HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 13-MAR-19 6JMR
TITLE CD98HC EXTRACELLULAR DOMAIN BOUND TO HBJ127 FAB AND MEM-108 FAB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBODY;
COMPND 3 CHAIN: E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ANTIBODY;
COMPND 7 CHAIN: F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: 4F2 CELL-SURFACE ANTIGEN HEAVY CHAIN;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: 4F2HC,4F2 HEAVY CHAIN ANTIGEN,LYMPHOCYTE ACTIVATION ANTIGEN
COMPND 13 4F2 LARGE SUBUNIT,SOLUTE CARRIER FAMILY 3 MEMBER 2;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: ANTIBODY;
COMPND 17 CHAIN: C;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 5;
COMPND 20 MOLECULE: ANTIBODY;
COMPND 21 CHAIN: D;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_TAXID: 10090;
SOURCE 4 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: SLC3A2, MDU1;
SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 MOL_ID: 4;
SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 20 ORGANISM_TAXID: 10090;
SOURCE 21 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 23 MOL_ID: 5;
SOURCE 24 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 25 ORGANISM_TAXID: 10090;
SOURCE 26 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 10090
KEYWDS TRANSPORTER, GLYCOPROTEIN, COMPLEX, MEMBRANE PROTEIN, MEMBRANE
KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.LEE,T.NISHIZAWA,T.KUSAKIZAKO,K.ODA,R.ISHITANI,T.YOKOYAMA,T.NAKANE,
AUTHOR 2 M.SHIROUZU,O.NUREKI
REVDAT 2 29-JUL-20 6JMR 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 19-JUN-19 6JMR 0
JRNL AUTH Y.LEE,P.WIRIYASERMKUL,C.JIN,L.QUAN,R.OHGAKI,S.OKUDA,
JRNL AUTH 2 T.KUSAKIZAKO,T.NISHIZAWA,K.ODA,R.ISHITANI,T.YOKOYAMA,
JRNL AUTH 3 T.NAKANE,M.SHIROUZU,H.ENDOU,S.NAGAMORI,Y.KANAI,O.NUREKI
JRNL TITL CRYO-EM STRUCTURE OF THE HUMAN L-TYPE AMINO ACID TRANSPORTER
JRNL TITL 2 1 IN COMPLEX WITH GLYCOPROTEIN CD98HC.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 26 510 2019
JRNL REFN ESSN 1545-9985
JRNL PMID 31160781
JRNL DOI 10.1038/S41594-019-0237-7
REMARK 2
REMARK 2 RESOLUTION. 4.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.100
REMARK 3 NUMBER OF PARTICLES : 160553
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6JMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1300011392.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : CD98HC EXTRACELLULAR DOMAIN
REMARK 245 BOUND TO MEM-108 FAB AND HBJ127
REMARK 245 FAB
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TECNAI ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 50.20
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, B, C, D, 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 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 ALA E 135
REMARK 465 ALA E 136
REMARK 465 GLN E 137
REMARK 465 THR E 138
REMARK 465 ASN E 139
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 GLU B 2
REMARK 465 LEU B 3
REMARK 465 GLN B 4
REMARK 465 PRO B 5
