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8j7t.pdb
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HEADER METAL TRANSPORT 28-APR-23 8J7T
TITLE CRYO-EM STRUCTURE OF HZNT7-FAB COMPLEX IN ZINC-UNBOUND STATE,
TITLE 2 DETERMINED IN OUTWARD-FACING CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC TRANSPORTER 7;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ZNT-7,SOLUTE CARRIER FAMILY 30 MEMBER 7,ZNT-LIKE TRANSPORTER
COMPND 5 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LIGHT CHAIN OF YN7114-08 FAB;
COMPND 9 CHAIN: C, D;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HEAVY CHAIN OF YN7114-08 FAB;
COMPND 13 CHAIN: E, F;
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 GENE: SLC30A7, ZNT7, ZNTL2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_TAXID: 10090;
SOURCE 11 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 15 ORGANISM_TAXID: 10090;
SOURCE 16 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10090
KEYWDS ZINC, PROTON, TRANSPORTER, GOLGI APPARATUS, METAL TRANSPORTER,
KEYWDS 2 HISTIDINE-RICH LOOP, METAL TRANSPORT
EXPDTA ELECTRON MICROSCOPY
AUTHOR B.B.HAN,K.INABA,S.WATANABE
REVDAT 1 20-SEP-23 8J7T 0
JRNL AUTH H.B.BUI,S.WATANABE,N.NOMURA,K.LIU,T.UEMURA,M.INOUE,
JRNL AUTH 2 A.TSUTSUMI,H.FUJITA,K.KINOSHITA,Y.KATO,S.IWATA,M.KIKKAWA,
JRNL AUTH 3 K.INABA
JRNL TITL CRYO-EM STRUCTURES OF HUMAN ZINC TRANSPORTER ZNT7 REVEAL THE
JRNL TITL 2 MECHANISM OF ZN 2+ UPTAKE INTO THE GOLGI APPARATUS.
JRNL REF NAT COMMUN V. 14 4770 2023
JRNL REFN ESSN 2041-1723
JRNL PMID 37553324
JRNL DOI 10.1038/S41467-023-40521-5
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.200
REMARK 3 NUMBER OF PARTICLES : 115162
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 8J7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-23.
REMARK 100 THE DEPOSITION ID IS D_1300036922.
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 : HUMAN ZNT7-FAB COMPLEX
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 : 7.50
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 : JEOL CRYO ARM 300
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1700.00
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) : 5000.00
REMARK 245 ILLUMINATION MODE : OTHER
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, F, D, B
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 MET A -13
REMARK 465 GLY A -12
REMARK 465 GLY A -11
REMARK 465 VAL A -10
REMARK 465 ALA A -9
REMARK 465 MET A -8
REMARK 465 PRO A -7
REMARK 465 GLY A -6
REMARK 465 ALA A -5
REMARK 465 GLU A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 VAL A -1
REMARK 465 VAL A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 ILE A 6
REMARK 465 LYS A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 GLU A 10
REMARK 465 TYR A 11
REMARK 465 LYS A 12
REMARK 465 PRO A 13
REMARK 465 PRO A 14
REMARK 465 LYS A 15
REMARK 465 PHE A 16
REMARK 465 ASN A 17
REMARK 465 LEU A 18
REMARK 465 PHE A 19
REMARK 465 GLY A 20
REMARK 465 LYS A 21
REMARK 465 VAL A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 GLU A 139
REMARK 465 HIS A 164
REMARK 465 GLY A 165
REMARK 465 HIS A 166
REMARK 465 SER A 167
REMARK 465 HIS A 168
REMARK 465 GLY A 169
REMARK 465 SER A 170
REMARK 465 GLY A 171
REMARK 465 HIS A 172
REMARK 465 GLY A 173
REMARK 465 HIS A 174
REMARK 465 SER A 175
REMARK 465 HIS A 176
REMARK 465 SER A 177
REMARK 465 LEU A 178
REMARK 465 PHE A 179
REMARK 465 ASN A 180
REMARK 465 GLY A 181
REMARK 465 ALA A 182
REMARK 465 LEU A 183
REMARK 465 ASP A 184
REMARK 465 GLN A 185
REMARK 465 ALA A 186
REMARK 465 HIS A 187
REMARK 465 GLY A 188
REMARK 465 HIS A 189
REMARK 465 VAL A 190
REMARK 465 ASP A 191
REMARK 465 HIS A 192
REMARK 465 CYS A 193
REMARK 465 HIS A 194
REMARK 465 SER A 195
REMARK 465 HIS A 196
REMARK 465 GLU A 197
REMARK 465 VAL A 198
REMARK 465 LYS A 199
REMARK 465 HIS A 200
REMARK 465 GLY A 201
REMARK 465 ALA A 202
REMARK 465 ALA A 203
REMARK 465 HIS A 204
REMARK 465 SER A 205
REMARK 465 HIS A 206
REMARK 465 ASP A 207
REMARK 465 HIS A 208
REMARK 465 ALA A 209
REMARK 465 HIS A 210
REMARK 465 GLY A 211
REMARK 465 HIS A 212
REMARK 465 GLY A 213
REMARK 465 HIS A 214
REMARK 465 PHE A 215
REMARK 465 HIS A 216
REMARK 465 SER A 217
REMARK 465 HIS A 218
REMARK 465 ASP A 219
REMARK 465 GLY A 220
REMARK 465 PRO A 221
REMARK 465 SER A 222
REMARK 465 LEU A 223
REMARK 465 LYS A 224
REMARK 465 GLU A 225
REMARK 465 THR A 226
REMARK 465 THR A 227
REMARK 465 GLY A 228
REMARK 465 ASN C 216
REMARK 465 GLU C 217
REMARK 465 CYS C 218
REMARK 465 ASP E 219
REMARK 465 CYS E 220
REMARK 465 GLY E 221
REMARK 465 CYS E 222
