Header list of 1dro.pdb file
Complete list - v 3 2 Bytes
HEADER CYTOSKELETON 29-SEP-95 1DRO
TITLE NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-SPECTRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 ORGAN: FRUIT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 OTHER_DETAILS: EXPRESSION VECTOR USED WAS PGEX-2T
KEYWDS CYTOSKELETON
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR P.ZHANG,S.TALLURI,H.DENG,D.BRANTON,G.WAGNER
REVDAT 3 03-NOV-21 1DRO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1DRO 1 VERSN
REVDAT 1 03-APR-96 1DRO 0
JRNL AUTH P.ZHANG,S.TALLURI,H.DENG,D.BRANTON,G.WAGNER
JRNL TITL SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
JRNL TITL 2 DROSOPHILA BETA-SPECTRIN.
JRNL REF STRUCTURE V. 3 1185 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8591029
JRNL DOI 10.1016/S0969-2126(01)00254-4
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : HAVEL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DRO 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_1000172911.
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 : 15
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 HG2 ARG A 88 HD21 LEU A 98 0.94
REMARK 500 HG2 LYS A 17 HA TRP A 32 1.29
REMARK 500 HB2 ALA A 101 HB2 MET A 107 1.31
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 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 1 GLU A 11 CD GLU A 11 OE1 0.110
REMARK 500 1 GLU A 19 CD GLU A 19 OE1 0.109
REMARK 500 1 GLU A 58 CD GLU A 58 OE2 0.111
REMARK 500 1 GLU A 64 CD GLU A 64 OE2 0.110
REMARK 500 1 GLU A 75 CD GLU A 75 OE2 0.109
REMARK 500 1 GLU A 106 CD GLU A 106 OE2 0.111
REMARK 500 2 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 2 GLU A 11 CD GLU A 11 OE1 0.110
REMARK 500 2 GLU A 19 CD GLU A 19 OE1 0.110
REMARK 500 2 GLU A 58 CD GLU A 58 OE1 0.109
REMARK 500 2 GLU A 64 CD GLU A 64 OE1 0.110
REMARK 500 2 GLU A 75 CD GLU A 75 OE1 0.110
REMARK 500 2 GLU A 106 CD GLU A 106 OE1 0.110
REMARK 500 3 GLU A 8 CD GLU A 8 OE1 0.110
REMARK 500 3 GLU A 11 CD GLU A 11 OE2 0.110
REMARK 500 3 GLU A 19 CD GLU A 19 OE2 0.110
REMARK 500 3 GLU A 58 CD GLU A 58 OE2 0.110
REMARK 500 3 GLU A 64 CD GLU A 64 OE2 0.110
REMARK 500 3 GLU A 75 CD GLU A 75 OE1 0.109
REMARK 500 3 GLU A 106 CD GLU A 106 OE2 0.111
REMARK 500 4 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 4 GLU A 11 CD GLU A 11 OE1 0.109
REMARK 500 4 GLU A 19 CD GLU A 19 OE1 0.110
REMARK 500 4 GLU A 58 CD GLU A 58 OE1 0.109
REMARK 500 4 GLU A 64 CD GLU A 64 OE1 0.109
REMARK 500 4 GLU A 75 CD GLU A 75 OE2 0.110
REMARK 500 4 GLU A 106 CD GLU A 106 OE2 0.115
REMARK 500 5 GLU A 8 CD GLU A 8 OE1 0.110
REMARK 500 5 GLU A 11 CD GLU A 11 OE1 0.110
REMARK 500 5 GLU A 19 CD GLU A 19 OE1 0.110
REMARK 500 5 GLU A 58 CD GLU A 58 OE2 0.110
REMARK 500 5 GLU A 64 CD GLU A 64 OE2 0.111
REMARK 500 5 GLU A 75 CD GLU A 75 OE2 0.110
REMARK 500 5 GLU A 106 CD GLU A 106 OE1 0.110
REMARK 500 6 GLU A 8 CD GLU A 8 OE2 0.109
