Header list of 1wa7.pdb file
Complete list - r 25 2 Bytes
HEADER SH3 DOMAIN 25-OCT-04 1WA7
TITLE SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE IN COMPLEX WITH A
TITLE 2 HERPESVIRAL LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE LYN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 39-101;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HYPOTHETICAL 28.7 KDA PROTEIN IN DHFR 3'REGION
COMPND 9 (ORF1);
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: TYROSINE KINASE INTERACTION PROTEIN, RESIDUES
COMPND 12 170-191;
COMPND 13 SYNONYM: TIP;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: INTRACELLULAR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SAIMIRIINE HERPESVIRUS 2;
SOURCE 12 ORGANISM_COMMON: HUMAN SAIMIRIINE HERPESVIRUS 2;
SOURCE 13 ORGANISM_TAXID: 10381;
SOURCE 14 STRAIN: 488;
SOURCE 15 VARIANT: SUBGROUP C;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS SH3 DOMAIN, LIGAND, TYROSINE KINASE, SIGNAL TRANSDUCTION,
KEYWDS 2 LYN, TIP, PROTO-ONCOGENE, HYPOTHETICAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.BAUER,K.SCHWEIMER,S.HOFFMANN,P.ROESCH,H.STICHT
REVDAT 3 24-FEB-09 1WA7 1 VERSN
REVDAT 2 13-JUL-05 1WA7 1 JRNL
REVDAT 1 07-JUL-05 1WA7 0
JRNL AUTH K.SCHWEIMER,S.HOFFMANN,F.BAUER,U.FRIEDRICH,
JRNL AUTH 2 C.KARDINAL,S.M.FELLER,B.BIESINGER,H.STICHT
JRNL TITL STRUCTURAL INVESTIGATION OF THE BINDING OF A
JRNL TITL 2 HERPESVIRAL PROTEIN TO THE SH3 DOMAIN OF TYROSINE
JRNL TITL 3 KINASE LCK.
JRNL REF BIOCHEMISTRY V. 41 5120 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11955060
JRNL DOI 10.1021/BI015986J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WA7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-04.
REMARK 100 THE PDBE ID CODE IS EBI-21410.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0 ; 298.0
REMARK 210 PH : 6.4 ; 6.4
REMARK 210 IONIC STRENGTH : 150 MM ; 150 MM
REMARK 210 PRESSURE : 1.0 ; 1.0
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O, 2.5
REMARK 210 MMOL/L ; 90% WATER/10%
REMARK 210 D2O, 1.5 MMOL/L
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 13C-EDITED NOESY,3D 15N-
REMARK 210 EDITED NOESY ; 3D 13C-
REMARK 210 EDITED NOESY,3D 15N-EDITED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 ; 800
REMARK 210 SPECTROMETER MODEL : AVANCE ; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER ; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW
REMARK 210 METHOD USED : XPLOR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE
REMARK 210 NMR SPECTROSCOPY ON 13C, 15N-LABELED LYNSH3 AND TIP
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 8
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O ALA A 15 - H GLY A 32 1.59
REMARK 500 O TRP A 45 - H ILE A 58 1.54
REMARK 500 H SER A 49 - O LYS A 54 1.46
REMARK 500 HB3 PRO A 59 - HD2 PRO B 180 1.58