REMARK 465 PRO B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 SER B 9
REMARK 465 ILE B 10
REMARK 465 ALA B 11
REMARK 465 VAL B 12
REMARK 465 VAL B 13
REMARK 465 SER B 14
REMARK 465 ILE B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 GLN B 18
REMARK 465 LEU B 19
REMARK 465 PRO B 20
REMARK 465 GLY B 21
REMARK 465 SER B 22
REMARK 465 HIS B 23
REMARK 465 SER B 24
REMARK 465 GLU B 25
REMARK 465 ALA B 26
REMARK 465 GLY B 27
REMARK 465 VAL B 28
REMARK 465 GLN B 29
REMARK 465 GLY B 30
REMARK 465 LEU B 31
REMARK 465 SER B 32
REMARK 465 ALA B 33
REMARK 465 GLY B 34
REMARK 465 ASP B 35
REMARK 465 ASP B 36
REMARK 465 SER B 37
REMARK 465 GLU B 38
REMARK 465 LEU B 39
REMARK 465 GLY B 40
REMARK 465 SER B 41
REMARK 465 HIS B 42
REMARK 465 CYS B 43
REMARK 465 VAL B 44
REMARK 465 ALA B 45
REMARK 465 GLN B 46
REMARK 465 THR B 47
REMARK 465 GLY B 48
REMARK 465 LEU B 49
REMARK 465 GLU B 50
REMARK 465 LEU B 51
REMARK 465 LEU B 52
REMARK 465 ALA B 53
REMARK 465 SER B 54
REMARK 465 GLY B 55
REMARK 465 ASP B 56
REMARK 465 PRO B 57
REMARK 465 LEU B 58
REMARK 465 PRO B 59
REMARK 465 SER B 60
REMARK 465 ALA B 61
REMARK 465 SER B 62
REMARK 465 GLN B 63
REMARK 465 ASN B 64
REMARK 465 ALA B 65
REMARK 465 GLU B 66
REMARK 465 MET B 67
REMARK 465 ILE B 68
REMARK 465 GLU B 69
REMARK 465 THR B 70
REMARK 465 GLY B 71
REMARK 465 SER B 72
REMARK 465 ASP B 73
REMARK 465 CYS B 74
REMARK 465 VAL B 75
REMARK 465 THR B 76
REMARK 465 GLN B 77
REMARK 465 ALA B 78
REMARK 465 GLY B 79
REMARK 465 LEU B 80
REMARK 465 GLN B 81
REMARK 465 LEU B 82
REMARK 465 LEU B 83
REMARK 465 ALA B 84
REMARK 465 SER B 85
REMARK 465 SER B 86
REMARK 465 ASP B 87
REMARK 465 PRO B 88
REMARK 465 PRO B 89
REMARK 465 ALA B 90
REMARK 465 LEU B 91
REMARK 465 ALA B 92
REMARK 465 SER B 93
REMARK 465 LYS B 94
REMARK 465 ASN B 95
REMARK 465 ALA B 96
REMARK 465 GLU B 97
REMARK 465 VAL B 98
REMARK 465 THR B 99
REMARK 465 GLY B 100
REMARK 465 THR B 101
REMARK 465 MET B 102
REMARK 465 SER B 103
REMARK 465 GLN B 104
REMARK 465 ASP B 105
REMARK 465 THR B 106
REMARK 465 GLU B 107
REMARK 465 VAL B 108
REMARK 465 ASP B 109
REMARK 465 MET B 110
REMARK 465 LYS B 111
REMARK 465 GLU B 112
REMARK 465 VAL B 113
REMARK 465 GLU B 114
REMARK 465 LEU B 115
REMARK 465 ASN B 116
REMARK 465 GLU B 117
REMARK 465 LEU B 118
REMARK 465 GLU B 119
REMARK 465 PRO B 120
REMARK 465 GLU B 121
REMARK 465 LYS B 122
REMARK 465 GLN B 123
REMARK 465 PRO B 124
REMARK 465 MET B 125
REMARK 465 ASN B 126
REMARK 465 ALA B 127
REMARK 465 ALA B 128
REMARK 465 SER B 129
REMARK 465 GLY B 130
REMARK 465 ALA B 131
REMARK 465 ALA B 132
REMARK 465 MET B 133
REMARK 465 SER B 134
REMARK 465 LEU B 135
REMARK 465 ALA B 136
REMARK 465 GLY B 137
REMARK 465 ALA B 138
REMARK 465 GLU B 139
REMARK 465 LYS B 140
REMARK 465 ASN B 141
REMARK 465 GLY B 142
REMARK 465 LEU B 143
REMARK 465 VAL B 144
REMARK 465 LYS B 145
REMARK 465 ILE B 146
REMARK 465 LYS B 147
REMARK 465 VAL B 148
REMARK 465 ALA B 149
REMARK 465 GLU B 150
REMARK 465 ASP B 151
REMARK 465 GLU B 152
