Header list of 1blk.pdb file
Complete list - b 16 2 Bytes
HEADER PHOSPHORYLATION 26-MAR-96 1BLK
TITLE NMR ENSEMBLE OF BLK SH2 DOMAIN USING CHEMICAL SHIFT REFINEMENT, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P55 BLK PROTEIN TYROSINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN, SRC HOMOLOGY 2;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PEPTIDE FREE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: P55 BLK KINASE (RESIDUES 107 -;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 10 EXPRESSION_SYSTEM_GENE: P55 BLK KINASE (RESIDUES 107 - 218)
KEYWDS SIGNAL TRANSDUCTION, TYROSINE KINASE, TRANSFERASE,
KEYWDS 2 PHOSPHOTRANSFERASE, PHOSPHORYLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.J.METZLER,B.LEITING,K.PRYOR,L.MUELLER,B.T.FARMER II
REVDAT 4 16-FEB-22 1BLK 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1BLK 1 VERSN
REVDAT 2 01-APR-03 1BLK 1 JRNL
REVDAT 1 12-MAR-97 1BLK 0
JRNL AUTH W.J.METZLER,B.LEITING,K.PRYOR,L.MUELLER,B.T.FARMER 2ND.
JRNL TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SH2 DOMAIN
JRNL TITL 2 FROM P55BLK KINASE.
JRNL REF BIOCHEMISTRY V. 35 6201 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8639560
JRNL DOI 10.1021/BI960157X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BLK 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_1000171891.
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: 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 HG1 THR A 107 H LEU A 108 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 1 SER A 43 CB SER A 43 OG 0.082
REMARK 500 1 SER A 96 CB SER A 96 OG 0.089
REMARK 500 2 SER A 2 CB SER A 2 OG 0.090
REMARK 500 2 SER A 43 CB SER A 43 OG 0.085
REMARK 500 2 SER A 51 CB SER A 51 OG 0.098
REMARK 500 2 SER A 53 CB SER A 53 OG 0.080
REMARK 500 2 SER A 71 CB SER A 71 OG 0.095
REMARK 500 2 SER A 80 CB SER A 80 OG 0.085
REMARK 500 2 SER A 96 CB SER A 96 OG 0.103
REMARK 500 3 SER A 2 CB SER A 2 OG 0.085
REMARK 500 3 SER A 96 CB SER A 96 OG 0.092
REMARK 500 4 SER A 2 CB SER A 2 OG 0.081
REMARK 500 4 SER A 20 CB SER A 20 OG 0.083
REMARK 500 4 SER A 37 CB SER A 37 OG 0.079
REMARK 500 4 SER A 53 CB SER A 53 OG 0.079
REMARK 500 4 SER A 96 CB SER A 96 OG 0.083
REMARK 500 5 SER A 2 CB SER A 2 OG 0.081
REMARK 500 5 SER A 43 CB SER A 43 OG 0.088
REMARK 500 5 SER A 80 CB SER A 80 OG 0.080
REMARK 500 5 SER A 96 CB SER A 96 OG 0.098
REMARK 500 7 SER A 37 CB SER A 37 OG 0.083
REMARK 500 7 SER A 51 CB SER A 51 OG 0.085
REMARK 500 8 SER A 20 CB SER A 20 OG 0.088
REMARK 500 8 SER A 37 CB SER A 37 OG 0.091
REMARK 500 8 SER A 45 CB SER A 45 OG 0.085
REMARK 500 8 SER A 96 CB SER A 96 OG 0.095
REMARK 500 9 SER A 2 CB SER A 2 OG 0.086
REMARK 500 9 SER A 43 CB SER A 43 OG 0.089
REMARK 500 9 SER A 45 CB SER A 45 OG 0.086
REMARK 500 9 SER A 51 CB SER A 51 OG 0.085
REMARK 500 10 SER A 71 CB SER A 71 OG 0.087
REMARK 500 10 SER A 96 CB SER A 96 OG 0.102
REMARK 500 11 SER A 2 CB SER A 2 OG 0.084
REMARK 500 11 SER A 20 CB SER A 20 OG 0.078
REMARK 500 11 SER A 53 CB SER A 53 OG 0.084
REMARK 500 11 SER A 71 CB SER A 71 OG 0.082
REMARK 500 12 SER A 20 CB SER A 20 OG 0.081
REMARK 500 13 SER A 2 CB SER A 2 OG 0.091
REMARK 500 13 SER A 45 CB SER A 45 OG 0.084
REMARK 500 13 SER A 51 CB SER A 51 OG 0.090
REMARK 500 13 SER A 53 CB SER A 53 OG 0.084
REMARK 500 13 SER A 71 CB SER A 71 OG 0.090
REMARK 500 13 SER A 96 CB SER A 96 OG 0.090
REMARK 500 14 SER A 53 CB SER A 53 OG 0.081
REMARK 500 14 SER A 71 CB SER A 71 OG 0.088