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 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 GLU A 43 -25.57 -148.50
REMARK 500 1 THR A 52 29.47 -161.30
REMARK 500 1 LYS A 53 44.00 86.31
REMARK 500 1 ASN A 67 -94.22 -77.29
REMARK 500 1 ASP B 171 -57.30 -167.25
REMARK 500 1 MET B 174 77.35 -154.92
REMARK 500 1 THR B 176 101.09 173.47
REMARK 500 1 ARG B 182 95.62 78.41
REMARK 500 1 GLU B 188 -87.43 -81.20
REMARK 500 1 GLN B 190 99.67 -66.88
REMARK 500 2 GLU A 43 -12.80 -157.24
REMARK 500 2 THR A 52 28.57 -160.13
REMARK 500 2 LYS A 53 44.86 86.32
REMARK 500 2 ASN A 67 -84.50 -97.35
REMARK 500 2 ASP B 171 -54.86 -172.63
REMARK 500 2 MET B 174 99.75 -162.14
REMARK 500 2 PRO B 175 -161.16 -77.00
REMARK 500 2 THR B 176 113.73 164.58
REMARK 500 2 LEU B 179 160.78 -47.20
REMARK 500 2 ARG B 182 81.66 80.59
REMARK 500 2 ALA B 184 62.70 37.74
REMARK 500 2 GLU B 188 -80.06 -75.57
REMARK 500 3 ASP A 11 -167.29 64.09
REMARK 500 3 GLU A 43 -17.80 -153.92
REMARK 500 3 THR A 52 29.54 -161.38
REMARK 500 3 LYS A 53 44.91 86.45
REMARK 500 3 LEU A 66 -158.05 -75.86
REMARK 500 3 ASN A 67 121.78 76.70
REMARK 500 3 ASP B 171 -56.27 -170.48
REMARK 500 3 MET B 174 91.35 51.13
REMARK 500 3 PRO B 175 -161.35 -77.52
REMARK 500 3 THR B 176 102.54 -177.24
REMARK 500 3 PRO B 180 -175.00 -69.92
REMARK 500 3 ARG B 182 94.33 78.71
REMARK 500 3 GLU B 188 -82.86 -75.69
REMARK 500 3 ARG B 189 85.64 72.50
REMARK 500 4 GLU A 43 -17.04 -154.21
REMARK 500 4 THR A 52 -21.47 168.15
REMARK 500 4 LYS A 53 42.61 140.55
REMARK 500 4 ASN A 67 -94.06 -123.47
REMARK 500 4 ASP B 171 59.75 170.03
REMARK 500 4 PRO B 175 -162.49 -79.44
REMARK 500 4 THR B 176 99.46 -170.15
REMARK 500 4 PRO B 180 -173.43 -69.34
REMARK 500 4 ARG B 182 95.02 80.99
REMARK 500 4 ARG B 189 105.05 78.25
REMARK 500 4 GLN B 190 -174.13 175.06
REMARK 500 5 GLU A 43 -20.95 -155.57
REMARK 500 5 THR A 52 28.42 -160.69
REMARK 500 5 LYS A 53 44.50 86.80
REMARK 500 5 ASP B 171 58.02 174.18
REMARK 500 5 MET B 174 51.37 39.69
REMARK 500 5 PRO B 175 -161.88 -78.95
REMARK 500 5 PRO B 180 -174.48 -67.96
REMARK 500 5 ARG B 182 104.95 84.23
REMARK 500 5 GLU B 188 -72.47 -69.77
REMARK 500 6 GLU A 43 -26.38 -148.69
REMARK 500 6 THR A 52 30.08 -161.06
REMARK 500 6 LYS A 53 45.49 85.78
REMARK 500 6 SER A 60 3.68 -62.88
REMARK 500 6 LEU A 66 -80.31 -103.74
REMARK 500 6 ASN A 67 152.94 -44.61
REMARK 500 6 ASP B 171 -55.55 -170.83
REMARK 500 6 THR B 176 116.60 161.80
REMARK 500 6 ARG B 182 98.02 82.22
REMARK 500 6 ALA B 184 72.89 35.63
REMARK 500 6 GLU B 188 -74.05 -77.52
REMARK 500 6 ARG B 189 101.31 71.77
REMARK 500 7 GLU A 43 -19.15 -156.48
REMARK 500 7 THR A 52 -21.87 168.02
REMARK 500 7 LYS A 53 41.89 140.93
REMARK 500 7 LEU A 66 97.82 -45.89
REMARK 500 7 ASP B 171 -55.63 -170.75
REMARK 500 7 MET B 174 117.03 160.50
REMARK 500 7 THR B 176 104.47 172.45