REMARK 465 ALA B 153
REMARK 465 GLU B 154
REMARK 465 ALA B 155
REMARK 465 ALA B 156
REMARK 465 ALA B 157
REMARK 465 ALA B 158
REMARK 465 ALA B 159
REMARK 465 LYS B 160
REMARK 465 PHE B 161
REMARK 465 THR B 162
REMARK 465 GLY B 163
REMARK 465 LEU B 164
REMARK 465 SER B 165
REMARK 465 LYS B 166
REMARK 465 GLU B 167
REMARK 465 GLU B 168
REMARK 465 LEU B 169
REMARK 465 LEU B 170
REMARK 465 LYS B 171
REMARK 465 VAL B 172
REMARK 465 ALA B 173
REMARK 465 GLY B 174
REMARK 465 SER B 175
REMARK 465 PRO B 176
REMARK 465 GLY B 177
REMARK 465 TRP B 178
REMARK 465 VAL B 179
REMARK 465 ARG B 180
REMARK 465 THR B 181
REMARK 465 ARG B 182
REMARK 465 TRP B 183
REMARK 465 ALA B 184
REMARK 465 LEU B 185
REMARK 465 LEU B 186
REMARK 465 LEU B 187
REMARK 465 LEU B 188
REMARK 465 PHE B 189
REMARK 465 TRP B 190
REMARK 465 LEU B 191
REMARK 465 GLY B 192
REMARK 465 TRP B 193
REMARK 465 LEU B 194
REMARK 465 GLY B 195
REMARK 465 MET B 196
REMARK 465 LEU B 197
REMARK 465 ALA B 198
REMARK 465 GLY B 199
REMARK 465 ALA B 200
REMARK 465 VAL B 201
REMARK 465 VAL B 202
REMARK 465 ILE B 203
REMARK 465 ILE B 204
REMARK 465 VAL B 205
REMARK 465 ARG B 206
REMARK 465 ALA B 207
REMARK 465 PRO B 208
REMARK 465 ARG B 209
REMARK 465 UNK C 134
REMARK 465 UNK C 135
REMARK 465 UNK C 136
REMARK 465 UNK C 137
REMARK 465 UNK C 138
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 GLN E 16 -169.87 -129.64
REMARK 500 ASP E 101 -30.76 -130.47
REMARK 500 PRO E 155 -7.79 -44.82
REMARK 500 LEU F 53 -53.98 -122.44
REMARK 500 ALA F 57 -14.59 73.62
REMARK 500 ALA F 90 -166.30 -161.76
REMARK 500 PHE F 103 -179.41 -179.65
REMARK 500 ASN F 143 63.84 63.57
REMARK 500 LEU B 308 17.54 -140.56
REMARK 500 TYR B 312 10.79 -142.32
REMARK 500 GLN B 322 70.44 56.37
REMARK 500 ASP B 355 58.36 35.42
REMARK 500 ASP B 397 36.11 -99.59
REMARK 500 SER B 403 34.28 -99.43
REMARK 500 SER B 410 71.24 57.03
REMARK 500 THR B 411 60.98 67.39
REMARK 500 CYS B 431 -167.08 -125.69
REMARK 500 ALA B 486 83.16 -157.31
REMARK 500 HIS B 538 28.07 -142.43
REMARK 500 ALA B 580 -75.46 -64.06
REMARK 500 SER B 581 10.51 55.55
REMARK 500 LEU B 595 73.99 61.15
REMARK 500 LYS B 615 68.58 60.36
REMARK 500 UNK C 106 -60.67 -91.00
REMARK 500 PHE C 151 47.45 -147.70
REMARK 500 LYS D 18 73.87 60.23
REMARK 500 UNK D 32 49.44 -83.63
REMARK 500 UNK D 57 -7.88 70.13
REMARK 500 UNK D 58 -4.32 -140.14
REMARK 500 ALA D 90 -169.77 -166.48
REMARK 500 ASN D 144 64.36 60.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL E 99 TYR E 100 -147.46
REMARK 500 PRO F 78 LEU F 79 145.35
REMARK 500 THR F 102 PHE F 103 143.79
REMARK 500 TRP B 557 ASP B 558 -138.75
REMARK 500 PHE C 151 PRO C 152 128.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-9850 RELATED DB: EMDB
REMARK 900 STRUCTURE OF A COMPLEX BOUND TO TWO FABS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS DO NOT KNOW THE ACTUAL SEQUENCES OF CHAINS C, D SINCE THE
REMARK 999 PROTEIN WAS DERIVED FROM AN COMMERCIAL ANTIBODY WHOSE SEQUENCE IS
REMARK 999 NOT AVAILABLE.