REMARK 500 6 GLU A 11 CD GLU A 11 OE2 0.110
REMARK 500 6 GLU A 19 CD GLU A 19 OE2 0.110
REMARK 500 6 GLU A 58 CD GLU A 58 OE2 0.110
REMARK 500 6 GLU A 64 CD GLU A 64 OE2 0.110
REMARK 500 6 GLU A 75 CD GLU A 75 OE1 0.110
REMARK 500 6 GLU A 106 CD GLU A 106 OE1 0.110
REMARK 500 7 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500 7 GLU A 11 CD GLU A 11 OE1 0.109
REMARK 500 7 GLU A 19 CD GLU A 19 OE1 0.111
REMARK 500 7 GLU A 58 CD GLU A 58 OE1 0.110
REMARK 500 7 GLU A 64 CD GLU A 64 OE2 0.111
REMARK 500 7 GLU A 75 CD GLU A 75 OE1 0.109
REMARK 500 7 GLU A 106 CD GLU A 106 OE1 0.111
REMARK 500 8 GLU A 8 CD GLU A 8 OE2 0.110
REMARK 500
REMARK 500 THIS ENTRY HAS 105 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 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ASP A 49 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 1 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 PRO A 65 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 1 ASP A 68 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ASP A 103 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ASP A 104 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 1 ASP A 119 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 2 ASP A 21 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 2 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ASP A 49 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 PRO A 65 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 2 ASP A 68 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 2 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ASP A 119 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ASP A 21 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ASP A 49 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 PRO A 65 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 3 ASP A 68 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 ASP A 79 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ASP A 103 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ASP A 104 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ASP A 119 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 ASP A 21 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 4 ASP A 33 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ASP A 49 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 PRO A 65 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 4 ASP A 68 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ASP A 103 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 198 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 SER A 2 -51.83 -125.73
REMARK 500 1 ALA A 6 -80.97 -72.27
REMARK 500 1 HIS A 18 -176.98 -60.76
REMARK 500 1 GLU A 19 129.10 -19.40
REMARK 500 1 ASP A 21 36.66 -165.08
REMARK 500 1 LYS A 25 -73.68 -165.54
REMARK 500 1 LYS A 26 -98.21 58.20
REMARK 500 1 SER A 28 -92.78 -153.92
REMARK 500 1 ASN A 29 104.96 63.95
REMARK 500 1 SER A 31 -41.27 -141.87
REMARK 500 1 LYS A 40 -75.90 -159.99