REMARK 500 7 PRO B 180 -176.04 -69.58
REMARK 500 7 ARG B 182 91.26 77.50
REMARK 500 7 ALA B 184 64.81 39.27
REMARK 500 7 GLU B 188 -90.35 -72.10
REMARK 500 7 ARG B 189 102.82 78.44
REMARK 500 8 GLU A 43 -18.78 -156.85
REMARK 500 8 THR A 52 29.69 -161.16
REMARK 500 8 LYS A 53 45.85 86.36
REMARK 500 8 ASN A 67 -81.49 75.59
REMARK 500 8 ASP B 171 59.62 172.68
REMARK 500 8 MET B 174 109.00 178.43
REMARK 500 8 THR B 176 105.31 178.37
REMARK 500 8 PRO B 180 -176.02 -68.92
REMARK 500 8 ARG B 182 89.90 78.75
REMARK 500 8 ALA B 184 60.87 37.26
REMARK 500 8 GLU B 188 -73.18 -103.98
REMARK 500 9 GLU A 43 -29.52 -149.43
REMARK 500 9 THR A 52 29.61 -161.24
REMARK 500 9 LYS A 53 45.20 86.59
REMARK 500 9 ASP B 171 -56.43 -169.61
REMARK 500 9 THR B 176 100.83 -173.18
REMARK 500 9 PRO B 180 -172.15 -69.13
REMARK 500 9 ARG B 182 92.92 91.49
REMARK 500 9 ALA B 184 69.81 36.66
REMARK 500 9 ASN B 185 45.42 39.46
REMARK 500 10 GLU A 43 -20.24 -158.00
REMARK 500 10 THR A 52 30.11 -161.16
REMARK 500 10 LYS A 53 45.41 85.58
REMARK 500 10 SER A 60 4.69 -65.20
REMARK 500 10 ASN A 67 157.95 171.06
REMARK 500 10 ASP B 171 -56.15 -170.18
REMARK 500 10 MET B 174 87.39 65.31
REMARK 500 10 THR B 176 117.56 160.59
REMARK 500 10 ARG B 182 95.67 79.41
REMARK 500 10 ALA B 184 69.13 35.64
REMARK 500 10 ARG B 189 -78.92 -177.63
REMARK 500 11 HIS A 23 -171.02 -66.39
REMARK 500 11 GLU A 43 -16.43 -153.24
REMARK 500 11 THR A 52 27.56 -160.40
REMARK 500 11 LYS A 53 43.46 87.20
REMARK 500 11 LYS A 65 179.81 -48.37
REMARK 500 11 ASN A 67 -154.54 -78.29
REMARK 500 11 ASP B 171 -57.14 -167.53
REMARK 500 11 PRO B 175 -160.50 -77.81
REMARK 500 11 LEU B 179 177.05 -49.94
REMARK 500 11 PRO B 180 -175.84 -67.36
REMARK 500 11 ARG B 182 93.07 77.00
REMARK 500 11 GLU B 188 -86.73 -81.78
REMARK 500 11 ARG B 189 119.28 61.89
REMARK 500 11 GLN B 190 27.87 -157.13
REMARK 500 12 GLU A 43 -10.87 -165.80
REMARK 500 12 THR A 52 -21.94 169.42
REMARK 500 12 LYS A 53 39.23 140.33
REMARK 500 12 LEU A 66 164.00 -47.84
REMARK 500 12 ASP B 171 -57.48 -166.50
REMARK 500 12 MET B 174 82.91 43.80
REMARK 500 12 PRO B 175 -161.69 -79.15
REMARK 500 12 PRO B 180 -176.57 -68.79
REMARK 500 12 ARG B 182 91.56 78.14
REMARK 500 12 GLU B 188 -81.40 -73.60
REMARK 500 12 ARG B 189 85.02 72.11
REMARK 500 13 GLU A 43 5.28 -172.44
REMARK 500 13 THR A 52 28.72 -161.54
REMARK 500 13 LYS A 53 44.33 87.09
REMARK 500 13 SER A 60 4.30 -67.93
REMARK 500 13 ASN A 67 -152.58 74.69
REMARK 500 13 ASP B 171 60.49 167.30
REMARK 500 13 MET B 174 105.65 -171.99
REMARK 500 13 THR B 176 107.16 168.24
REMARK 500 13 ARG B 182 81.44 78.94
REMARK 500 13 ALA B 184 61.93 36.35
REMARK 500 13 GLU B 188 -83.83 -69.66
REMARK 500 13 GLN B 190 -70.40 -58.83
REMARK 500 14 GLU A 43 -15.10 -158.77
REMARK 500 14 THR A 52 27.51 -160.62
REMARK 500 14 LYS A 53 45.17 87.83