DBREF 6JMR E 1 220 PDB 6JMR 6JMR 1 220
DBREF 6JMR F 1 218 PDB 6JMR 6JMR 1 218
DBREF 6JMR B 2 630 UNP P08195 4F2_HUMAN 2 630
DBREF 6JMR C 1 219 PDB 6JMR 6JMR 1 219
DBREF 6JMR D 1 219 PDB 6JMR 6JMR 1 219
SEQADV 6JMR GLY B 0 UNP P08195 EXPRESSION TAG
SEQADV 6JMR SER B 1 UNP P08195 EXPRESSION TAG
SEQRES 1 E 220 GLN VAL LYS LEU LEU GLU SER GLY PRO GLY LEU VAL GLN
SEQRES 2 E 220 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 E 220 PHE SER LEU THR THR TYR GLY ILE HIS TRP VAL ARG GLN
SEQRES 4 E 220 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 E 220 SER ASN GLY ARG ILE ASP TYR ASN ALA ALA PHE ILE SER
SEQRES 6 E 220 ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 E 220 PHE PHE LYS MET ASN SER LEU GLN ASP ASP ASP THR ALA
SEQRES 8 E 220 ILE TYR TYR CYS ALA ARG ASN VAL TYR ASP SER LEU THR
SEQRES 9 E 220 TRP PHE THR TYR TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 E 220 SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU
SEQRES 11 E 220 ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR
SEQRES 12 E 220 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL
SEQRES 13 E 220 THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL
SEQRES 14 E 220 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR
SEQRES 15 E 220 LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO
SEQRES 16 E 220 SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER
SEQRES 17 E 220 SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP
SEQRES 1 F 218 ASP ILE GLN MET THR GLN SER PRO SER SER LEU ALA VAL
SEQRES 2 F 218 SER VAL GLY GLU LYS VAL THR MET THR CYS LYS SER SER
SEQRES 3 F 218 GLN SER LEU LEU TYR SER SER ASN GLN LYS ASN TYR LEU
SEQRES 4 F 218 ALA TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU
SEQRES 5 F 218 LEU ILE PHE TRP ALA SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 F 218 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE PRO
SEQRES 7 F 218 LEU THR ILE SER SER VAL LYS ALA GLU ASP LEU ALA VAL
SEQRES 8 F 218 TYR PHE CYS GLN GLN TYR THR SER TYR PRO THR PHE GLY
SEQRES 9 F 218 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA
SEQRES 10 F 218 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU
SEQRES 11 F 218 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN
SEQRES 12 F 218 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP
SEQRES 13 F 218 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR
SEQRES 14 F 218 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER
SEQRES 15 F 218 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN
SEQRES 16 F 218 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER
SEQRES 17 F 218 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU
SEQRES 1 B 631 GLY SER GLU LEU GLN PRO PRO GLU ALA SER ILE ALA VAL
SEQRES 2 B 631 VAL SER ILE PRO ARG GLN LEU PRO GLY SER HIS SER GLU
SEQRES 3 B 631 ALA GLY VAL GLN GLY LEU SER ALA GLY ASP ASP SER GLU
SEQRES 4 B 631 LEU GLY SER HIS CYS VAL ALA GLN THR GLY LEU GLU LEU
SEQRES 5 B 631 LEU ALA SER GLY ASP PRO LEU PRO SER ALA SER GLN ASN