REMARK 465 LYS E 223
REMARK 465 PRO E 224
REMARK 465 CYS E 225
REMARK 465 ILE E 226
REMARK 465 CYS E 227
REMARK 465 THR E 228
REMARK 465 VAL E 229
REMARK 465 PRO E 230
REMARK 465 GLU E 231
REMARK 465 VAL E 232
REMARK 465 SER E 233
REMARK 465 SER E 234
REMARK 465 ASP F 219
REMARK 465 CYS F 220
REMARK 465 GLY F 221
REMARK 465 CYS F 222
REMARK 465 LYS F 223
REMARK 465 PRO F 224
REMARK 465 CYS F 225
REMARK 465 ILE F 226
REMARK 465 CYS F 227
REMARK 465 THR F 228
REMARK 465 VAL F 229
REMARK 465 PRO F 230
REMARK 465 GLU F 231
REMARK 465 VAL F 232
REMARK 465 SER F 233
REMARK 465 SER F 234
REMARK 465 ASN D 216
REMARK 465 GLU D 217
REMARK 465 CYS D 218
REMARK 465 MET B -13
REMARK 465 GLY B -12
REMARK 465 GLY B -11
REMARK 465 VAL B -10
REMARK 465 ALA B -9
REMARK 465 MET B -8
REMARK 465 PRO B -7
REMARK 465 GLY B -6
REMARK 465 ALA B -5
REMARK 465 GLU B -4
REMARK 465 ASP B -3
REMARK 465 ASP B -2
REMARK 465 VAL B -1
REMARK 465 VAL B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 PRO B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 ILE B 6
REMARK 465 LYS B 7
REMARK 465 ASP B 8
REMARK 465 ASP B 9
REMARK 465 GLU B 10
REMARK 465 TYR B 11
REMARK 465 LYS B 12
REMARK 465 PRO B 13
REMARK 465 PRO B 14
REMARK 465 LYS B 15
REMARK 465 PHE B 16
REMARK 465 ASN B 17
REMARK 465 LEU B 18
REMARK 465 PHE B 19
REMARK 465 GLY B 20
REMARK 465 LYS B 21
REMARK 465 VAL B 136
REMARK 465 HIS B 137
REMARK 465 HIS B 138
REMARK 465 GLU B 139
REMARK 465 HIS B 164
REMARK 465 GLY B 165
REMARK 465 HIS B 166
REMARK 465 SER B 167
REMARK 465 HIS B 168
REMARK 465 GLY B 169
REMARK 465 SER B 170
REMARK 465 GLY B 171
REMARK 465 HIS B 172
REMARK 465 GLY B 173
REMARK 465 HIS B 174
REMARK 465 SER B 175
REMARK 465 HIS B 176
REMARK 465 SER B 177
REMARK 465 LEU B 178
REMARK 465 PHE B 179
REMARK 465 ASN B 180
REMARK 465 GLY B 181
REMARK 465 ALA B 182
REMARK 465 LEU B 183
REMARK 465 ASP B 184
REMARK 465 GLN B 185
REMARK 465 ALA B 186
REMARK 465 HIS B 187
REMARK 465 GLY B 188
REMARK 465 HIS B 189
REMARK 465 VAL B 190
REMARK 465 ASP B 191
REMARK 465 HIS B 192
REMARK 465 CYS B 193
REMARK 465 HIS B 194
REMARK 465 SER B 195
REMARK 465 HIS B 196
REMARK 465 GLU B 197
REMARK 465 VAL B 198
REMARK 465 LYS B 199
REMARK 465 HIS B 200
REMARK 465 GLY B 201
REMARK 465 ALA B 202
REMARK 465 ALA B 203
REMARK 465 HIS B 204
REMARK 465 SER B 205
REMARK 465 HIS B 206
REMARK 465 ASP B 207
REMARK 465 HIS B 208
REMARK 465 ALA B 209
REMARK 465 HIS B 210
REMARK 465 GLY B 211
REMARK 465 HIS B 212
REMARK 465 GLY B 213
REMARK 465 HIS B 214
REMARK 465 PHE B 215
REMARK 465 HIS B 216
REMARK 465 SER B 217
REMARK 465 HIS B 218
REMARK 465 ASP B 219
REMARK 465 GLY B 220
REMARK 465 PRO B 221
REMARK 465 SER B 222
REMARK 465 LEU B 223
REMARK 465 LYS B 224
REMARK 465 GLU B 225
REMARK 465 THR B 226
REMARK 465 THR B 227
REMARK 465 GLY B 228
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 ASN A 60 47.98 35.56
REMARK 500 PHE C 36 58.84 -96.58
REMARK 500 ALA C 55 -12.55 72.93
REMARK 500 ARG C 72 -96.19 59.15
REMARK 500 SER E 133 -153.87 57.85
REMARK 500 ASN E 138 -165.94 54.97
REMARK 500 SER F 133 -153.88 57.86
REMARK 500 ASN F 138 -165.96 55.00
REMARK 500 PHE D 36 58.89 -96.58
REMARK 500 ALA D 55 -12.54 72.97
REMARK 500 ARG D 72 -96.25 59.21
REMARK 500 ASN B 60 47.97 35.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-36048 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HZNT7-FAB COMPLEX IN ZINC-UNBOUND STATE,
REMARK 900 DETERMINED IN OUTWARD-FACING CONFORMATION
DBREF 8J7T A 1 376 UNP Q8NEW0 ZNT7_HUMAN 1 376
DBREF 8J7T C 1 218 PDB 8J7T 8J7T 1 218
DBREF 8J7T E 1 234 PDB 8J7T 8J7T 1 234
DBREF 8J7T F 1 234 PDB 8J7T 8J7T 1 234
DBREF 8J7T D 1 218 PDB 8J7T 8J7T 1 218
DBREF 8J7T B 1 376 UNP Q8NEW0 ZNT7_HUMAN 1 376
SEQADV 8J7T MET A -13 UNP Q8NEW0 INITIATING METHIONINE
SEQADV 8J7T GLY A -12 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T GLY A -11 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T VAL A -10 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ALA A -9 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T MET A -8 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T PRO A -7 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T GLY A -6 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ALA A -5 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T GLU A -4 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ASP A -3 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ASP A -2 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T VAL A -1 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T VAL A 0 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T MET B -13 UNP Q8NEW0 INITIATING METHIONINE
