Header list of 1gxi.pdb file
Complete list - n 17 2 Bytes
HEADER PHOTOSYNTHESIS 05-APR-02 1GXI
TITLE PSAE SUBUNIT OF THE PHOTOSYSTEM I OF THE CYANOBACTERIUM SYNECHOCYSTIS
TITLE 2 SP. PCC 6803
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IV;
COMPND 3 CHAIN: E;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, PSAE SUBUNIT, RESIDUES 1-73
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803
KEYWDS PHOTOSYNTHESIS, PHOTOSYSTEM I, PSAE SUB-UNIT, THYLAKOID
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR P.BARTH,P.SAVARIN,B.GILQUIN,B.LAGOUTTE,F.OCHSENBEIN
REVDAT 3 17-JAN-18 1GXI 1 TITLE COMPND JRNL
REVDAT 2 24-FEB-09 1GXI 1 VERSN
REVDAT 1 04-APR-03 1GXI 0
JRNL AUTH P.BARTH,P.SAVARIN,B.GILQUIN,B.LAGOUTTE,F.OCHSENBEIN
JRNL TITL SOLUTION NMR STRUCTURE AND BACKBONE DYNAMICS OF THE PSAE
JRNL TITL 2 SUBUNIT OF PHOTOSYETM I FROM SYNECHOCYSTIS SP. PCC 6803
JRNL REF BIOCHEMISTRY V. 41 13902 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12437347
JRNL DOI 10.1021/BI0259599
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.BARTH,I.GUILLOUARD,P.SETIF
REMARK 1 TITL ESSENTIAL ROLE OF A SINGLE ARGININE OF PHOTOSYSTEM I IN
REMARK 1 TITL 2 STABILIZING THE ELECTRON TRANSFER COMPLEX WITH FERREDOXIN
REMARK 1 REF J.BIOL.CHEM. V. 275 7030 2000
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 10702267
REMARK 1 DOI 10.1074/JBC.275.10.7030
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.L.MAYER,G.SHEN,D.BRYANT,J.LECOMTE,C.J.FALZONE
REMARK 1 TITL THE SOLUTION STRUCTURE OF PHOTOSYSTEM I ACCESSORY PROTEIN E
REMARK 1 TITL 2 FROM THE CYANOBACTERIUM NOSTOC SP. STRAIN PCC 8009
REMARK 1 REF BIOCHEMISTRY V. 38 13736 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 10521281
REMARK 1 DOI 10.1021/BI9910373
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER STRUCTURAL STATISTICS: 14 SA STRUCTURES
REMARK 3 SAAVEMIN RMS DEVIATIONS FROM EXP. RESTRAINTS[A]
REMARK 3 NOE DISTANCE RESTRAINTS (1430) NULL NULL DIHEDRAL
REMARK 3 ANGLE RESTRAINTS (130) NULL NULL DEVIATIONS FROM
REMARK 3 IDEAL GEOMETRY BONDS 0.017 A NULL ANGLES 30.0 DEG
REMARK 3 NULL IMPROPERS 2.3 DEG NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GXI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1290009661.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; HMQC-COSY; TOCSY; NOESY;
REMARK 210 NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER XWINNMR XWINNMR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST 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: E
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 400
REMARK 400 COMPOUND
REMARK 400 STABILIZES THE INTERACTION BETWEEN PSAC AND THE PSI
REMARK 400 CORE, ASSISTS THE DOCKING OF THE FERREDOXIN TO PSI AND
REMARK 400 INTERACTS WITH FERREDOXIN-NADP OXIDOREDUCTASE
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 HG SER E 26 O PRO E 35 1.60
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 ARG E 12 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 2 ARG E 4 NE - CZ - NH1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 2 ARG E 4 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 2 ARG E 9 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 ARG E 12 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 ARG E 9 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 ARG E 12 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 3 ARG E 12 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 3 ARG E 39 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG E 39 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 TYR E 45 C - N - CA ANGL. DEV. = 19.2 DEGREES