REMARK 500 1 ALA A 41 34.87 -175.95
REMARK 500 1 LYS A 51 -90.74 -111.38
REMARK 500 1 SER A 55 -80.42 -70.53
REMARK 500 1 PRO A 57 6.94 -68.12
REMARK 500 1 THR A 60 -123.69 -151.03
REMARK 500 1 ARG A 62 -25.55 79.48
REMARK 500 1 PRO A 65 164.87 -30.84
REMARK 500 1 ALA A 72 -173.94 -61.30
REMARK 500 1 ALA A 73 -157.76 -125.99
REMARK 500 1 ALA A 77 -81.67 -63.09
REMARK 500 1 ASP A 79 47.92 -160.29
REMARK 500 1 LEU A 91 -163.60 -63.81
REMARK 500 1 ASP A 103 -81.89 -89.53
REMARK 500 1 ASP A 104 -31.74 161.80
REMARK 500 1 SER A 113 -71.35 -54.16
REMARK 500 1 ASP A 119 67.59 -108.21
REMARK 500 1 THR A 121 -56.67 -145.11
REMARK 500 2 LYS A 17 43.59 -147.37
REMARK 500 2 GLU A 19 114.81 -3.36
REMARK 500 2 SER A 22 -99.11 48.43
REMARK 500 2 THR A 23 152.42 64.94
REMARK 500 2 LYS A 25 116.63 65.98
REMARK 500 2 ALA A 27 125.54 179.12
REMARK 500 2 SER A 28 -58.73 94.48
REMARK 500 2 ARG A 30 74.64 -167.04
REMARK 500 2 LYS A 40 -164.57 -171.04
REMARK 500 2 LYS A 51 -71.13 -50.51
REMARK 500 2 SER A 55 -83.88 -88.23
REMARK 500 2 THR A 60 -84.90 -59.04
REMARK 500 2 ARG A 62 -22.13 76.83
REMARK 500 2 PRO A 65 169.63 -40.28
REMARK 500 2 ALA A 72 150.38 -42.97
REMARK 500 2 ALA A 77 -139.80 50.30
REMARK 500 2 SER A 78 -81.54 -163.54
REMARK 500 2 ASP A 79 31.73 -156.78
REMARK 500 2 TYR A 80 -92.73 -67.30
REMARK 500 2 THR A 81 -69.20 165.34
REMARK 500 2 LEU A 91 -159.61 -106.79
REMARK 500 2 HIS A 102 -85.65 -77.98
REMARK 500
REMARK 500 THIS ENTRY HAS 422 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DRO A 1 122 UNP Q00963 SPTCB_DROME 2141 2262
SEQADV 1DRO SER A 2 UNP Q00963 GLY 2142 ENGINEERED MUTATION
SEQADV 1DRO GLY A 3 UNP Q00963 THR 2143 ENGINEERED MUTATION
SEQADV 1DRO THR A 4 UNP Q00963 PRO 2144 ENGINEERED MUTATION
SEQRES 1 A 122 GLY SER GLY THR GLY ALA GLY GLU GLY HIS GLU GLY TYR
SEQRES 2 A 122 VAL THR ARG LYS HIS GLU TRP ASP SER THR THR LYS LYS
SEQRES 3 A 122 ALA SER ASN ARG SER TRP ASP LYS VAL TYR MET ALA ALA
SEQRES 4 A 122 LYS ALA GLY ARG ILE SER PHE TYR LYS ASP GLN LYS GLY
SEQRES 5 A 122 TYR LYS SER ASN PRO GLU LEU THR PHE ARG GLY GLU PRO
SEQRES 6 A 122 SER TYR ASP LEU GLN ASN ALA ALA ILE GLU ILE ALA SER
SEQRES 7 A 122 ASP TYR THR LYS LYS LYS HIS VAL LEU ARG VAL LYS LEU
SEQRES 8 A 122 ALA ASN GLY ALA LEU PHE LEU LEU GLN ALA HIS ASP ASP
SEQRES 9 A 122 THR GLU MET SER GLN TRP VAL THR SER LEU LYS ALA GLN
SEQRES 10 A 122 SER ASP SER THR ALA
HELIX 1 A1 GLN A 50 ASN A 56 1 7
HELIX 2 A2 THR A 105 SER A 118 1WELL-DEFINED 14
SHEET 1 SH1 4 HIS A 10 THR A 15 0
SHEET 2 SH1 4 ASP A 33 ALA A 39 -1 N VAL A 35 O VAL A 14
SHEET 3 SH1 4 ARG A 43 TYR A 47 -1 N SER A 45 O ALA A 38
SHEET 4 SH1 4 PRO A 65 LEU A 69 -1 N TYR A 67 O ILE A 44
SHEET 1 SH2 4 ARG A 16 GLU A 19 0
SHEET 2 SH2 4 LEU A 96 ALA A 101 -1 O LEU A 98 N LYS A 17
SHEET 3 SH2 4 VAL A 86 LYS A 90 -1 N VAL A 89 O PHE A 97
SHEET 4 SH2 4 ALA A 73 ILE A 76 -1 N GLU A 75 O ARG A 88
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 - v 3 2 Bytes