SEQADV 8J7T GLY B -12 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T GLY B -11 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T VAL B -10 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ALA B -9 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T MET B -8 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T PRO B -7 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T GLY B -6 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ALA B -5 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T GLU B -4 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ASP B -3 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T ASP B -2 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T VAL B -1 UNP Q8NEW0 EXPRESSION TAG
SEQADV 8J7T VAL B 0 UNP Q8NEW0 EXPRESSION TAG
SEQRES 1 A 390 MET GLY GLY VAL ALA MET PRO GLY ALA GLU ASP ASP VAL
SEQRES 2 A 390 VAL MET LEU PRO LEU SER ILE LYS ASP ASP GLU TYR LYS
SEQRES 3 A 390 PRO PRO LYS PHE ASN LEU PHE GLY LYS ILE SER GLY TRP
SEQRES 4 A 390 PHE ARG SER ILE LEU SER ASP LYS THR SER ARG ASN LEU
SEQRES 5 A 390 PHE PHE PHE LEU CYS LEU ASN LEU SER PHE ALA PHE VAL
SEQRES 6 A 390 GLU LEU LEU TYR GLY ILE TRP SER ASN CYS LEU GLY LEU
SEQRES 7 A 390 ILE SER ASP SER PHE HIS MET PHE PHE ASP SER THR ALA
SEQRES 8 A 390 ILE LEU ALA GLY LEU ALA ALA SER VAL ILE SER LYS TRP
SEQRES 9 A 390 ARG ASP ASN ASP ALA PHE SER TYR GLY TYR VAL ARG ALA
SEQRES 10 A 390 GLU VAL LEU ALA GLY PHE VAL ASN GLY LEU PHE LEU ILE
SEQRES 11 A 390 PHE THR ALA PHE PHE ILE PHE SER GLU GLY VAL GLU ARG
SEQRES 12 A 390 ALA LEU ALA PRO PRO ASP VAL HIS HIS GLU ARG LEU LEU
SEQRES 13 A 390 LEU VAL SER ILE LEU GLY PHE VAL VAL ASN LEU ILE GLY
SEQRES 14 A 390 ILE PHE VAL PHE LYS HIS GLY GLY HIS GLY HIS SER HIS
SEQRES 15 A 390 GLY SER GLY HIS GLY HIS SER HIS SER LEU PHE ASN GLY
SEQRES 16 A 390 ALA LEU ASP GLN ALA HIS GLY HIS VAL ASP HIS CYS HIS
SEQRES 17 A 390 SER HIS GLU VAL LYS HIS GLY ALA ALA HIS SER HIS ASP
SEQRES 18 A 390 HIS ALA HIS GLY HIS GLY HIS PHE HIS SER HIS ASP GLY
SEQRES 19 A 390 PRO SER LEU LYS GLU THR THR GLY PRO SER ARG GLN ILE
SEQRES 20 A 390 LEU GLN GLY VAL PHE LEU HIS ILE LEU ALA ASP THR LEU
SEQRES 21 A 390 GLY SER ILE GLY VAL ILE ALA SER ALA ILE MET MET GLN
SEQRES 22 A 390 ASN PHE GLY LEU MET ILE ALA ASP PRO ILE CYS SER ILE
SEQRES 23 A 390 LEU ILE ALA ILE LEU ILE VAL VAL SER VAL ILE PRO LEU
SEQRES 24 A 390 LEU ARG GLU SER VAL GLY ILE LEU MET GLN ARG THR PRO
SEQRES 25 A 390 PRO LEU LEU GLU ASN SER LEU PRO GLN CYS TYR GLN ARG
SEQRES 26 A 390 VAL GLN GLN LEU GLN GLY VAL TYR SER LEU GLN GLU GLN
SEQRES 27 A 390 HIS PHE TRP THR LEU CYS SER ASP VAL TYR VAL GLY THR
SEQRES 28 A 390 LEU LYS LEU ILE VAL ALA PRO ASP ALA ASP ALA ARG TRP
SEQRES 29 A 390 ILE LEU SER GLN THR HIS ASN ILE PHE THR GLN ALA GLY
SEQRES 30 A 390 VAL ARG GLN LEU TYR VAL GLN ILE ASP PHE ALA ALA MET
SEQRES 1 C 218 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL
SEQRES 2 C 218 SER LEU ARG ARG ARG ALA THR ILE SER CYS ARG ALA SER
SEQRES 3 C 218 GLU SER VAL ASP GLY TYR GLY HIS SER PHE MET HIS TRP
SEQRES 4 C 218 TYR GLN GLN LYS SER GLY GLN PRO PRO LYS LEU LEU ILE
SEQRES 5 C 218 TYR ARG ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG
SEQRES 6 C 218 PHE SER GLY SER GLY SER ARG THR ASP PHE THR LEU THR
SEQRES 7 C 218 ILE ASP PRO VAL GLU ALA ASP ASP ALA ALA THR TYR TYR
SEQRES 8 C 218 CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY SER
SEQRES 9 C 218 GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO
SEQRES 10 C 218 THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR
SEQRES 11 C 218 SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE
SEQRES 12 C 218 TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY
SEQRES 13 C 218 SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP
SEQRES 14 C 218 GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR
SEQRES 15 C 218 LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER
SEQRES 16 C 218 TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO
SEQRES 17 C 218 ILE VAL LYS SER PHE ASN ARG ASN GLU CYS
SEQRES 1 E 234 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ALA
SEQRES 2 E 234 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 E 234 PHE SER LEU THR ASN TYR ALA VAL HIS TRP VAL ARG GLN
SEQRES 4 E 234 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 E 234 SER ASN GLY ARG THR ASP TYR ASN ALA ALA PHE ILE SER
SEQRES 6 E 234 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 E 234 PHE PHE LYS MET ASN SER LEU GLN ALA ASP ASP THR ALA