REMARK 500 3 SER E 53 C - N - CA ANGL. DEV. = 16.1 DEGREES
REMARK 500 4 ARG E 4 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 ARG E 4 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 4 ASP E 6 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 4 ASP E 6 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 4 ARG E 9 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 4 ARG E 9 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 4 PHE E 40 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 4 ARG E 42 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 4 GLU E 62 C - N - CA ANGL. DEV. = 16.4 DEGREES
REMARK 500 5 ASP E 6 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 5 ASP E 6 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 ARG E 9 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 5 ARG E 9 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 5 ARG E 12 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ARG E 39 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 5 ARG E 39 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 6 ARG E 4 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 6 ARG E 9 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 6 ARG E 12 NE - CZ - NH1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 6 ARG E 39 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 6 ARG E 39 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 6 GLY E 54 C - N - CA ANGL. DEV. = 14.5 DEGREES
REMARK 500 6 LEU E 65 CB - CG - CD2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 7 ARG E 4 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 7 ARG E 9 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 7 ARG E 12 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ARG E 39 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 7 ARG E 39 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 7 ARG E 42 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 8 ARG E 4 NH1 - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 8 ARG E 4 NE - CZ - NH1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 8 ARG E 12 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 8 TYR E 16 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 8 TYR E 16 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 8 ARG E 42 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 8 ARG E 42 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 8 GLU E 62 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 8 LEU E 65 CB - CG - CD2 ANGL. DEV. = 12.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 97 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 ASP E 6 47.98 -81.63
REMARK 500 1 LYS E 7 97.33 -11.91
REMARK 500 1 ILE E 10 104.22 -53.83
REMARK 500 1 ARG E 12 -72.91 -72.75
REMARK 500 1 THR E 13 -61.92 127.44
REMARK 500 1 ALA E 25 45.12 -85.31
REMARK 500 1 VAL E 27 28.98 -79.88
REMARK 500 1 SER E 30 35.08 -88.54
REMARK 500 1 ILE E 32 -157.64 -133.94
REMARK 500 1 ARG E 42 75.07 -115.59
REMARK 500 1 ASN E 44 72.70 47.68
REMARK 500 1 TYR E 45 36.45 -56.24
REMARK 500 1 ASN E 46 76.35 -101.69
REMARK 500 1 SER E 53 37.94 -141.68
REMARK 500 1 GLU E 62 -29.18 -19.94
REMARK 500 1 VAL E 68 -40.83 -132.70
REMARK 500 2 LEU E 2 -157.83 -96.73
REMARK 500 2 ILE E 10 108.95 -52.18