SEQRES 6 B 631 ALA GLU MET ILE GLU THR GLY SER ASP CYS VAL THR GLN
SEQRES 7 B 631 ALA GLY LEU GLN LEU LEU ALA SER SER ASP PRO PRO ALA
SEQRES 8 B 631 LEU ALA SER LYS ASN ALA GLU VAL THR GLY THR MET SER
SEQRES 9 B 631 GLN ASP THR GLU VAL ASP MET LYS GLU VAL GLU LEU ASN
SEQRES 10 B 631 GLU LEU GLU PRO GLU LYS GLN PRO MET ASN ALA ALA SER
SEQRES 11 B 631 GLY ALA ALA MET SER LEU ALA GLY ALA GLU LYS ASN GLY
SEQRES 12 B 631 LEU VAL LYS ILE LYS VAL ALA GLU ASP GLU ALA GLU ALA
SEQRES 13 B 631 ALA ALA ALA ALA LYS PHE THR GLY LEU SER LYS GLU GLU
SEQRES 14 B 631 LEU LEU LYS VAL ALA GLY SER PRO GLY TRP VAL ARG THR
SEQRES 15 B 631 ARG TRP ALA LEU LEU LEU LEU PHE TRP LEU GLY TRP LEU
SEQRES 16 B 631 GLY MET LEU ALA GLY ALA VAL VAL ILE ILE VAL ARG ALA
SEQRES 17 B 631 PRO ARG CYS ARG GLU LEU PRO ALA GLN LYS TRP TRP HIS
SEQRES 18 B 631 THR GLY ALA LEU TYR ARG ILE GLY ASP LEU GLN ALA PHE
SEQRES 19 B 631 GLN GLY HIS GLY ALA GLY ASN LEU ALA GLY LEU LYS GLY
SEQRES 20 B 631 ARG LEU ASP TYR LEU SER SER LEU LYS VAL LYS GLY LEU
SEQRES 21 B 631 VAL LEU GLY PRO ILE HIS LYS ASN GLN LYS ASP ASP VAL
SEQRES 22 B 631 ALA GLN THR ASP LEU LEU GLN ILE ASP PRO ASN PHE GLY
SEQRES 23 B 631 SER LYS GLU ASP PHE ASP SER LEU LEU GLN SER ALA LYS
SEQRES 24 B 631 LYS LYS SER ILE ARG VAL ILE LEU ASP LEU THR PRO ASN
SEQRES 25 B 631 TYR ARG GLY GLU ASN SER TRP PHE SER THR GLN VAL ASP
SEQRES 26 B 631 THR VAL ALA THR LYS VAL LYS ASP ALA LEU GLU PHE TRP
SEQRES 27 B 631 LEU GLN ALA GLY VAL ASP GLY PHE GLN VAL ARG ASP ILE
SEQRES 28 B 631 GLU ASN LEU LYS ASP ALA SER SER PHE LEU ALA GLU TRP
SEQRES 29 B 631 GLN ASN ILE THR LYS GLY PHE SER GLU ASP ARG LEU LEU
SEQRES 30 B 631 ILE ALA GLY THR ASN SER SER ASP LEU GLN GLN ILE LEU
SEQRES 31 B 631 SER LEU LEU GLU SER ASN LYS ASP LEU LEU LEU THR SER
SEQRES 32 B 631 SER TYR LEU SER ASP SER GLY SER THR GLY GLU HIS THR
SEQRES 33 B 631 LYS SER LEU VAL THR GLN TYR LEU ASN ALA THR GLY ASN
SEQRES 34 B 631 ARG TRP CYS SER TRP SER LEU SER GLN ALA ARG LEU LEU
SEQRES 35 B 631 THR SER PHE LEU PRO ALA GLN LEU LEU ARG LEU TYR GLN
SEQRES 36 B 631 LEU MET LEU PHE THR LEU PRO GLY THR PRO VAL PHE SER
SEQRES 37 B 631 TYR GLY ASP GLU ILE GLY LEU ASP ALA ALA ALA LEU PRO
SEQRES 38 B 631 GLY GLN PRO MET GLU ALA PRO VAL MET LEU TRP ASP GLU
SEQRES 39 B 631 SER SER PHE PRO ASP ILE PRO GLY ALA VAL SER ALA ASN
SEQRES 40 B 631 MET THR VAL LYS GLY GLN SER GLU ASP PRO GLY SER LEU
SEQRES 41 B 631 LEU SER LEU PHE ARG ARG LEU SER ASP GLN ARG SER LYS
SEQRES 42 B 631 GLU ARG SER LEU LEU HIS GLY ASP PHE HIS ALA PHE SER
SEQRES 43 B 631 ALA GLY PRO GLY LEU PHE SER TYR ILE ARG HIS TRP ASP
SEQRES 44 B 631 GLN ASN GLU ARG PHE LEU VAL VAL LEU ASN PHE GLY ASP
SEQRES 45 B 631 VAL GLY LEU SER ALA GLY LEU GLN ALA SER ASP LEU PRO
SEQRES 46 B 631 ALA SER ALA SER LEU PRO ALA LYS ALA ASP LEU LEU LEU
SEQRES 47 B 631 SER THR GLN PRO GLY ARG GLU GLU GLY SER PRO LEU GLU
SEQRES 48 B 631 LEU GLU ARG LEU LYS LEU GLU PRO HIS GLU GLY LEU LEU
SEQRES 49 B 631 LEU ARG PHE PRO TYR ALA ALA
SEQRES 1 C 219 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA
SEQRES 2 C 219 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 C 219 PHE PRO LEU THR UNK UNK UNK UNK UNK TRP VAL ARG GLN
SEQRES 4 C 219 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY UNK UNK UNK
SEQRES 5 C 219 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 6 C 219 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 C 219 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR ALA
SEQRES 8 C 219 ARG TYR TYR CYS ALA ARG UNK UNK UNK UNK UNK UNK UNK
SEQRES 9 C 219 UNK UNK UNK TRP GLY GLN GLY THR SER VAL THR VAL SER
SEQRES 10 C 219 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA
SEQRES 11 C 219 PRO GLY SER UNK UNK UNK UNK UNK SER MET VAL THR LEU
SEQRES 12 C 219 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 C 219 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 C 219 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 C 219 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER
SEQRES 16 C 219 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 C 219 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP
SEQRES 1 D 219 ASP ILE VAL MET SER GLN SER PRO SER SER LEU VAL VAL
SEQRES 2 D 219 SER VAL GLY GLU LYS VAL THR MET SER CYS UNK UNK UNK
SEQRES 3 D 219 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 D 219 UNK TRP TYR GLN GLN LYS PRO GLY GLN SER PRO LYS LEU
SEQRES 5 D 219 LEU ILE TYR UNK UNK UNK UNK UNK UNK UNK GLY VAL PRO
SEQRES 6 D 219 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR
SEQRES 7 D 219 LEU THR ILE SER SER VAL LYS ALA GLU ASP LEU ALA VAL
SEQRES 8 D 219 TYR TYR CYS UNK UNK UNK UNK UNK UNK UNK UNK UNK PHE
SEQRES 9 D 219 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA
SEQRES 10 D 219 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN
SEQRES 11 D 219 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN
SEQRES 12 D 219 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE
SEQRES 13 D 219 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP
SEQRES 14 D 219 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER
SEQRES 15 D 219 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS
SEQRES 16 D 219 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR
SEQRES 17 D 219 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU
HET NAG A 1 14
HET NAG A 2 14
HET NAG B 703 14
HET NAG B 704 14
HET NAG B 705 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 6 NAG 5(C8 H15 N O6)
HELIX 1 AA1 SER E 28 TYR E 32 5 5
HELIX 2 AA2 GLN E 86 THR E 90 5 5
HELIX 3 AA3 GLN F 129 SER F 132 5 4
HELIX 4 AA4 LYS F 188 ARG F 193 1 6
HELIX 5 AA5 ASP B 229 GLN B 234 1 6
HELIX 6 AA6 ASN B 240 LEU B 244 5 5
HELIX 7 AA7 GLY B 246 SER B 252 1 7
HELIX 8 AA8 SER B 286 LYS B 298 1 13
HELIX 9 AA9 GLN B 322 ALA B 340 1 19
HELIX 10 AB1 ASP B 355 PHE B 370 1 16
HELIX 11 AB2 ASP B 384 LEU B 389 1 6
HELIX 12 AB3 HIS B 414 THR B 426 1 13
HELIX 13 AB4 TYR B 453 LEU B 460 1 8
HELIX 14 AB5 ASP B 492 PHE B 496 5 5
HELIX 15 AB6 THR B 508 SER B 513 1 6
HELIX 16 AB7 LEU B 519 ARG B 524 1 6