SEQRES 8 E 234 ILE TYR TYR CYS ALA ARG LYS LEU ALA TYR GLU GLY ALA
SEQRES 9 E 234 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER
SEQRES 10 E 234 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA
SEQRES 11 E 234 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU
SEQRES 12 E 234 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 E 234 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 E 234 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 E 234 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER
SEQRES 16 E 234 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 E 234 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY
SEQRES 18 E 234 CYS LYS PRO CYS ILE CYS THR VAL PRO GLU VAL SER SER
SEQRES 1 F 234 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ALA
SEQRES 2 F 234 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY
SEQRES 3 F 234 PHE SER LEU THR ASN TYR ALA VAL HIS TRP VAL ARG GLN
SEQRES 4 F 234 SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP
SEQRES 5 F 234 SER ASN GLY ARG THR ASP TYR ASN ALA ALA PHE ILE SER
SEQRES 6 F 234 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL
SEQRES 7 F 234 PHE PHE LYS MET ASN SER LEU GLN ALA ASP ASP THR ALA
SEQRES 8 F 234 ILE TYR TYR CYS ALA ARG LYS LEU ALA TYR GLU GLY ALA
SEQRES 9 F 234 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER
SEQRES 10 F 234 SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA
SEQRES 11 F 234 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU
SEQRES 12 F 234 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 F 234 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 F 234 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 F 234 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER
SEQRES 16 F 234 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 F 234 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY
SEQRES 18 F 234 CYS LYS PRO CYS ILE CYS THR VAL PRO GLU VAL SER SER
SEQRES 1 D 218 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL
SEQRES 2 D 218 SER LEU ARG ARG ARG ALA THR ILE SER CYS ARG ALA SER
SEQRES 3 D 218 GLU SER VAL ASP GLY TYR GLY HIS SER PHE MET HIS TRP
SEQRES 4 D 218 TYR GLN GLN LYS SER GLY GLN PRO PRO LYS LEU LEU ILE
SEQRES 5 D 218 TYR ARG ALA SER ASN LEU GLU SER GLY VAL PRO ALA ARG
SEQRES 6 D 218 PHE SER GLY SER GLY SER ARG THR ASP PHE THR LEU THR
SEQRES 7 D 218 ILE ASP PRO VAL GLU ALA ASP ASP ALA ALA THR TYR TYR
SEQRES 8 D 218 CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY SER
SEQRES 9 D 218 GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO
SEQRES 10 D 218 THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR
SEQRES 11 D 218 SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE
SEQRES 12 D 218 TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY
SEQRES 13 D 218 SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP
SEQRES 14 D 218 GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR
SEQRES 15 D 218 LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER
SEQRES 16 D 218 TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO
SEQRES 17 D 218 ILE VAL LYS SER PHE ASN ARG ASN GLU CYS
SEQRES 1 B 390 MET GLY GLY VAL ALA MET PRO GLY ALA GLU ASP ASP VAL
SEQRES 2 B 390 VAL MET LEU PRO LEU SER ILE LYS ASP ASP GLU TYR LYS
SEQRES 3 B 390 PRO PRO LYS PHE ASN LEU PHE GLY LYS ILE SER GLY TRP
SEQRES 4 B 390 PHE ARG SER ILE LEU SER ASP LYS THR SER ARG ASN LEU
SEQRES 5 B 390 PHE PHE PHE LEU CYS LEU ASN LEU SER PHE ALA PHE VAL
SEQRES 6 B 390 GLU LEU LEU TYR GLY ILE TRP SER ASN CYS LEU GLY LEU
SEQRES 7 B 390 ILE SER ASP SER PHE HIS MET PHE PHE ASP SER THR ALA
SEQRES 8 B 390 ILE LEU ALA GLY LEU ALA ALA SER VAL ILE SER LYS TRP
SEQRES 9 B 390 ARG ASP ASN ASP ALA PHE SER TYR GLY TYR VAL ARG ALA
SEQRES 10 B 390 GLU VAL LEU ALA GLY PHE VAL ASN GLY LEU PHE LEU ILE
SEQRES 11 B 390 PHE THR ALA PHE PHE ILE PHE SER GLU GLY VAL GLU ARG
SEQRES 12 B 390 ALA LEU ALA PRO PRO ASP VAL HIS HIS GLU ARG LEU LEU
SEQRES 13 B 390 LEU VAL SER ILE LEU GLY PHE VAL VAL ASN LEU ILE GLY
SEQRES 14 B 390 ILE PHE VAL PHE LYS HIS GLY GLY HIS GLY HIS SER HIS
SEQRES 15 B 390 GLY SER GLY HIS GLY HIS SER HIS SER LEU PHE ASN GLY
SEQRES 16 B 390 ALA LEU ASP GLN ALA HIS GLY HIS VAL ASP HIS CYS HIS
SEQRES 17 B 390 SER HIS GLU VAL LYS HIS GLY ALA ALA HIS SER HIS ASP
SEQRES 18 B 390 HIS ALA HIS GLY HIS GLY HIS PHE HIS SER HIS ASP GLY
SEQRES 19 B 390 PRO SER LEU LYS GLU THR THR GLY PRO SER ARG GLN ILE
SEQRES 20 B 390 LEU GLN GLY VAL PHE LEU HIS ILE LEU ALA ASP THR LEU
SEQRES 21 B 390 GLY SER ILE GLY VAL ILE ALA SER ALA ILE MET MET GLN