REMARK 500 2 GLU E 14 48.75 -66.07
REMARK 500 2 VAL E 24 85.29 -68.79
REMARK 500 2 ALA E 25 50.00 -88.96
REMARK 500 2 SER E 26 -71.80 -94.71
REMARK 500 2 GLU E 28 -45.62 -141.82
REMARK 500 2 SER E 30 53.36 -69.87
REMARK 500 2 ILE E 32 -153.13 -140.15
REMARK 500 2 ARG E 42 60.56 -115.35
REMARK 500 2 TYR E 45 -8.33 -50.42
REMARK 500 2 SER E 51 -156.68 76.36
REMARK 500 2 ALA E 52 -105.64 -96.59
REMARK 500 2 SER E 53 43.73 -68.51
REMARK 500 2 GLU E 62 -26.95 -27.27
REMARK 500 2 ALA E 70 63.85 -69.27
REMARK 500 3 LEU E 2 -156.51 -94.49
REMARK 500 3 GLU E 28 -67.09 -162.81
REMARK 500 3 ILE E 32 -159.33 -130.94
REMARK 500 3 ASN E 44 45.42 -79.16
REMARK 500 3 TYR E 45 -18.60 9.85
REMARK 500 3 ASN E 46 40.79 -76.28
REMARK 500 3 SER E 53 -25.80 41.95
REMARK 500 3 GLU E 62 -17.94 -25.66
REMARK 500 3 ALA E 70 56.36 -104.73
REMARK 500 4 LEU E 2 -154.86 -99.69
REMARK 500 4 GLU E 14 44.01 -74.72
REMARK 500 4 VAL E 24 73.99 -62.32
REMARK 500 4 ALA E 25 25.65 -79.96
REMARK 500 4 GLU E 28 -56.93 -169.34
REMARK 500 4 SER E 30 -41.12 -27.22
REMARK 500 4 ILE E 32 -167.24 -116.78
REMARK 500 4 ASP E 41 38.02 -88.53
REMARK 500 4 ARG E 42 36.13 -96.08
REMARK 500
REMARK 500 THIS ENTRY HAS 180 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 E 12 0.09 SIDE CHAIN
REMARK 500 1 TYR E 18 0.10 SIDE CHAIN
REMARK 500 1 PHE E 40 0.10 SIDE CHAIN
REMARK 500 2 ARG E 4 0.08 SIDE CHAIN
REMARK 500 2 ARG E 12 0.08 SIDE CHAIN
REMARK 500 2 PHE E 40 0.09 SIDE CHAIN
REMARK 500 2 ARG E 42 0.08 SIDE CHAIN
REMARK 500 3 ARG E 4 0.11 SIDE CHAIN
REMARK 500 3 ARG E 39 0.10 SIDE CHAIN
REMARK 500 3 PHE E 40 0.11 SIDE CHAIN
REMARK 500 3 ARG E 42 0.08 SIDE CHAIN
REMARK 500 4 ARG E 12 0.10 SIDE CHAIN
REMARK 500 4 ARG E 39 0.08 SIDE CHAIN
REMARK 500 5 ARG E 4 0.17 SIDE CHAIN
REMARK 500 5 ARG E 12 0.15 SIDE CHAIN
REMARK 500 5 PHE E 40 0.09 SIDE CHAIN
REMARK 500 5 ARG E 42 0.09 SIDE CHAIN
REMARK 500 6 ARG E 4 0.10 SIDE CHAIN
REMARK 500 6 ARG E 12 0.17 SIDE CHAIN
REMARK 500 6 ARG E 39 0.08 SIDE CHAIN
REMARK 500 7 ARG E 39 0.14 SIDE CHAIN
REMARK 500 7 PHE E 40 0.13 SIDE CHAIN
REMARK 500 8 ARG E 9 0.08 SIDE CHAIN
REMARK 500 8 ARG E 39 0.09 SIDE CHAIN
REMARK 500 8 PHE E 40 0.12 SIDE CHAIN
REMARK 500 8 TYR E 45 0.08 SIDE CHAIN
REMARK 500 8 PHE E 60 0.10 SIDE CHAIN
REMARK 500 11 ARG E 4 0.12 SIDE CHAIN
REMARK 500 11 TYR E 16 0.10 SIDE CHAIN
REMARK 500 11 ARG E 39 0.11 SIDE CHAIN
REMARK 500 11 PHE E 40 0.09 SIDE CHAIN
REMARK 500 12 ARG E 39 0.09 SIDE CHAIN
REMARK 500 12 PHE E 40 0.08 SIDE CHAIN
REMARK 500 13 ARG E 4 0.08 SIDE CHAIN
REMARK 500 13 ARG E 12 0.10 SIDE CHAIN
REMARK 500 14 ARG E 12 0.09 SIDE CHAIN
REMARK 500 14 PHE E 60 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GXI E 1 73 UNP P12975 PSAE_SYNY3 1 73
SEQRES 1 E 73 ALA LEU ASN ARG GLY ASP LYS VAL ARG ILE LYS ARG THR
SEQRES 2 E 73 GLU SER TYR TRP TYR GLY ASP VAL GLY THR VAL ALA SER
SEQRES 3 E 73 VAL GLU LYS SER GLY ILE LEU TYR PRO VAL ILE VAL ARG
SEQRES 4 E 73 PHE ASP ARG VAL ASN TYR ASN GLY PHE SER GLY SER ALA
SEQRES 5 E 73 SER GLY VAL ASN THR ASN ASN PHE ALA GLU ASN GLU LEU
SEQRES 6 E 73 GLU LEU VAL GLN ALA ALA ALA LYS
HELIX 1 1 ALA E 61 ASN E 63 5 3
SHEET 1 EA 3 ASP E 20 GLY E 22 0
SHEET 2 EA 3 VAL E 8 ILE E 10 -1 O VAL E 8 N GLY E 22
SHEET 3 EA 3 LEU E 65 LEU E 67 -1 O GLU E 66 N ARG E 9
SHEET 1 EB 2 VAL E 36 VAL E 38 0
SHEET 2 EB 2 ASN E 58 PHE E 60 -1 O ASN E 58 N VAL E 38
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 - n 17 2 Bytes