REMARK 500 14 SER A 60 5.24 -65.97
REMARK 500 14 ASP B 171 61.31 165.89
REMARK 500 14 MET B 174 69.65 176.41
REMARK 500 14 PRO B 175 -162.34 -79.19
REMARK 500 14 THR B 176 102.79 -174.33
REMARK 500 14 ARG B 182 91.25 76.34
REMARK 500 14 GLU B 188 -90.67 -51.13
REMARK 500 14 ARG B 189 -169.02 -164.79
REMARK 500 15 GLU A 43 -19.76 -153.15
REMARK 500 15 THR A 52 29.08 -161.08
REMARK 500 15 LYS A 53 45.46 86.93
REMARK 500 15 LEU A 66 113.45 171.93
REMARK 500 15 ASP B 171 57.75 176.84
REMARK 500 15 PRO B 175 -159.73 -77.05
REMARK 500 15 PRO B 180 -175.29 -69.14
REMARK 500 15 ARG B 182 95.34 81.97
REMARK 500 15 GLU B 188 -86.63 -71.98
REMARK 500 15 GLN B 190 -72.92 -44.12
REMARK 500 16 GLU A 43 -16.99 -158.43
REMARK 500 16 THR A 52 29.16 -160.88
REMARK 500 16 LYS A 53 42.98 85.91
REMARK 500 16 LEU A 66 -75.37 -67.21
REMARK 500 16 ASN A 67 -140.90 -142.17
REMARK 500 16 ASP B 171 -56.58 -168.53
REMARK 500 16 THR B 176 107.47 172.15
REMARK 500 16 PRO B 178 97.24 -67.33
REMARK 500 16 LEU B 179 162.42 -39.24
REMARK 500 16 ARG B 182 84.26 78.27
REMARK 500 16 ALA B 184 62.23 38.60
REMARK 500 16 GLU B 188 -87.26 -70.93
REMARK 500 16 ARG B 189 -164.17 -72.79
REMARK 500 16 GLN B 190 44.64 -105.88
REMARK 500 17 GLU A 39 130.99 -176.99
REMARK 500 17 GLU A 43 -5.90 -159.20
REMARK 500 17 THR A 52 29.35 -161.50
REMARK 500 17 LYS A 53 44.31 86.68
REMARK 500 17 LEU A 66 55.39 39.88
REMARK 500 17 ASP B 171 -56.25 -170.50
REMARK 500 17 MET B 174 112.07 59.23
REMARK 500 17 PRO B 175 -161.88 -78.94
REMARK 500 17 THR B 176 97.58 -164.77
REMARK 500 17 PRO B 180 -172.30 -68.96
REMARK 500 17 ARG B 182 96.27 87.83
REMARK 500 17 GLU B 188 -86.04 -69.91
REMARK 500 17 ARG B 189 140.52 73.05
REMARK 500 17 GLN B 190 -40.93 -139.14
REMARK 500 18 THR A 52 -21.72 168.10
REMARK 500 18 LYS A 53 42.48 140.84
REMARK 500 18 ASN A 67 -81.47 -43.41
REMARK 500 18 ASP B 171 58.80 172.71
REMARK 500 18 THR B 176 100.14 -171.12
REMARK 500 18 PRO B 178 -165.52 -69.13
REMARK 500 18 PRO B 180 -174.65 -67.24
REMARK 500 18 ARG B 182 96.73 76.47
REMARK 500 18 ALA B 184 68.56 60.65
REMARK 500 18 ARG B 189 -156.84 -149.48
REMARK 500 18 GLN B 190 30.06 -153.49
REMARK 500 19 TYR A 19 -76.45 -70.36
REMARK 500 19 GLU A 39 96.08 -160.03
REMARK 500 19 THR A 52 29.68 -160.45
REMARK 500 19 LYS A 53 43.03 85.25
REMARK 500 19 LEU A 66 -81.28 -91.38
REMARK 500 19 ASP B 171 -58.73 -161.77
REMARK 500 19 MET B 174 89.58 43.19
REMARK 500 19 PRO B 175 -160.67 -77.77
REMARK 500 19 LEU B 179 163.54 -40.38
REMARK 500 19 ARG B 182 91.78 84.81
REMARK 500 19 ALA B 184 67.03 38.21
REMARK 500 19 GLU B 188 -73.17 -67.64
REMARK 500 19 ARG B 189 158.35 74.25
REMARK 500 19 GLN B 190 23.45 -143.44
REMARK 500 20 GLU A 43 -16.00 -157.52
REMARK 500 20 THR A 52 28.14 -161.04
REMARK 500 20 LYS A 53 44.20 87.38
REMARK 500 20 ASN A 67 12.77 -149.04
