Header list of 1bal.pdb file
Complete list - b 16 2 Bytes
HEADER GLYCOLYSIS 20-FEB-92 1BAL
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE
TITLE 2 DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM THE 2-OXOGLUTARATE
TITLE 3 DEHYDROGENASE MULTIENZYME COMPLEX OF (ESCHERICHIA COLI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.1.61;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS GLYCOLYSIS
EXPDTA SOLUTION NMR
NUMMDL 56
AUTHOR G.M.CLORE,M.A.ROBIEN,A.M.GRONENBORN
REVDAT 4 16-FEB-22 1BAL 1 REMARK
REVDAT 3 24-FEB-09 1BAL 1 VERSN
REVDAT 2 01-APR-03 1BAL 1 JRNL
REVDAT 1 31-JAN-94 1BAL 0
JRNL AUTH M.A.ROBIEN,G.M.CLORE,J.G.OMICHINSKI,R.N.PERHAM,E.APPELLA,
JRNL AUTH 2 K.SAKAGUCHI,A.M.GRONENBORN
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING
JRNL TITL 2 DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM
JRNL TITL 3 THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF
JRNL TITL 4 ESCHERICHIA COLI.
JRNL REF BIOCHEMISTRY V. 31 3463 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1554728
JRNL DOI 10.1021/BI00128A021
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:
REMARK 3 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL
REMARK 3 STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS
REMARK 3 ABOVE. THE STRUCTURES ARE BASED ON 630 INTERPROTON
REMARK 3 DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; AND 46
REMARK 3 PHI AND 35 PSI BACKBONE TORSION ANGLE RESTRAINTS AND 20
REMARK 3 CHI1 SIDE CHAIN TORSION ANGLE RESTRAINTS DERIVED FROM
REMARK 3 COUPLING CONSTANTS AND NOE DATA. THE LATTER ARE OBTAINED
REMARK 3 USING THE CONFORMATIONAL GRID SEARCH PROGRAM STEREOSEARCH
REMARK 3 (M.NILGES,G.M.CLORE,A.M.GRONENBORN (1990) BIOPOLYMERS
REMARK 3 29, 813-822). THE METHOD USED TO DETERMINE THE STRUCTURES
REMARK 3 IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL
REMARK 3 SIMULATED ANNEALING METHOD (M.NILGES,G.M.CLORE,
REMARK 3 A.M.GRONENBORN, FEBS LETT. 229, 317-324 (1988)).
REMARK 3
REMARK 3 THIS ENTRY CONTAINS THE COORDINATES OF 56 INDIVIDUAL
REMARK 3 SIMULATED ANNEALING STRUCTURES. THE COORDINATES OF THE
REMARK 3 (SA)R MINIMIZED AVERAGE STRUCTURE ARE PRESENTED IN PROTEIN
REMARK 3 DATA BANK ENTRY 1BBL. (SA)R RESTRAINED MINIMIZED MEAN
REMARK 3 STRUCTURE WAS DERIVED BY AVERAGING THE COORDINATES OF THE
REMARK 3 INDIVIDUAL SA STRUCTURES BEST FITTED TO RESIDUES 14 - 30
REMARK 3 AND 39 - 47, AND SUBJECTING THE RESULTING COORDINATES TO
REMARK 3 RESTRAINED MINIMIZATION. RESIDUES 1 - 11 AND 48 - 51 ARE
REMARK 3 COMPLETELY DISORDERED AND ARE NOT INCLUDED IN THE
REMARK 3 COORDINATE SET.
REMARK 3
REMARK 3 THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF ENTRY 1BBL HAS
REMARK 3 NO MEANING. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF
REMARK 3 THIS ENTRY REPRESENTS THE ATOMIC RMS DEVIATIONS OF THE 56
REMARK 3 INDIVIDUAL STRUCTURES ABOUT THE MEAN STRUCTURE.
REMARK 3
REMARK 3 ALL THE INTERPROTON DISTANCE AND TORSION ANGLE RESTRAINTS
REMARK 3 ARE PRESENTED IN PROTEIN DATA BANK ENTRY R1BBLMR.
REMARK 4
REMARK 4 1BAL 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_1000171530.