HELIX 17 AB8 LEU B 526 GLU B 533 1 8
HELIX 18 AB9 GLU B 533 GLY B 539 1 7
HELIX 19 AC1 PRO C 28 UNK C 32 5 5
HELIX 20 AC2 UNK C 63 LEU C 67 5 5
HELIX 21 AC3 GLN C 86 THR C 90 5 5
HELIX 22 AC4 SER D 127 SER D 133 1 7
HELIX 23 AC5 LYS D 189 ARG D 194 1 6
SHEET 1 AA1 4 GLU E 6 SER E 7 0
SHEET 2 AA1 4 ILE E 20 THR E 23 -1 O THR E 21 N SER E 7
SHEET 3 AA1 4 GLN E 77 MET E 82 -1 O VAL E 78 N CYS E 22
SHEET 4 AA1 4 LEU E 67 ASP E 72 -1 N THR E 70 O PHE E 79
SHEET 1 AA2 5 LEU E 11 VAL E 12 0
SHEET 2 AA2 5 THR E 113 VAL E 117 1 O THR E 116 N VAL E 12
SHEET 3 AA2 5 ALA E 91 ASN E 98 -1 N TYR E 93 O THR E 113
SHEET 4 AA2 5 ILE E 34 GLN E 39 -1 N GLN E 39 O ILE E 92
SHEET 5 AA2 5 GLU E 46 ILE E 51 -1 O ILE E 51 N ILE E 34
SHEET 1 AA3 4 LEU E 11 VAL E 12 0
SHEET 2 AA3 4 THR E 113 VAL E 117 1 O THR E 116 N VAL E 12
SHEET 3 AA3 4 ALA E 91 ASN E 98 -1 N TYR E 93 O THR E 113
SHEET 4 AA3 4 TRP E 105 TYR E 108 -1 O THR E 107 N ARG E 97
SHEET 1 AA4 4 SER E 126 LEU E 130 0
SHEET 2 AA4 4 MET E 141 TYR E 151 -1 O LEU E 147 N TYR E 128
SHEET 3 AA4 4 LEU E 180 PRO E 190 -1 O TYR E 181 N TYR E 151
SHEET 4 AA4 4 VAL E 169 THR E 171 -1 N HIS E 170 O SER E 186
SHEET 1 AA5 4 SER E 126 LEU E 130 0
SHEET 2 AA5 4 MET E 141 TYR E 151 -1 O LEU E 147 N TYR E 128
SHEET 3 AA5 4 LEU E 180 PRO E 190 -1 O TYR E 181 N TYR E 151
SHEET 4 AA5 4 VAL E 175 GLN E 177 -1 N GLN E 177 O LEU E 180
SHEET 1 AA6 3 THR E 157 TRP E 160 0
SHEET 2 AA6 3 VAL E 199 HIS E 205 -1 O ALA E 204 N THR E 157
SHEET 3 AA6 3 THR E 210 ILE E 216 -1 O LYS E 214 N CYS E 201
SHEET 1 AA7 4 MET F 4 GLN F 6 0
SHEET 2 AA7 4 VAL F 19 SER F 25 -1 O LYS F 24 N THR F 5
SHEET 3 AA7 4 ASP F 76 ILE F 81 -1 O LEU F 79 N MET F 21
SHEET 4 AA7 4 PHE F 68 GLY F 70 -1 N THR F 69 O THR F 80
SHEET 1 AA8 5 SER F 10 ALA F 12 0
SHEET 2 AA8 5 GLY F 106 GLU F 110 1 O GLU F 110 N LEU F 11
SHEET 3 AA8 5 VAL F 91 GLN F 96 -1 N TYR F 92 O THR F 107
SHEET 4 AA8 5 LEU F 39 GLN F 44 -1 N GLN F 44 O VAL F 91
SHEET 5 AA8 5 LYS F 51 PHE F 55 -1 O LYS F 51 N GLN F 43
SHEET 1 AA9 4 THR F 119 PHE F 123 0
SHEET 2 AA9 4 VAL F 138 PHE F 144 -1 O PHE F 140 N SER F 121
SHEET 3 AA9 4 TYR F 178 LEU F 184 -1 O MET F 180 N LEU F 141
SHEET 4 AA9 4 VAL F 164 SER F 167 -1 N LEU F 165 O THR F 183
SHEET 1 AB1 2 GLY F 134 ALA F 135 0
SHEET 2 AB1 2 LEU F 186 THR F 187 -1 O LEU F 186 N ALA F 135
SHEET 1 AB2 4 SER F 158 ARG F 160 0
SHEET 2 AB2 4 ASN F 150 ILE F 155 -1 N ILE F 155 O SER F 158
SHEET 3 AB2 4 SER F 196 THR F 202 -1 O THR F 202 N ASN F 150
SHEET 4 AB2 4 LYS F 212 ASN F 215 -1 O LYS F 212 N CYS F 199
SHEET 1 AB3 5 LEU B 259 LEU B 261 0
SHEET 2 AB3 5 VAL B 304 ASP B 307 1 O ILE B 305 N LEU B 261
SHEET 3 AB3 5 PHE B 345 GLN B 346 1 O GLN B 346 N LEU B 306
SHEET 4 AB3 5 LEU B 376 GLY B 379 1 O ILE B 377 N PHE B 345
SHEET 5 AB3 5 LEU B 400 THR B 401 1 O THR B 401 N ALA B 378
SHEET 1 AB4 2 HIS B 265 ASN B 267 0
SHEET 2 AB4 2 THR B 275 ILE B 280 -1 O GLN B 279 N LYS B 266
SHEET 1 AB5 2 CYS B 431 TRP B 433 0
SHEET 2 AB5 2 GLY B 462 PRO B 464 1 O THR B 463 N TRP B 433