REMARK 500 20 ASP B 171 -58.49 -164.00
REMARK 500 20 MET B 174 118.82 59.07
REMARK 500 20 PRO B 175 -163.66 -79.61
REMARK 500 20 THR B 176 102.62 -176.16
REMARK 500 20 ARG B 182 112.78 141.05
REMARK 500 20 ALA B 184 52.88 37.99
REMARK 500 20 GLU B 188 -102.45 -72.89
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 B 182 0.30 SIDE CHAIN
REMARK 500 1 ARG B 189 0.24 SIDE CHAIN
REMARK 500 2 ARG B 182 0.22 SIDE CHAIN
REMARK 500 2 ARG B 189 0.16 SIDE CHAIN
REMARK 500 3 ARG B 182 0.27 SIDE CHAIN
REMARK 500 3 ARG B 189 0.27 SIDE CHAIN
REMARK 500 4 ARG B 182 0.29 SIDE CHAIN
REMARK 500 4 ARG B 189 0.15 SIDE CHAIN
REMARK 500 5 ARG B 189 0.31 SIDE CHAIN
REMARK 500 6 ARG B 189 0.18 SIDE CHAIN
REMARK 500 7 ARG B 182 0.19 SIDE CHAIN
REMARK 500 7 ARG B 189 0.31 SIDE CHAIN
REMARK 500 8 ARG B 182 0.32 SIDE CHAIN
REMARK 500 8 ARG B 189 0.31 SIDE CHAIN
REMARK 500 9 ARG B 182 0.31 SIDE CHAIN
REMARK 500 9 ARG B 189 0.15 SIDE CHAIN
REMARK 500 10 ARG B 182 0.24 SIDE CHAIN
REMARK 500 10 ARG B 189 0.27 SIDE CHAIN
REMARK 500 11 ARG B 182 0.24 SIDE CHAIN
REMARK 500 11 ARG B 189 0.22 SIDE CHAIN
REMARK 500 12 ARG B 182 0.28 SIDE CHAIN
REMARK 500 12 ARG B 189 0.19 SIDE CHAIN
REMARK 500 13 ARG B 182 0.21 SIDE CHAIN
REMARK 500 13 ARG B 189 0.32 SIDE CHAIN
REMARK 500 14 ARG B 182 0.25 SIDE CHAIN
REMARK 500 14 ARG B 189 0.30 SIDE CHAIN
REMARK 500 15 ARG B 182 0.29 SIDE CHAIN
REMARK 500 15 ARG B 189 0.22 SIDE CHAIN
REMARK 500 16 ARG B 182 0.18 SIDE CHAIN
REMARK 500 16 ARG B 189 0.31 SIDE CHAIN
REMARK 500 17 ARG B 182 0.26 SIDE CHAIN
REMARK 500 17 ARG B 189 0.25 SIDE CHAIN
REMARK 500 18 ARG B 182 0.28 SIDE CHAIN
REMARK 500 18 ARG B 189 0.30 SIDE CHAIN
REMARK 500 19 ARG B 182 0.19 SIDE CHAIN
REMARK 500 19 ARG B 189 0.31 SIDE CHAIN
REMARK 500 20 ARG B 182 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W1F RELATED DB: PDB
REMARK 900 SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE
DBREF 1WA7 A 4 5 PDB 1WA7 1WA7 4 5
DBREF 1WA7 A 6 68 UNP P07948 LYN_HUMAN 39 101
DBREF 1WA7 B 170 191 UNP P22575 YDH1_SHV2C 170 191
SEQRES 1 A 65 GLY SER PRO GLU GLU GLN GLY ASP ILE VAL VAL ALA LEU
SEQRES 2 A 65 TYR PRO TYR ASP GLY ILE HIS PRO ASP ASP LEU SER PHE
SEQRES 3 A 65 LYS LYS GLY GLU LYS MET LYS VAL LEU GLU GLU HIS GLY
SEQRES 4 A 65 GLU TRP TRP LYS ALA LYS SER LEU LEU THR LYS LYS GLU
SEQRES 5 A 65 GLY PHE ILE PRO SER ASN TYR VAL ALA LYS LEU ASN THR
SEQRES 1 B 22 TRP ASP PRO GLY MET PRO THR PRO PRO LEU PRO PRO ARG
SEQRES 2 B 22 PRO ALA ASN LEU GLY GLU ARG GLN ALA
SHEET 1 AA 5 LYS A 54 PRO A 59 0
SHEET 2 AA 5 TRP A 44 SER A 49 -1 O TRP A 45 N ILE A 58
SHEET 3 AA 5 LYS A 34 GLU A 39 -1 O LYS A 36 N LYS A 48
SHEET 4 AA 5 ILE A 12 ALA A 15 -1 O VAL A 13 N MET A 35
SHEET 5 AA 5 VAL A 63 LYS A 65 -1 O ALA A 64 N VAL A 14
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 - r 25 2 Bytes