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 : 56
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: 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
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 23 CG HIS A 23 ND1 -0.115
REMARK 500 1 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 2 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 2 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 3 HIS A 23 CG HIS A 23 ND1 -0.114
REMARK 500 3 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 4 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 4 HIS A 47 CG HIS A 47 ND1 -0.114
REMARK 500 5 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 5 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 6 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 6 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 7 HIS A 23 CG HIS A 23 ND1 -0.114
REMARK 500 7 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 8 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 8 HIS A 47 CG HIS A 47 ND1 -0.114
REMARK 500 9 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 9 HIS A 47 CG HIS A 47 ND1 -0.114
REMARK 500 10 HIS A 23 CG HIS A 23 ND1 -0.114
REMARK 500 10 HIS A 47 CG HIS A 47 ND1 -0.117
REMARK 500 11 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 11 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 12 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 12 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 13 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 13 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 14 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 14 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 15 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 15 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 16 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 16 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 17 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 17 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 18 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 18 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 19 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 19 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 20 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 20 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 21 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 21 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 22 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 22 HIS A 47 CG HIS A 47 ND1 -0.113
REMARK 500 23 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 23 HIS A 47 CG HIS A 47 ND1 -0.116
REMARK 500 24 HIS A 23 CG HIS A 23 ND1 -0.115
REMARK 500 24 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500 25 HIS A 23 CG HIS A 23 ND1 -0.116
REMARK 500 25 HIS A 47 CG HIS A 47 ND1 -0.115
REMARK 500
REMARK 500 THIS ENTRY HAS 112 BOND 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 SER A 3 -154.43 -151.62
REMARK 500 1 ASN A 8 -124.90 -79.64
REMARK 500 1 ASN A 9 153.94 -46.77
REMARK 500 1 ASP A 10 -114.96 -101.24
REMARK 500 1 ALA A 11 -130.55 -165.83
REMARK 500 1 THR A 33 35.36 -87.70
REMARK 500 1 LYS A 46 44.35 -77.26
REMARK 500 1 HIS A 47 -43.24 -149.70
REMARK 500 1 LEU A 48 -121.12 -73.70
REMARK 500 1 ALA A 49 -149.31 -148.76
REMARK 500 2 SER A 3 28.39 -145.79
REMARK 500 2 ASN A 8 -139.70 -76.25
REMARK 500 2 ASN A 9 67.16 -167.70
REMARK 500 2 ASP A 10 -106.45 -57.55
REMARK 500 2 ALA A 11 -74.37 -136.02
REMARK 500 2 THR A 40 -149.54 -148.21
REMARK 500 2 ASP A 43 -48.00 -130.30
REMARK 500 3 ALA A 2 -116.93 -129.13
REMARK 500 3 SER A 3 179.60 -58.95