REMARK 500 14 SER A 80 CB SER A 80 OG 0.085
REMARK 500 15 SER A 20 CB SER A 20 OG 0.082
REMARK 500 15 SER A 43 CB SER A 43 OG 0.083
REMARK 500 15 SER A 45 CB SER A 45 OG 0.084
REMARK 500 15 SER A 71 CB SER A 71 OG 0.083
REMARK 500
REMARK 500 THIS ENTRY HAS 70 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 ILE A 40 CG1 - CB - CG2 ANGL. DEV. = -15.6 DEGREES
REMARK 500 1 THR A 59 CA - CB - OG1 ANGL. DEV. = 13.7 DEGREES
REMARK 500 1 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -13.2 DEGREES
REMARK 500 3 PHE A 38 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 4 THR A 58 OG1 - CB - CG2 ANGL. DEV. = 14.1 DEGREES
REMARK 500 4 THR A 59 CA - CB - OG1 ANGL. DEV. = 13.1 DEGREES
REMARK 500 5 THR A 8 CA - CB - OG1 ANGL. DEV. = 14.2 DEGREES
REMARK 500 5 LEU A 39 CB - CG - CD2 ANGL. DEV. = 11.7 DEGREES
REMARK 500 5 ILE A 40 CG1 - CB - CG2 ANGL. DEV. = -14.1 DEGREES
REMARK 500 5 THR A 58 OG1 - CB - CG2 ANGL. DEV. = 14.4 DEGREES
REMARK 500 5 THR A 59 CA - CB - OG1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 5 THR A 87 CA - CB - OG1 ANGL. DEV. = 13.5 DEGREES
REMARK 500 5 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 6 THR A 8 OG1 - CB - CG2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 6 THR A 87 CA - CB - OG1 ANGL. DEV. = 14.0 DEGREES
REMARK 500 7 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 7 ASP A 100 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 7 ASP A 100 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 7 THR A 107 CA - CB - OG1 ANGL. DEV. = 13.2 DEGREES
REMARK 500 8 ASP A 100 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 8 ASP A 100 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 9 LEU A 39 CB - CG - CD2 ANGL. DEV. = 12.7 DEGREES
REMARK 500 9 ILE A 40 CG1 - CB - CG2 ANGL. DEV. = -14.9 DEGREES
REMARK 500 9 THR A 58 CA - CB - OG1 ANGL. DEV. = 15.7 DEGREES
REMARK 500 9 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 9 ASP A 100 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 9 ASP A 100 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 9 THR A 107 CA - CB - CG2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 10 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 10 ASP A 100 CB - CG - OD1 ANGL. DEV. = -9.6 DEGREES
REMARK 500 10 ASP A 100 CB - CG - OD2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 11 THR A 87 CA - CB - OG1 ANGL. DEV. = 14.9 DEGREES
REMARK 500 11 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -12.9 DEGREES
REMARK 500 12 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 13 LEU A 39 CB - CG - CD2 ANGL. DEV. = 12.2 DEGREES
REMARK 500 13 THR A 58 CA - CB - OG1 ANGL. DEV. = 14.1 DEGREES
REMARK 500 14 LEU A 39 CB - CG - CD2 ANGL. DEV. = 12.6 DEGREES
REMARK 500 14 THR A 58 CA - CB - OG1 ANGL. DEV. = 15.3 DEGREES
REMARK 500 14 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 15 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 16 LEU A 39 CB - CG - CD2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 16 THR A 87 CA - CB - OG1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 16 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 17 LEU A 39 CB - CG - CD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500 17 LEU A 39 CB - CG - CD2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 17 THR A 58 CA - CB - OG1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 17 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -13.0 DEGREES
