1BTG header
HEADER GROWTH FACTOR 29-AUG-95 1BTG 1BTG 2
TITLE CRYSTAL STRUCTURE OF BETA NERVE GROWTH FACTOR AT 2.5 A 1BTG 3
TITLE 2 RESOLUTION IN C2 SPACE GROUP WITH ZN IONS BOUND 1BTG 4
COMPND MOL_ID: 1; 1BTG 5
COMPND 2 MOLECULE: BETA NERVE GROWTH FACTOR; 1BTG 6
COMPND 3 CHAIN: A, B, C; 1BTG 7
COMPND 4 SYNONYM: BNGF; 1BTG 8
COMPND 5 ENGINEERED: YES; 1BTG 9
COMPND 6 MUTATION: BIS-DES-OCTA 1BTG 10
COMPND 7 (MISSING RESIDUES 1-8, PROTEOLYTICALLY CLEAVED); 1BTG 11
COMPND 8 OTHER_DETAILS: ZN IONS BOUND 1BTG 12
SOURCE MOL_ID: 1; 1BTG 13
SOURCE 2 SYNTHETIC: YES; 1BTG 14
SOURCE 3 ORGANISM_SCIENTIFIC: MUS MUSCULUS; 1BTG 15
SOURCE 4 ORGANISM_COMMON: MOUSE; 1BTG 16
SOURCE 5 ORGAN: SALIVARY GLANDS 1BTG 17
KEYWDS NERVE 1BTG 18
EXPDTA X-RAY DIFFRACTION 1BTG 19
AUTHOR D.R.HOLLAND,B.W.MATTHEWS 1BTG 20
REVDAT 1 08-MAR-96 1BTG 0 1BTG 21
JRNL AUTH D.R.HOLLAND,L.S.COUSENS,W.MENG,B.W.MATTHEWS 1BTG 22
JRNL TITL NERVE GROWTH FACTOR IN DIFFERENT CRYSTAL FORMS 1BTG 23
JRNL TITL 2 DISPLAYS STRUCTURAL FLEXIBILITY AND REVEALS ZINC 1BTG 24
JRNL TITL 3 BINDING SITES 1BTG 25
JRNL REF J.MOL.BIOL. V. 239 385 1994 1BTG 26
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1BTG 27
REMARK 1 1BTG 28
REMARK 2 1BTG 29
REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1BTG 30
REMARK 3 1BTG 31
REMARK 3 REFINEMENT. 1BTG 32
REMARK 3 PROGRAM : TNT 1BTG 33
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS 1BTG 34
REMARK 3 1BTG 35
REMARK 3 MODEL QUALITY. 1BTG 36
REMARK 3 R VALUE (WITH SIGMA CUTOFF) : 0.179 1BTG 37
REMARK 3 SIGMA CUTOFF LEVEL : 2. 1BTG 38
REMARK 3 1BTG 39
REMARK 3 DATA USED IN REFINEMENT. 1BTG 40
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.5 1BTG 41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20. 1BTG 42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2. 1BTG 43
REMARK 3 NUMBER OF REFLECTIONS : 44269 1BTG 44
REMARK 3 1BTG 45
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1BTG 46
REMARK 3 PROTEIN ATOMS : 2508 1BTG 47
REMARK 3 NUCLEIC ACID ATOMS : 0 1BTG 48
REMARK 3 HETEROGEN ATOMS : 3 1BTG 49
REMARK 3 SOLVENT ATOMS : 53 1BTG 50
REMARK 3 1BTG 51
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT 1BTG 52
REMARK 3 BOND LENGTHS (A) : 0.014 ; 0.02 ; 1BTG 53
REMARK 3 BOND ANGLES (DEGREES) : 2.4 ; 2.5 ; 1BTG 54
REMARK 3 1BTG 55
REMARK 3 DATA COLLECTION. 1BTG 56
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 15194 1BTG 57
REMARK 3 COMPLETENESS OF DATA 89. % 1BTG 58
REMARK 3 REJECTION CRITERIA 3. SIGMA(I) 1BTG 59
REMARK 4 1BTG 60
REMARK 4 SOME SIDECHAINS ARE NOT SEEN IN FINAL ELECTRON DENSITY 1BTG 61
REMARK 4 MAP AND HAVE BEEN TRUNCATED TO AN ALA RESIDUE. 1BTG 62
REMARK 4 CHAIN A: LYS 74. 1BTG 63
REMARK 4 CHAIN B: GLU 41, ILE 44, ASN 46, SER 47, GLU 65, LYS 74. 1BTG 64
REMARK 4 CHAIN C: LYS 32, LYS 34, ILE 44, SER 47. 1BTG 65
REMARK 5 1BTG 66