REMARK 500 3 GLU A 5 10.21 -145.29
REMARK 500 3 ASN A 8 -81.65 -60.65
REMARK 500 3 ASN A 9 -74.17 -170.81
REMARK 500 3 ASP A 10 -149.64 -156.20
REMARK 500 3 ALA A 11 -77.26 -68.05
REMARK 500 3 LEU A 12 -158.00 -58.43
REMARK 500 3 LEU A 19 -7.70 -55.25
REMARK 500 3 THR A 33 -67.98 -143.99
REMARK 500 3 LEU A 48 43.69 -78.24
REMARK 500 4 SER A 3 -15.86 -150.02
REMARK 500 4 GLU A 6 -15.14 -142.32
REMARK 500 4 GLN A 7 93.49 -57.76
REMARK 500 4 ASN A 9 36.31 -79.87
REMARK 500 4 ALA A 11 -71.79 -77.15
REMARK 500 4 ALA A 15 -15.73 -49.59
REMARK 500 4 ASN A 24 93.40 56.56
REMARK 500 4 ASP A 26 97.37 -56.10
REMARK 500 4 ALA A 27 0.24 -62.34
REMARK 500 4 THR A 33 45.52 -93.20
REMARK 500 4 GLU A 42 -6.40 -57.45
REMARK 500 4 LYS A 46 39.37 -76.48
REMARK 500 4 HIS A 47 -35.30 -145.12
REMARK 500 4 LEU A 48 -74.66 -88.63
REMARK 500 4 ALA A 49 135.32 -177.09
REMARK 500 4 LYS A 50 -173.58 -60.52
REMARK 500 5 SER A 3 -136.12 -98.12
REMARK 500 5 GLU A 5 92.59 -43.35
REMARK 500 5 ASN A 8 -14.04 -150.43
REMARK 500 5 ASN A 9 178.23 53.14
REMARK 500 5 PRO A 14 0.57 -63.61
REMARK 500 5 ILE A 16 -13.36 -47.18
REMARK 500
REMARK 500 THIS ENTRY HAS 528 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 17 0.31 SIDE CHAIN
REMARK 500 1 ARG A 18 0.23 SIDE CHAIN
REMARK 500 1 ARG A 38 0.29 SIDE CHAIN
REMARK 500 1 ARG A 41 0.31 SIDE CHAIN
REMARK 500 2 ARG A 17 0.23 SIDE CHAIN
REMARK 500 2 ARG A 18 0.32 SIDE CHAIN
REMARK 500 2 ARG A 38 0.18 SIDE CHAIN
REMARK 500 2 ARG A 41 0.25 SIDE CHAIN
REMARK 500 3 ARG A 17 0.24 SIDE CHAIN
REMARK 500 3 ARG A 18 0.18 SIDE CHAIN
REMARK 500 3 ARG A 38 0.28 SIDE CHAIN
REMARK 500 3 ARG A 41 0.21 SIDE CHAIN
REMARK 500 4 ARG A 17 0.28 SIDE CHAIN
REMARK 500 4 ARG A 18 0.32 SIDE CHAIN
REMARK 500 4 ARG A 38 0.22 SIDE CHAIN
REMARK 500 4 ARG A 41 0.19 SIDE CHAIN
REMARK 500 5 ARG A 17 0.28 SIDE CHAIN
REMARK 500 5 ARG A 18 0.30 SIDE CHAIN
REMARK 500 5 ARG A 38 0.20 SIDE CHAIN
REMARK 500 5 ARG A 41 0.17 SIDE CHAIN
REMARK 500 6 ARG A 17 0.32 SIDE CHAIN
REMARK 500 6 ARG A 18 0.32 SIDE CHAIN
REMARK 500 6 ARG A 38 0.26 SIDE CHAIN
REMARK 500 6 ARG A 41 0.28 SIDE CHAIN
REMARK 500 7 ARG A 17 0.21 SIDE CHAIN
REMARK 500 7 ARG A 18 0.28 SIDE CHAIN
REMARK 500 7 ARG A 41 0.28 SIDE CHAIN
REMARK 500 8 ARG A 17 0.09 SIDE CHAIN
REMARK 500 8 ARG A 18 0.23 SIDE CHAIN
REMARK 500 8 ARG A 38 0.32 SIDE CHAIN
REMARK 500 8 ARG A 41 0.29 SIDE CHAIN
REMARK 500 9 ARG A 17 0.09 SIDE CHAIN
REMARK 500 9 ARG A 38 0.28 SIDE CHAIN
REMARK 500 9 ARG A 41 0.24 SIDE CHAIN
REMARK 500 10 ARG A 17 0.27 SIDE CHAIN
REMARK 500 10 ARG A 38 0.32 SIDE CHAIN
REMARK 500 10 ARG A 41 0.32 SIDE CHAIN
REMARK 500 11 ARG A 17 0.32 SIDE CHAIN
REMARK 500 11 ARG A 18 0.32 SIDE CHAIN
REMARK 500 11 ARG A 38 0.19 SIDE CHAIN
REMARK 500 11 ARG A 41 0.27 SIDE CHAIN
REMARK 500 12 ARG A 17 0.29 SIDE CHAIN
REMARK 500 12 ARG A 18 0.25 SIDE CHAIN
REMARK 500 12 ARG A 38 0.31 SIDE CHAIN
REMARK 500 12 ARG A 41 0.10 SIDE CHAIN
REMARK 500 13 ARG A 17 0.30 SIDE CHAIN
REMARK 500 13 ARG A 18 0.32 SIDE CHAIN
REMARK 500 13 ARG A 38 0.21 SIDE CHAIN
REMARK 500 13 ARG A 41 0.32 SIDE CHAIN
REMARK 500 14 ARG A 17 0.17 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 207 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BBL RELATED DB: PDB
DBREF 1BAL A 2 51 UNP P07016 ODO2_ECOLI 103 152
SEQRES 1 A 51 TYR ALA SER LEU GLU GLU GLN ASN ASN ASP ALA LEU SER
SEQRES 2 A 51 PRO ALA ILE ARG ARG LEU LEU ALA GLU HIS ASN LEU ASP
SEQRES 3 A 51 ALA SER ALA ILE LYS GLY THR GLY VAL GLY GLY ARG LEU
SEQRES 4 A 51 THR ARG GLU ASP VAL GLU LYS HIS LEU ALA LYS ALA
HELIX 1 1 SER A 13 ARG A 17 5 5
HELIX 2 2 ARG A 18 HIS A 23 1 6
HELIX 3 3 THR A 40 GLU A 45 1 6
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