REMARK 500 18 LEU A 39 CB - CG - CD2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 18 VAL A 92 CG1 - CB - CG2 ANGL. DEV. = -11.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 61 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 93.27 -169.70
REMARK 500 1 VAL A 3 74.30 40.23
REMARK 500 1 ALA A 4 -60.25 -158.42
REMARK 500 1 PRO A 5 98.30 -61.90
REMARK 500 1 VAL A 6 76.50 -177.95
REMARK 500 1 GLU A 7 77.16 55.90
REMARK 500 1 VAL A 11 50.95 -151.38
REMARK 500 1 LYS A 13 49.55 -69.85
REMARK 500 1 TRP A 14 -58.89 -140.80
REMARK 500 1 ARG A 17 -151.45 -82.42
REMARK 500 1 ALA A 35 108.64 -49.75
REMARK 500 1 GLU A 44 48.05 -76.14
REMARK 500 1 SER A 45 -39.18 -141.53
REMARK 500 1 LYS A 47 44.57 -71.55
REMARK 500 1 GLN A 60 42.25 -99.23
REMARK 500 1 VAL A 64 -165.02 -113.71
REMARK 500 1 ASN A 74 38.50 -143.62
REMARK 500 1 THR A 107 -72.06 -115.64
REMARK 500 1 PRO A 109 178.23 -58.79
REMARK 500 1 LEU A 113 87.27 67.04
REMARK 500 2 SER A 2 75.66 68.69
REMARK 500 2 ALA A 4 78.11 67.46
REMARK 500 2 GLU A 7 -72.13 77.35
REMARK 500 2 THR A 8 -63.04 -156.64
REMARK 500 2 VAL A 11 -85.64 -145.89
REMARK 500 2 GLU A 12 167.28 63.06
REMARK 500 2 LYS A 13 -59.95 81.63
REMARK 500 2 ARG A 17 -167.88 54.65
REMARK 500 2 GLU A 44 42.34 -75.66
REMARK 500 2 SER A 45 -21.79 -144.57
REMARK 500 2 GLN A 60 -66.96 -95.75
REMARK 500 2 VAL A 64 -163.54 -114.49
REMARK 500 2 CYS A 103 14.88 52.49
REMARK 500 2 THR A 107 -65.86 -108.90
REMARK 500 2 PRO A 109 95.61 -54.32
REMARK 500 2 CYS A 110 -151.84 34.85
REMARK 500 2 ASN A 112 -71.42 -138.55
REMARK 500 3 VAL A 3 146.13 67.56
REMARK 500 3 PRO A 5 -174.09 -61.84
REMARK 500 3 VAL A 6 -71.05 -142.57
REMARK 500 3 GLU A 10 64.38 -107.40
REMARK 500 3 VAL A 11 -74.25 -158.61
REMARK 500 3 GLU A 12 88.78 57.72
REMARK 500 3 LYS A 13 42.26 -74.05
REMARK 500 3 TRP A 14 -54.87 -143.68
REMARK 500 3 ARG A 17 -144.29 -80.41
REMARK 500 3 ALA A 35 99.61 14.92
REMARK 500 3 GLU A 44 49.43 -76.07
REMARK 500 3 SER A 45 -42.67 -141.07
REMARK 500 3 LYS A 47 38.31 -71.43
REMARK 500
REMARK 500 THIS ENTRY HAS 394 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 9 TYR A 67 0.07 SIDE CHAIN
REMARK 500 16 TYR A 67 0.08 SIDE CHAIN
REMARK 500 20 TYR A 67 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BLK A 1 114 UNP P16277 BLK_MOUSE 99 217
SEQADV 1BLK GLY A 1 UNP P16277 PRO 102 CONFLICT
SEQADV 1BLK A UNP P16277 ASN 104 DELETION
SEQADV 1BLK A UNP P16277 PHE 105 DELETION
SEQRES 1 A 114 GLY SER VAL ALA PRO VAL GLU THR LEU GLU VAL GLU LYS
SEQRES 2 A 114 TRP PHE PHE ARG THR ILE SER ARG LYS ASP ALA GLU ARG
SEQRES 3 A 114 GLN LEU LEU ALA PRO MET ASN LYS ALA GLY SER PHE LEU
SEQRES 4 A 114 ILE ARG GLU SER GLU SER ASN LYS GLY ALA PHE SER LEU
SEQRES 5 A 114 SER VAL LYS ASP ILE THR THR GLN GLY GLU VAL VAL LYS
SEQRES 6 A 114 HIS TYR LYS ILE ARG SER LEU ASP ASN GLY GLY TYR TYR
SEQRES 7 A 114 ILE SER PRO ARG ILE THR PHE PRO THR LEU GLN ALA LEU
SEQRES 8 A 114 VAL GLN HIS TYR SER LYS LYS GLY ASP GLY LEU CYS GLN
SEQRES 9 A 114 LYS LEU THR LEU PRO CYS VAL ASN LEU ALA
HELIX 1 1 ARG A 21 LEU A 28 1 8
HELIX 2 2 LEU A 88 LYS A 97 1 10
SHEET 1 A 4 TRP A 14 PHE A 16 0
SHEET 2 A 4 SER A 37 GLU A 42 1 N ILE A 40 O PHE A 16
SHEET 3 A 4 ALA A 49 ILE A 57 -1 N SER A 53 O LEU A 39
SHEET 4 A 4 GLU A 62 ILE A 69 -1 N ILE A 69 O PHE A 50
SHEET 1 B 3 ARG A 70 LEU A 72 0
SHEET 2 B 3 GLY A 76 SER A 80 -1 N TYR A 78 O ARG A 70
SHEET 3 B 3 ILE A 83 PHE A 85 -1 N PHE A 85 O TYR A 77
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