SEQRES 22 B 390 ASN PHE GLY LEU MET ILE ALA ASP PRO ILE CYS SER ILE
SEQRES 23 B 390 LEU ILE ALA ILE LEU ILE VAL VAL SER VAL ILE PRO LEU
SEQRES 24 B 390 LEU ARG GLU SER VAL GLY ILE LEU MET GLN ARG THR PRO
SEQRES 25 B 390 PRO LEU LEU GLU ASN SER LEU PRO GLN CYS TYR GLN ARG
SEQRES 26 B 390 VAL GLN GLN LEU GLN GLY VAL TYR SER LEU GLN GLU GLN
SEQRES 27 B 390 HIS PHE TRP THR LEU CYS SER ASP VAL TYR VAL GLY THR
SEQRES 28 B 390 LEU LYS LEU ILE VAL ALA PRO ASP ALA ASP ALA ARG TRP
SEQRES 29 B 390 ILE LEU SER GLN THR HIS ASN ILE PHE THR GLN ALA GLY
SEQRES 30 B 390 VAL ARG GLN LEU TYR VAL GLN ILE ASP PHE ALA ALA MET
HELIX 1 AA1 ILE A 22 ASP A 32 1 11
HELIX 2 AA2 ASP A 32 SER A 59 1 28
HELIX 3 AA3 LEU A 62 LYS A 89 1 28
HELIX 4 AA4 VAL A 101 LEU A 131 1 31
HELIX 5 AA5 LEU A 142 PHE A 159 1 18
HELIX 6 AA6 SER A 230 PHE A 261 1 32
HELIX 7 AA7 ILE A 265 MET A 294 1 30
HELIX 8 AA8 PRO A 298 ASN A 303 1 6
HELIX 9 AA9 SER A 304 GLN A 314 1 11
HELIX 10 AB1 ASP A 347 ALA A 362 1 16
HELIX 11 AB2 GLU C 83 ALA C 87 5 5
HELIX 12 AB3 SER C 125 GLY C 132 1 8
HELIX 13 AB4 LYS C 187 ARG C 192 1 6
HELIX 14 AB5 ALA E 61 ILE E 64 5 4
HELIX 15 AB6 GLN E 86 THR E 90 5 5
HELIX 16 AB7 SER E 161 SER E 163 5 3
HELIX 17 AB8 SER E 191 TRP E 193 5 3
HELIX 18 AB9 ALA F 61 ILE F 64 5 4
HELIX 19 AC1 GLN F 86 THR F 90 5 5
HELIX 20 AC2 SER F 161 SER F 163 5 3
HELIX 21 AC3 SER F 191 TRP F 193 5 3
HELIX 22 AC4 GLU D 83 ALA D 87 5 5
HELIX 23 AC5 SER D 125 GLY D 132 1 8
HELIX 24 AC6 LYS D 187 ARG D 192 1 6
HELIX 25 AC7 SER B 23 ASP B 32 1 10
HELIX 26 AC8 ASP B 32 SER B 59 1 28
HELIX 27 AC9 LEU B 62 LYS B 89 1 28
HELIX 28 AD1 VAL B 101 LEU B 131 1 31
HELIX 29 AD2 LEU B 142 PHE B 159 1 18
HELIX 30 AD3 SER B 230 PHE B 261 1 32
HELIX 31 AD4 ILE B 265 MET B 294 1 30
HELIX 32 AD5 PRO B 298 ASN B 303 1 6
HELIX 33 AD6 SER B 304 GLN B 314 1 11
HELIX 34 AD7 ASP B 347 ALA B 362 1 16
SHEET 1 AA1 3 VAL A 318 CYS A 330 0
SHEET 2 AA1 3 VAL A 333 VAL A 342 -1 O ILE A 341 N TYR A 319
SHEET 3 AA1 3 GLN A 366 PHE A 373 1 O GLN A 370 N LEU A 340
SHEET 1 AA2 4 LEU C 4 SER C 7 0
SHEET 2 AA2 4 ALA C 19 ALA C 25 -1 O ARG C 24 N THR C 5
SHEET 3 AA2 4 ASP C 74 ILE C 79 -1 O LEU C 77 N ILE C 21
SHEET 4 AA2 4 PHE C 66 SER C 71 -1 N SER C 69 O THR C 76
SHEET 1 AA3 6 SER C 10 SER C 14 0
SHEET 2 AA3 6 THR C 106 LYS C 111 1 O LYS C 111 N VAL C 13
SHEET 3 AA3 6 THR C 89 GLN C 94 -1 N TYR C 90 O THR C 106
SHEET 4 AA3 6 MET C 37 GLN C 42 -1 N GLN C 42 O THR C 89
SHEET 5 AA3 6 LYS C 49 TYR C 53 -1 O LYS C 49 N GLN C 41
SHEET 6 AA3 6 ASN C 57 LEU C 58 -1 O ASN C 57 N TYR C 53
SHEET 1 AA4 4 SER C 10 SER C 14 0
SHEET 2 AA4 4 THR C 106 LYS C 111 1 O LYS C 111 N VAL C 13
SHEET 3 AA4 4 THR C 89 GLN C 94 -1 N TYR C 90 O THR C 106
SHEET 4 AA4 4 THR C 101 PHE C 102 -1 O THR C 101 N GLN C 94
SHEET 1 AA5 2 ASP C 30 GLY C 31 0
SHEET 2 AA5 2 HIS C 34 SER C 35 -1 O HIS C 34 N GLY C 31
SHEET 1 AA6 4 THR C 118 PHE C 122 0
SHEET 2 AA6 4 GLY C 133 PHE C 143 -1 O PHE C 139 N SER C 120
SHEET 3 AA6 4 TYR C 177 THR C 186 -1 O SER C 181 N CYS C 138
SHEET 4 AA6 4 VAL C 163 TRP C 167 -1 N LEU C 164 O THR C 182
SHEET 1 AA7 4 SER C 157 ARG C 159 0
SHEET 2 AA7 4 ASN C 149 ILE C 154 -1 N ILE C 154 O SER C 157
SHEET 3 AA7 4 TYR C 196 HIS C 202 -1 O THR C 197 N LYS C 153
SHEET 4 AA7 4 SER C 205 PHE C 213 -1 O LYS C 211 N CYS C 198
SHEET 1 AA8 4 GLN E 3 SER E 7 0
SHEET 2 AA8 4 LEU E 18 SER E 25 -1 O THR E 21 N SER E 7
SHEET 3 AA8 4 GLN E 77 MET E 82 -1 O PHE E 80 N ILE E 20
SHEET 4 AA8 4 LEU E 67 ASP E 72 -1 N ASP E 72 O GLN E 77
SHEET 1 AA9 6 LEU E 11 VAL E 12 0
SHEET 2 AA9 6 THR E 112 VAL E 116 1 O THR E 115 N VAL E 12
SHEET 3 AA9 6 ALA E 91 LYS E 98 -1 N ALA E 91 O VAL E 114
SHEET 4 AA9 6 VAL E 34 SER E 40 -1 N VAL E 37 O TYR E 94
SHEET 5 AA9 6 GLY E 44 ILE E 51 -1 O GLU E 46 N ARG E 38
SHEET 6 AA9 6 THR E 57 TYR E 59 -1 O ASP E 58 N VAL E 50
SHEET 1 AB1 4 LEU E 11 VAL E 12 0
SHEET 2 AB1 4 THR E 112 VAL E 116 1 O THR E 115 N VAL E 12
SHEET 3 AB1 4 ALA E 91 LYS E 98 -1 N ALA E 91 O VAL E 114
SHEET 4 AB1 4 MET E 105 TRP E 108 -1 O TYR E 107 N ARG E 97
SHEET 1 AB2 4 SER E 125 LEU E 129 0
SHEET 2 AB2 4 MET E 140 TYR E 150 -1 O LEU E 146 N TYR E 127
SHEET 3 AB2 4 LEU E 179 PRO E 189 -1 O VAL E 188 N VAL E 141
SHEET 4 AB2 4 VAL E 168 THR E 170 -1 N HIS E 169 O SER E 185
SHEET 1 AB3 4 SER E 125 LEU E 129 0
SHEET 2 AB3 4 MET E 140 TYR E 150 -1 O LEU E 146 N TYR E 127
SHEET 3 AB3 4 LEU E 179 PRO E 189 -1 O VAL E 188 N VAL E 141
SHEET 4 AB3 4 VAL E 174 GLN E 176 -1 N GLN E 176 O LEU E 179
SHEET 1 AB4 3 THR E 156 TRP E 159 0
SHEET 2 AB4 3 THR E 199 HIS E 204 -1 O ASN E 201 N THR E 158
