 - C6 - N6 ANGL. DEV. = 5.3 DEGREES
REMARK 500 DG A 9 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG A 9 C5 - C6 - N1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DG A 9 N1 - C6 - O6 ANGL. DEV. = 5.6 DEGREES
REMARK 500 DG A 9 C8 - N9 - C1' ANGL. DEV. = 8.5 DEGREES
REMARK 500 DG A 9 C4 - N9 - C1' ANGL. DEV. = -8.0 DEGREES
REMARK 500 DG A 11 C5 - C6 - N1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DG A 11 N1 - C6 - O6 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DG A 12 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG A 12 C5 - C6 - N1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 DG A 12 N1 - C6 - O6 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DC A 13 C4 - C5 - C6 ANGL. DEV. = -3.4 DEGREES
REMARK 500 DG A 15 O4' - C1' - N9 ANGL. DEV. = -6.6 DEGREES
REMARK 500 DG A 15 C5 - C6 - N1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DG A 15 N1 - C6 - O6 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DT A 16 O4' - C4' - C3' ANGL. DEV. = -4.3 DEGREES
REMARK 500 DT A 16 C4 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 DT A 16 C6 - C5 - C7 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DA B 17 O4' - C1' - N9 ANGL. DEV. = -5.0 DEGREES
REMARK 500 DA B 17 C3' - O3' - P ANGL. DEV. = 7.8 DEGREES
REMARK 500 DA B 19 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG B 20 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG B 20 C5 - C6 - N1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DG B 20 N1 - C6 - O6 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC B 21 C2 - N3 - C4 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC B 21 C3' - O3' - P ANGL. DEV. = 8.6 DEGREES
REMARK 500 DA B 23 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DA B 23 C6 - N1 - C2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DC B 24 C6 - N1 - C2 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC B 24 C2 - N1 - C1' ANGL. DEV. = -8.0 DEGREES
REMARK 500 DT B 25 N3 - C4 - O4 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DT B 26 N3 - C4 - O4 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DT B 26 C4 - C5 - C7 ANGL. DEV. = -5.5 DEGREES
REMARK 500 DT B 26 C6 - C5 - C7 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DG B 27 C5 - C6 - N1 ANGL. DEV. = -3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 63 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 ARG P 102 51.16 -92.36
REMARK 500 LYS P 103 66.82 31.84
REMARK 500 ARG P 139 22.87 85.47
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 DG A 4 0.06 SIDE CHAIN
REMARK 500 DG A 9 0.06 SIDE CHAIN
REMARK 500 DT B 26 0.12 SIDE CHAIN
REMARK 500 DA B 28 0.09 SIDE CHAIN
REMARK 500 PHE P 149 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NK2 RELATED DB: PDB
REMARK 900 ENSEMBLE OF 20 STRUCTURES
DBREF 1NK3 P 100 162 UNP P22808 VND_DROME 68 130
DBREF 1NK3 A 1 16 PDB 1NK3 1NK3 1 16
DBREF 1NK3 B 17 32 PDB 1NK3 1NK3 17 32
SEQRES 1 A 16 DT DG DT DG DT DC DA DA DG DT DG DG DC
SEQRES 2 A 16 DT DG DT
SEQRES 1 B 16 DA DC DA DG DC DC DA DC DT DT DG DA DC
SEQRES 2 B 16 DA DC DA
SEQRES 1 P 77 ALA SER ASP GLY LEU PRO ASN LYS LYS ARG LYS ARG ARG
SEQRES 2 P 77 VAL LEU PHE THR LYS ALA GLN THR TYR GLU LEU GLU ARG
SEQRES 3 P 77 ARG PHE ARG GLN GLN ARG TYR LEU SER ALA PRO GLU ARG
SEQRES 4 P 77 GLU HIS LEU ALA SER LEU ILE ARG LEU THR PRO THR GLN
SEQRES 5 P 77 VAL LYS ILE TRP PHE GLN ASN HIS ARG TYR LYS THR LYS
SEQRES 6 P 77 ARG ALA GLN ASN GLU LYS GLY TYR GLU GLY HIS PRO
HELIX 1 I LYS P 110 GLN P 122 1 13
HELIX 2 II ALA P 128 ILE P 138 1 11
HELIX 3 III PRO P 142 GLU P 162 1 21
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
Complete list - 23 20 Bytes