SHEET 1 AB6 5 ASP B 540 HIS B 542 0
SHEET 2 AB6 5 SER B 552 HIS B 556 -1 O ILE B 554 N HIS B 542
SHEET 3 AB6 5 ARG B 562 VAL B 566 -1 O VAL B 565 N TYR B 553
SHEET 4 AB6 5 LEU B 622 PHE B 626 -1 O LEU B 624 N LEU B 564
SHEET 5 AB6 5 LEU B 597 SER B 598 -1 N LEU B 597 O LEU B 623
SHEET 1 AB7 2 LYS B 592 ALA B 593 0
SHEET 2 AB7 2 LEU B 609 GLU B 610 -1 O LEU B 609 N ALA B 593
SHEET 1 AB8 2 GLN C 3 GLU C 6 0
SHEET 2 AB8 2 CYS C 22 SER C 25 -1 O THR C 23 N LYS C 5
SHEET 1 AB9 5 GLY C 10 VAL C 12 0
SHEET 2 AB9 5 THR C 112 VAL C 116 1 O THR C 115 N VAL C 12
SHEET 3 AB9 5 ARG C 92 UNK C 98 -1 N TYR C 93 O THR C 112
SHEET 4 AB9 5 UNK C 33 GLN C 39 -1 N GLN C 39 O ARG C 92
SHEET 5 AB9 5 GLU C 46 UNK C 50 -1 O GLU C 46 N ARG C 38
SHEET 1 AC1 2 LEU C 18 SER C 19 0
SHEET 2 AC1 2 LYS C 81 MET C 82 -1 O MET C 82 N LEU C 18
SHEET 1 AC2 4 SER C 125 LEU C 129 0
SHEET 2 AC2 4 MET C 140 TYR C 150 -1 O LEU C 146 N TYR C 127
SHEET 3 AC2 4 LEU C 179 SER C 183 -1 O TYR C 180 N TYR C 150
SHEET 4 AC2 4 VAL C 174 GLN C 176 -1 N GLN C 176 O LEU C 179
SHEET 1 AC3 3 SER C 125 LEU C 129 0
SHEET 2 AC3 3 MET C 140 TYR C 150 -1 O LEU C 146 N TYR C 127
SHEET 3 AC3 3 VAL C 186 PRO C 189 -1 O VAL C 186 N LEU C 143
SHEET 1 AC4 3 THR C 156 VAL C 157 0
SHEET 2 AC4 3 THR C 199 HIS C 204 -1 O ALA C 203 N THR C 156
SHEET 3 AC4 3 THR C 209 LYS C 214 -1 O VAL C 211 N VAL C 202
SHEET 1 AC5 4 MET D 4 GLN D 6 0
SHEET 2 AC5 4 THR D 20 UNK D 25 -1 O UNK D 24 N SER D 5
SHEET 3 AC5 4 ASP D 76 THR D 80 -1 O LEU D 79 N MET D 21
SHEET 4 AC5 4 SER D 71 SER D 73 -1 N SER D 71 O THR D 78
SHEET 1 AC6 2 SER D 10 SER D 14 0
SHEET 2 AC6 2 LYS D 109 LYS D 113 1 O GLU D 111 N LEU D 11
SHEET 1 AC7 3 LYS D 51 ILE D 54 0
SHEET 2 AC7 3 UNK D 39 GLN D 44 -1 N GLN D 43 O LYS D 51
SHEET 3 AC7 3 VAL D 91 UNK D 96 -1 O TYR D 93 N TYR D 42
SHEET 1 AC8 4 SER D 122 PHE D 124 0
SHEET 2 AC8 4 GLY D 135 PHE D 145 -1 O VAL D 139 N PHE D 124
SHEET 3 AC8 4 TYR D 179 THR D 188 -1 O TYR D 179 N PHE D 145
SHEET 4 AC8 4 VAL D 165 TRP D 169 -1 N SER D 168 O SER D 182
SHEET 1 AC9 4 SER D 159 ARG D 161 0
SHEET 2 AC9 4 ASN D 151 ILE D 156 -1 N ILE D 156 O SER D 159
SHEET 3 AC9 4 SER D 197 THR D 203 -1 O THR D 203 N ASN D 151
SHEET 4 AC9 4 ILE D 211 ASN D 216 -1 O PHE D 215 N TYR D 198
SSBOND 1 CYS E 22 CYS E 95 1555 1555 2.04
SSBOND 2 CYS E 146 CYS E 201 1555 1555 2.03
SSBOND 3 CYS F 23 CYS F 94 1555 1555 2.03
SSBOND 4 CYS F 139 CYS F 199 1555 1555 2.03
SSBOND 5 CYS C 22 CYS C 95 1555 1555 2.03
SSBOND 6 CYS C 145 CYS C 200 1555 1555 2.02
SSBOND 7 CYS D 23 CYS D 94 1555 1555 2.04
SSBOND 8 CYS D 140 CYS D 200 1555 1555 2.02
LINK ND2 ASN B 365 C1 NAG B 705 1555 1555 1.44
LINK ND2 ASN B 381 C1 NAG A 1 1555 1555 1.44
LINK ND2 ASN B 424 C1 NAG B 703 1555 1555 1.46
LINK ND2 ASN B 506 C1 NAG B 704 1555 1555 1.44
LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.47
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 0.003532 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003532 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