SHEET 3 AB4 3 THR E 209 LYS E 214 -1 O THR E 209 N HIS E 204
SHEET 1 AB5 4 GLN F 3 SER F 7 0
SHEET 2 AB5 4 LEU F 18 SER F 25 -1 O THR F 21 N SER F 7
SHEET 3 AB5 4 GLN F 77 MET F 82 -1 O PHE F 80 N ILE F 20
SHEET 4 AB5 4 LEU F 67 ASP F 72 -1 N ASP F 72 O GLN F 77
SHEET 1 AB6 6 LEU F 11 VAL F 12 0
SHEET 2 AB6 6 THR F 112 VAL F 116 1 O THR F 115 N VAL F 12
SHEET 3 AB6 6 ALA F 91 LYS F 98 -1 N ALA F 91 O VAL F 114
SHEET 4 AB6 6 VAL F 34 SER F 40 -1 N VAL F 37 O TYR F 94
SHEET 5 AB6 6 GLY F 44 ILE F 51 -1 O GLU F 46 N ARG F 38
SHEET 6 AB6 6 THR F 57 TYR F 59 -1 O ASP F 58 N VAL F 50
SHEET 1 AB7 4 LEU F 11 VAL F 12 0
SHEET 2 AB7 4 THR F 112 VAL F 116 1 O THR F 115 N VAL F 12
SHEET 3 AB7 4 ALA F 91 LYS F 98 -1 N ALA F 91 O VAL F 114
SHEET 4 AB7 4 MET F 105 TRP F 108 -1 O TYR F 107 N ARG F 97
SHEET 1 AB8 4 SER F 125 LEU F 129 0
SHEET 2 AB8 4 MET F 140 TYR F 150 -1 O LEU F 146 N TYR F 127
SHEET 3 AB8 4 LEU F 179 PRO F 189 -1 O VAL F 188 N VAL F 141
SHEET 4 AB8 4 VAL F 168 THR F 170 -1 N HIS F 169 O SER F 185
SHEET 1 AB9 4 SER F 125 LEU F 129 0
SHEET 2 AB9 4 MET F 140 TYR F 150 -1 O LEU F 146 N TYR F 127
SHEET 3 AB9 4 LEU F 179 PRO F 189 -1 O VAL F 188 N VAL F 141
SHEET 4 AB9 4 VAL F 174 GLN F 176 -1 N GLN F 176 O LEU F 179
SHEET 1 AC1 3 THR F 156 TRP F 159 0
SHEET 2 AC1 3 THR F 199 HIS F 204 -1 O ASN F 201 N THR F 158
SHEET 3 AC1 3 THR F 209 LYS F 214 -1 O THR F 209 N HIS F 204
SHEET 1 AC2 4 LEU D 4 SER D 7 0
SHEET 2 AC2 4 ALA D 19 ALA D 25 -1 O ARG D 24 N THR D 5
SHEET 3 AC2 4 ASP D 74 ILE D 79 -1 O PHE D 75 N CYS D 23
SHEET 4 AC2 4 PHE D 66 SER D 71 -1 N SER D 69 O THR D 76
SHEET 1 AC3 6 SER D 10 SER D 14 0
SHEET 2 AC3 6 THR D 106 LYS D 111 1 O LYS D 111 N VAL D 13
SHEET 3 AC3 6 THR D 89 GLN D 94 -1 N TYR D 90 O THR D 106
SHEET 4 AC3 6 MET D 37 GLN D 42 -1 N GLN D 42 O THR D 89
SHEET 5 AC3 6 LYS D 49 TYR D 53 -1 O LYS D 49 N GLN D 41
SHEET 6 AC3 6 ASN D 57 LEU D 58 -1 O ASN D 57 N TYR D 53
SHEET 1 AC4 4 SER D 10 SER D 14 0
SHEET 2 AC4 4 THR D 106 LYS D 111 1 O LYS D 111 N VAL D 13
SHEET 3 AC4 4 THR D 89 GLN D 94 -1 N TYR D 90 O THR D 106
SHEET 4 AC4 4 THR D 101 PHE D 102 -1 O THR D 101 N GLN D 94
SHEET 1 AC5 2 ASP D 30 GLY D 31 0
SHEET 2 AC5 2 HIS D 34 SER D 35 -1 O HIS D 34 N GLY D 31
SHEET 1 AC6 4 THR D 118 PHE D 122 0
SHEET 2 AC6 4 GLY D 133 PHE D 143 -1 O PHE D 139 N SER D 120
SHEET 3 AC6 4 TYR D 177 THR D 186 -1 O SER D 181 N CYS D 138
SHEET 4 AC6 4 VAL D 163 TRP D 167 -1 N LEU D 164 O THR D 182
SHEET 1 AC7 4 SER D 157 ARG D 159 0
SHEET 2 AC7 4 ASN D 149 ILE D 154 -1 N ILE D 154 O SER D 157
SHEET 3 AC7 4 TYR D 196 HIS D 202 -1 O THR D 197 N LYS D 153
SHEET 4 AC7 4 SER D 205 PHE D 213 -1 O LYS D 211 N CYS D 198
SHEET 1 AC8 3 VAL B 318 CYS B 330 0
SHEET 2 AC8 3 VAL B 333 VAL B 342 -1 O ILE B 341 N TYR B 319
SHEET 3 AC8 3 GLN B 366 PHE B 373 1 O GLN B 370 N LEU B 340
SSBOND 1 CYS C 23 CYS C 92 1555 1555 2.04
SSBOND 2 CYS C 138 CYS C 198 1555 1555 2.04
SSBOND 3 CYS E 22 CYS E 95 1555 1555 2.03
SSBOND 4 CYS E 145 CYS E 200 1555 1555 2.04
SSBOND 5 CYS F 22 CYS F 95 1555 1555 2.03
SSBOND 6 CYS F 145 CYS F 200 1555 1555 2.04
SSBOND 7 CYS D 23 CYS D 92 1555 1555 2.04
SSBOND 8 CYS D 138 CYS D 198 1555 1555 2.04
CISPEP 1 SER C 7 PRO C 8 0 -2.02
CISPEP 2 ASP C 80 PRO C 81 0 -1.94
CISPEP 3 ASP C 98 PRO C 99 0 1.43
CISPEP 4 TYR C 144 PRO C 145 0 -1.40
CISPEP 5 PHE E 151 PRO E 152 0 -2.94
CISPEP 6 GLU E 153 PRO E 154 0 -6.27
CISPEP 7 TRP E 193 PRO E 194 0 -1.09
CISPEP 8 PHE F 151 PRO F 152 0 -2.90
CISPEP 9 GLU F 153 PRO F 154 0 -6.36
CISPEP 10 TRP F 193 PRO F 194 0 -1.09
CISPEP 11 SER D 7 PRO D 8 0 -1.99
CISPEP 12 ASP D 80 PRO D 81 0 -2.06
CISPEP 13 ASP D 98 PRO D 99 0 1.41
CISPEP 14 TYR D 144 PRO D 145 0 -1.41
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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
ATOM 1 N ILE A 22 168.444 204.163 202.797 1.00121.31 N
ATOM 2 CA ILE A 22 167.871 203.873 204.104 1.00125.02 C
ATOM 3 C ILE A 22 166.351 203.825 204.018 1.00125.56 C
ATOM 4 O ILE A 22 165.745 202.767 204.178 1.00124.04 O
ATOM 5 CB ILE A 22 168.322 204.904 205.151 1.00126.75 C
ATOM 6 CG1 ILE A 22 169.849 204.996 205.187 1.00125.86 C
ATOM 7 CG2 ILE A 22 167.770 204.546 206.523 1.00122.49 C
ATOM 8 CD1 ILE A 22 170.378 205.990 206.198 1.00123.50 C
ATOM 9 N SER A 23 165.740 204.986 203.768 1.00122.39 N
ATOM 10 CA SER A 23 164.285 205.052 203.675 1.00120.13 C
ATOM 11 C SER A 23 163.765 204.242 202.494 1.00121.91 C
ATOM 12 O SER A 23 162.747 203.550 202.609 1.00120.66 O
ATOM 13 CB SER A 23 163.833 206.507 203.568 1.00120.77 C
ATOM 14 OG SER A 23 164.339 207.112 202.391 1.00121.16 O