REMARK 5 ALTHOUGH THE N- AND C-TERMINI OF THE A, B, AND C 1BTG 67
REMARK 5 MOLECULES ARE CHARACTERIZED BY HIGH TEMPERATURE FACTORS, 1BTG 68
REMARK 5 THEY ARE SEEN IN OMIT MAPS. 1BTG 69
REMARK 7 1BTG 70
REMARK 6 SITE 1BTG 71
REMARK 6 SITE_IDENTIFIER: ZN2 1BTG 72
REMARK 6 ZN BOUND BETWEEN 2 MOLECULES. 1BTG 73
REMARK 18 1BTG 74
REMARK 18 EXPERIMENTAL DETAILS. 1BTG 75
REMARK 18 DATE OF DATA COLLECTION : JAN-93 1BTG 76
REMARK 18 MONOCHROMATIC (Y/N) : Y 1BTG 77
REMARK 18 LAUE (Y/N) : N 1BTG 78
REMARK 18 WAVELENGTH OR RANGE (A) : 1.54 1BTG 79
REMARK 18 DETECTOR TYPE : MULTIWIRE 1BTG 80
REMARK 18 DETECTOR MANUFACTURER : SDMS 1BTG 81
REMARK 18 INTENSITY-INTEGRATION SOFTWARE : HOWARD ET AL. 1BTG 82
REMARK 18 MERGING R VALUE (INTENSITY) : 0.050 1BTG 83
REMARK 19 1BTG 84
REMARK 19 SOLVENT CONTENT (VS) : 63. % 1BTG 85
REMARK 999 1BTG 86
REMARK 999 FOR CHAIN "A" - 1 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1BTG 87
REMARK 999 1BTG 88
REMARK 999 FOR CHAIN "A" - 1 C-TERMINAL RESIDUES NOT IN ATOMS LIST 1BTG 89
REMARK 999 1BTG 90
REMARK 999 FOR CHAIN "B" - 1 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1BTG 91
REMARK 999 1BTG 92
REMARK 999 FOR CHAIN "C" - 1 N-TERMINAL RESIDUES NOT IN ATOMS LIST 1BTG 93
DBREF 1BTG A 10 117 SWS P01139 NGF_MOUSE 131 238 1BTG 94
DBREF 1BTG B 10 118 SWS P01139 NGF_MOUSE 131 239 1BTG 95
DBREF 1BTG C 10 118 SWS P01139 NGF_MOUSE 131 239 1BTG 96
SEQRES 1 A 110 MET GLY GLU PHE SER VAL CYS ASP SER VAL SER VAL TRP 1BTG 97
SEQRES 2 A 110 VAL GLY ASP LYS THR THR ALA THR ASP ILE LYS GLY LYS 1BTG 98
SEQRES 3 A 110 GLU VAL THR VAL LEU ALA GLU VAL ASN ILE ASN ASN SER 1BTG 99
SEQRES 4 A 110 VAL PHE ARG GLN TYR PHE PHE GLU THR LYS CYS ARG ALA 1BTG 100
SEQRES 5 A 110 SER ASN PRO VAL GLU SER GLY CYS ARG GLY ILE ASP SER 1BTG 101
SEQRES 6 A 110 LYS HIS TRP ASN SER TYR CYS THR THR THR HIS THR PHE 1BTG 102
SEQRES 7 A 110 VAL LYS ALA LEU THR THR ASP GLU LYS GLN ALA ALA TRP 1BTG 103
SEQRES 8 A 110 ARG PHE ILE ARG ILE ASP THR ALA CYS VAL CYS VAL LEU 1BTG 104
SEQRES 9 A 110 SER ARG LYS ALA THR ARG 1BTG 105
SEQRES 1 B 110 MET GLY GLU PHE SER VAL CYS ASP SER VAL SER VAL TRP 1BTG 106
SEQRES 2 B 110 VAL GLY ASP LYS THR THR ALA THR ASP ILE LYS GLY LYS 1BTG 107
SEQRES 3 B 110 GLU VAL THR VAL LEU ALA GLU VAL ASN ILE ASN ASN SER 1BTG 108
SEQRES 4 B 110 VAL PHE ARG GLN TYR PHE PHE GLU THR LYS CYS ARG ALA 1BTG 109
SEQRES 5 B 110 SER ASN PRO VAL GLU SER GLY CYS ARG GLY ILE ASP SER 1BTG 110
SEQRES 6 B 110 LYS HIS TRP ASN SER TYR CYS THR THR THR HIS THR PHE 1BTG 111
SEQRES 7 B 110 VAL LYS ALA LEU THR THR ASP GLU LYS GLN ALA ALA TRP 1BTG 112
SEQRES 8 B 110 ARG PHE ILE ARG ILE ASP THR ALA CYS VAL CYS VAL LEU 1BTG 113
SEQRES 9 B 110 SER ARG LYS ALA THR ARG 1BTG 114
SEQRES 1 C 110 MET GLY GLU PHE SER VAL CYS ASP SER VAL SER VAL TRP 1BTG 115
SEQRES 2 C 110 VAL GLY ASP LYS THR THR ALA THR ASP ILE LYS GLY LYS 1BTG 116