ATOM 15 N GLY A 24 164.451 204.311 201.351 1.00119.61 N
ATOM 16 CA GLY A 24 164.003 203.595 200.170 1.00116.92 C
ATOM 17 C GLY A 24 164.082 202.088 200.289 1.00119.28 C
ATOM 18 O GLY A 24 163.362 201.383 199.575 1.00118.70 O
ATOM 19 N TRP A 25 164.943 201.578 201.173 1.00115.79 N
ATOM 20 CA TRP A 25 165.032 200.136 201.371 1.00115.66 C
ATOM 21 C TRP A 25 163.753 199.575 201.980 1.00116.58 C
ATOM 22 O TRP A 25 163.354 198.450 201.659 1.00114.13 O
ATOM 23 CB TRP A 25 166.230 199.799 202.259 1.00113.63 C
ATOM 24 CG TRP A 25 167.435 199.314 201.512 1.00115.37 C
ATOM 25 CD1 TRP A 25 168.051 199.927 200.461 1.00114.28 C
ATOM 26 CD2 TRP A 25 168.180 198.116 201.769 1.00116.40 C
ATOM 27 NE1 TRP A 25 169.129 199.183 200.045 1.00114.12 N
ATOM 28 CE2 TRP A 25 169.229 198.067 200.832 1.00114.67 C
ATOM 29 CE3 TRP A 25 168.058 197.080 202.700 1.00115.00 C
ATOM 30 CZ2 TRP A 25 170.151 197.023 200.799 1.00113.50 C
ATOM 31 CZ3 TRP A 25 168.974 196.044 202.664 1.00112.25 C
ATOM 32 CH2 TRP A 25 170.007 196.024 201.720 1.00114.34 C
ATOM 33 N PHE A 26 163.104 200.339 202.861 1.00111.26 N
ATOM 34 CA PHE A 26 161.948 199.824 203.589 1.00108.23 C
ATOM 35 C PHE A 26 160.780 199.530 202.656 1.00107.36 C
ATOM 36 O PHE A 26 160.133 198.484 202.772 1.00107.37 O
ATOM 37 CB PHE A 26 161.537 200.810 204.679 1.00105.54 C
ATOM 38 CG PHE A 26 162.182 200.542 206.002 1.00106.77 C
ATOM 39 CD1 PHE A 26 163.554 200.648 206.150 1.00109.25 C
ATOM 40 CD2 PHE A 26 161.422 200.181 207.098 1.00106.00 C
ATOM 41 CE1 PHE A 26 164.156 200.399 207.367 1.00109.95 C
ATOM 42 CE2 PHE A 26 162.017 199.933 208.319 1.00108.16 C
ATOM 43 CZ PHE A 26 163.386 200.042 208.454 1.00107.39 C
ATOM 44 N ARG A 27 160.489 200.440 201.725 1.00111.62 N
ATOM 45 CA ARG A 27 159.385 200.200 200.800 1.00113.90 C
ATOM 46 C ARG A 27 159.662 199.005 199.900 1.00114.14 C
ATOM 47 O ARG A 27 158.725 198.346 199.439 1.00115.44 O
ATOM 48 CB ARG A 27 159.102 201.445 199.957 1.00115.85 C
ATOM 49 CG ARG A 27 158.413 202.590 200.700 1.00114.94 C
ATOM 50 CD ARG A 27 159.366 203.366 201.598 1.00116.57 C
ATOM 51 NE ARG A 27 160.109 204.379 200.857 1.00117.36 N
ATOM 52 CZ ARG A 27 160.714 205.420 201.411 1.00118.20 C
ATOM 53 NH1 ARG A 27 160.691 205.616 202.719 1.00115.97 N
ATOM 54 NH2 ARG A 27 161.361 206.284 200.635 1.00115.73 N
ATOM 55 N SER A 28 160.936 198.715 199.633 1.00105.53 N
ATOM 56 CA SER A 28 161.277 197.519 198.873 1.00105.37 C
ATOM 57 C SER A 28 161.074 196.259 199.706 1.00106.16 C
ATOM 58 O SER A 28 160.661 195.219 199.179 1.00105.29 O
ATOM 59 CB SER A 28 162.717 197.611 198.371 1.00105.52 C
ATOM 60 OG SER A 28 163.327 196.334 198.326 1.00108.15 O
ATOM 61 N ILE A 29 161.366 196.330 201.006 1.00 98.14 N
ATOM 62 CA ILE A 29 161.182 195.173 201.877 1.00 94.19 C
ATOM 63 C ILE A 29 159.706 194.818 201.993 1.00 94.95 C
ATOM 64 O ILE A 29 159.316 193.657 201.834 1.00101.12 O
ATOM 65 CB ILE A 29 161.807 195.437 203.258 1.00 96.33 C
ATOM 66 CG1 ILE A 29 163.325 195.574 203.142 1.00 98.86 C
ATOM 67 CG2 ILE A 29 161.451 194.331 204.224 1.00 97.35 C
ATOM 68 CD1 ILE A 29 163.954 196.328 204.286 1.00 97.87 C
ATOM 69 N LEU A 30 158.859 195.814 202.254 1.00 96.80 N
ATOM 70 CA LEU A 30 157.438 195.548 202.440 1.00 99.92 C
ATOM 71 C LEU A 30 156.740 195.154 201.146 1.00 98.95 C
ATOM 72 O LEU A 30 155.610 194.658 201.195 1.00 99.30 O
ATOM 73 CB LEU A 30 156.750 196.768 203.048 1.00 98.82 C
ATOM 74 CG LEU A 30 157.472 197.436 204.217 1.00 97.28 C
ATOM 75 CD1 LEU A 30 156.771 198.724 204.607 1.00 98.13 C
ATOM 76 CD2 LEU A 30 157.567 196.490 205.400 1.00 96.65 C
ATOM 77 N SER A 31 157.377 195.371 199.995 1.00101.27 N
ATOM 78 CA SER A 31 156.750 195.020 198.725 1.00102.72 C
ATOM 79 C SER A 31 156.617 193.509 198.563 1.00103.55 C
ATOM 80 O SER A 31 155.608 193.024 198.038 1.00102.34 O
ATOM 81 CB SER A 31 157.550 195.617 197.569 1.00101.49 C
ATOM 82 OG SER A 31 158.784 194.943 197.403 1.00104.00 O
ATOM 83 N ASP A 32 157.617 192.752 199.001 1.00 97.55 N
ATOM 84 CA ASP A 32 157.644 191.313 198.795 1.00 93.41 C
ATOM 85 C ASP A 32 157.135 190.574 200.025 1.00 95.01 C
ATOM 86 O ASP A 32 157.317 191.017 201.161 1.00 96.25 O
ATOM 87 CB ASP A 32 159.059 190.845 198.457 1.00 93.35 C
ATOM 88 CG ASP A 32 159.085 189.454 197.860 1.00 96.88 C
ATOM 89 OD1 ASP A 32 159.011 188.472 198.628 1.00 95.86 O
ATOM 90 OD2 ASP A 32 159.175 189.340 196.620 1.00 98.25 O
ATOM 91 N LYS A 33 156.490 189.431 199.783 1.00 96.25 N
ATOM 92 CA LYS A 33 155.936 188.637 200.875 1.00 95.96 C
ATOM 93 C LYS A 33 157.042 188.006 201.712 1.00 94.82 C
ATOM 94 O LYS A 33 157.008 188.055 202.948 1.00 97.26 O