SEQRES 3 C 110 GLU VAL THR VAL LEU ALA GLU VAL ASN ILE ASN ASN SER 1BTG 117
SEQRES 4 C 110 VAL PHE ARG GLN TYR PHE PHE GLU THR LYS CYS ARG ALA 1BTG 118
SEQRES 5 C 110 SER ASN PRO VAL GLU SER GLY CYS ARG GLY ILE ASP SER 1BTG 119
SEQRES 6 C 110 LYS HIS TRP ASN SER TYR CYS THR THR THR HIS THR PHE 1BTG 120
SEQRES 7 C 110 VAL LYS ALA LEU THR THR ASP GLU LYS GLN ALA ALA TRP 1BTG 121
SEQRES 8 C 110 ARG PHE ILE ARG ILE ASP THR ALA CYS VAL CYS VAL LEU 1BTG 122
SEQRES 9 C 110 SER ARG LYS ALA THR ARG 1BTG 123
HET ZN 900 1 ZINC ION 1BTG 124
HET ZN 901 1 ZINC ION 1BTG 125
HET ZN 902 1 ZINC ION 1BTG 126
FORMUL 4 ZN 3(ZN1 2+) 1BTG 127
FORMUL 5 HOH *54(H2 O1) 1BTG 128
SHEET 1 A 2 SER A 17 VAL A 22 0 1BTG 129
SHEET 2 A 2 PHE A 53 CYS A 58 -1 N LYS A 57 O VAL A 18 1BTG 130
SHEET 1 B 2 THR A 27 THR A 29 0 1BTG 131
SHEET 2 B 2 GLU A 35 THR A 37 -1 N VAL A 36 O ALA A 28 1BTG 132
SHEET 1 C 2 GLU A 41 ILE A 44 0 1BTG 133
SHEET 2 C 2 SER A 47 ARG A 50 -1 N PHE A 49 O VAL A 42 1BTG 134
SHEET 1 J 2 TRP A 76 THR A 92 0 1BTG 135
SHEET 2 J 2 ALA A 97 ARG A 114 -1 N SER A 113 O ASN A 77 1BTG 136
SHEET 1 D 2 SER B 17 VAL B 22 0 1BTG 137
SHEET 2 D 2 PHE B 53 CYS B 58 -1 N LYS B 57 O VAL B 18 1BTG 138
SHEET 1 E 2 THR B 27 THR B 29 0 1BTG 139
SHEET 2 E 2 GLU B 35 THR B 37 -1 N VAL B 36 O ALA B 28 1BTG 140
SHEET 1 F 2 GLU B 41 ASN B 43 0 1BTG 141
SHEET 2 F 2 VAL B 48 ARG B 50 -1 N PHE B 49 O VAL B 42 1BTG 142
SHEET 1 K 2 TRP B 76 THR B 92 0 1BTG 143
SHEET 2 K 2 ALA B 97 ARG B 114 -1 N SER B 113 O ASN B 77 1BTG 144
SHEET 1 G 2 SER C 17 VAL C 22 0 1BTG 145
SHEET 2 G 2 PHE C 53 CYS C 58 -1 N LYS C 57 O VAL C 18 1BTG 146
SHEET 1 H 2 THR C 27 THR C 29 0 1BTG 147
SHEET 2 H 2 GLU C 35 THR C 37 -1 N VAL C 36 O ALA C 28 1BTG 148
SHEET 1 I 2 GLU C 41 ASN C 43 0 1BTG 149
SHEET 2 I 2 VAL C 48 ARG C 50 -1 N PHE C 49 O VAL C 42 1BTG 150
SHEET 1 L 2 TRP C 76 THR C 92 0 1BTG 151
SHEET 2 L 2 ALA C 97 ARG C 114 -1 N SER C 113 O ASN C 77 1BTG 152
SSBOND 1 CYS A 15 CYS A 80 1BTG 153
SSBOND 2 CYS A 58 CYS A 108 1BTG 154
SSBOND 3 CYS A 68 CYS A 110 1BTG 155
SSBOND 4 CYS B 15 CYS B 80 1BTG 156
SSBOND 5 CYS B 58 CYS B 108 1BTG 157
SSBOND 6 CYS B 68 CYS B 110 1BTG 158
SSBOND 7 CYS C 15 CYS C 80 1BTG 159
SSBOND 8 CYS C 58 CYS C 108 1BTG 160
SSBOND 9 CYS C 68 CYS C 110 1BTG 161
SITE 1 ZN1 2 VAL C 48 ASP C 105 1BTG 162
SITE 1 ZN2 2 ASP C 105 GLU A 94 1BTG 163
SITE 1 ZN3 2 ASP B 105 HIS B 84 1BTG 164
CRYST1 109.800 93.900 58.900 90.00 123.10 90.00 C 2 12 1BTG 165
ORIGX1 1.000000 0.000000 0.000000 0.00000 1BTG 166
ORIGX2 0.000000 1.000000 0.000000 0.00000 1BTG 167
ORIGX3 0.000000 0.000000 1.000000 0.00000 1BTG 168
SCALE1 0.009107 0.000000 0.005937 0.00000 1BTG 169
SCALE2 0.000000 0.010650 0.000000 0.00000 1BTG 170
SCALE3 0.000000 0.000000 0.020267 0.00000 1BTG 171
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