ATOM 95 CB LYS A 33 155.004 187.565 200.310 1.00 95.72 C
ATOM 96 CG LYS A 33 154.560 186.513 201.310 1.00 97.37 C
ATOM 97 CD LYS A 33 153.140 186.781 201.780 1.00 97.92 C
ATOM 98 CE LYS A 33 152.835 186.061 203.081 1.00 98.05 C
ATOM 99 NZ LYS A 33 151.787 186.765 203.868 1.00 96.23 N
ATOM 100 N THR A 34 158.034 187.407 201.050 1.00 89.74 N
ATOM 101 CA THR A 34 159.151 186.805 201.767 1.00 91.71 C
ATOM 102 C THR A 34 159.911 187.848 202.573 1.00 93.41 C
ATOM 103 O THR A 34 160.209 187.636 203.754 1.00 91.21 O
ATOM 104 CB THR A 34 160.090 186.109 200.781 1.00 89.59 C
ATOM 105 OG1 THR A 34 159.397 185.037 200.132 1.00 94.00 O
ATOM 106 CG2 THR A 34 161.305 185.553 201.502 1.00 91.16 C
ATOM 107 N SER A 35 160.216 188.989 201.952 1.00 87.12 N
ATOM 108 CA SER A 35 160.945 190.045 202.643 1.00 81.15 C
ATOM 109 C SER A 35 160.132 190.618 203.794 1.00 84.65 C
ATOM 110 O SER A 35 160.681 190.918 204.858 1.00 91.37 O
ATOM 111 CB SER A 35 161.323 191.147 201.655 1.00 86.72 C
ATOM 112 OG SER A 35 161.895 190.601 200.482 1.00 88.95 O
ATOM 113 N ARG A 36 158.823 190.786 203.601 1.00 80.75 N
ATOM 114 CA ARG A 36 157.980 191.322 204.665 1.00 81.53 C
ATOM 115 C ARG A 36 157.938 190.381 205.863 1.00 86.74 C
ATOM 116 O ARG A 36 158.070 190.813 207.016 1.00 88.40 O
ATOM 117 CB ARG A 36 156.572 191.575 204.132 1.00 84.20 C
ATOM 118 CG ARG A 36 155.705 192.413 205.044 1.00 86.89 C
ATOM 119 CD ARG A 36 154.505 192.990 204.312 1.00 89.55 C
ATOM 120 NE ARG A 36 154.275 192.350 203.022 1.00 95.22 N
ATOM 121 CZ ARG A 36 153.479 191.307 202.831 1.00 94.05 C
ATOM 122 NH1 ARG A 36 152.826 190.743 203.834 1.00 92.32 N
ATOM 123 NH2 ARG A 36 153.336 190.817 201.604 1.00 90.96 N
ATOM 124 N ASN A 37 157.750 189.083 205.608 1.00 89.83 N
ATOM 125 CA ASN A 37 157.734 188.119 206.702 1.00 87.56 C
ATOM 126 C ASN A 37 159.083 188.059 207.402 1.00 90.31 C
ATOM 127 O ASN A 37 159.149 187.983 208.636 1.00 93.59 O
ATOM 128 CB ASN A 37 157.340 186.740 206.181 1.00 89.73 C
ATOM 129 CG ASN A 37 155.933 186.707 205.640 1.00 92.65 C
ATOM 130 OD1 ASN A 37 155.670 186.096 204.607 1.00 92.47 O
ATOM 131 ND2 ASN A 37 155.018 187.374 206.330 1.00 92.16 N
ATOM 132 N LEU A 38 160.172 188.093 206.631 1.00 82.82 N
ATOM 133 CA LEU A 38 161.501 188.077 207.227 1.00 81.09 C
ATOM 134 C LEU A 38 161.723 189.300 208.103 1.00 82.49 C
ATOM 135 O LEU A 38 162.274 189.192 209.203 1.00 83.57 O
ATOM 136 CB LEU A 38 162.560 188.001 206.131 1.00 80.35 C
ATOM 137 CG LEU A 38 162.853 186.608 205.585 1.00 79.74 C
ATOM 138 CD1 LEU A 38 163.594 186.699 204.270 1.00 80.83 C
ATOM 139 CD2 LEU A 38 163.649 185.821 206.595 1.00 76.66 C
ATOM 140 N PHE A 39 161.295 190.473 207.634 1.00 86.83 N
ATOM 141 CA PHE A 39 161.463 191.691 208.414 1.00 84.08 C
ATOM 142 C PHE A 39 160.653 191.643 209.702 1.00 87.08 C
ATOM 143 O PHE A 39 161.147 192.030 210.766 1.00 95.69 O
ATOM 144 CB PHE A 39 161.069 192.906 207.577 1.00 85.73 C
ATOM 145 CG PHE A 39 161.178 194.206 208.312 1.00 86.32 C
ATOM 146 CD1 PHE A 39 162.392 194.627 208.821 1.00 88.22 C
ATOM 147 CD2 PHE A 39 160.066 195.005 208.500 1.00 86.90 C
ATOM 148 CE1 PHE A 39 162.494 195.820 209.500 1.00 89.20 C
ATOM 149 CE2 PHE A 39 160.163 196.199 209.180 1.00 86.58 C
ATOM 150 CZ PHE A 39 161.378 196.607 209.679 1.00 86.98 C
ATOM 151 N PHE A 40 159.404 191.178 209.630 1.00 85.73 N
ATOM 152 CA PHE A 40 158.599 191.095 210.846 1.00 92.00 C
ATOM 153 C PHE A 40 159.190 190.109 211.846 1.00 91.70 C
ATOM 154 O PHE A 40 159.246 190.394 213.050 1.00 92.81 O
ATOM 155 CB PHE A 40 157.156 190.729 210.512 1.00 92.75 C
ATOM 156 CG PHE A 40 156.386 191.844 209.870 1.00 94.61 C
ATOM 157 CD1 PHE A 40 156.577 193.151 210.279 1.00 96.53 C
ATOM 158 CD2 PHE A 40 155.473 191.591 208.864 1.00 89.57 C
ATOM 159 CE1 PHE A 40 155.874 194.182 209.698 1.00 95.65 C
ATOM 160 CE2 PHE A 40 154.763 192.621 208.285 1.00 89.65 C
ATOM 161 CZ PHE A 40 154.968 193.918 208.699 1.00 93.50 C
ATOM 162 N PHE A 41 159.644 188.946 211.374 1.00 79.88 N
ATOM 163 CA PHE A 41 160.247 187.986 212.291 1.00 82.40 C
ATOM 164 C PHE A 41 161.538 188.529 212.895 1.00 87.29 C
ATOM 165 O PHE A 41 161.813 188.319 214.083 1.00 89.51 O
ATOM 166 CB PHE A 41 160.493 186.659 211.580 1.00 82.30 C
ATOM 167 CG PHE A 41 160.668 185.507 212.517 1.00 85.89 C
ATOM 168 CD1 PHE A 41 159.624 185.092 213.324 1.00 84.55 C
ATOM 169 CD2 PHE A 41 161.875 184.839 212.594 1.00 83.91 C
ATOM 170 CE1 PHE A 41 159.785 184.038 214.193 1.00 86.00 C
ATOM 171 CE2 PHE A 41 162.038 183.781 213.458 1.00 84.24 C
ATOM 172 CZ PHE A 41 160.992 183.379 214.258 1.00 86.64 C
ATOM 173 N LEU A 42 162.340 189.230 212.092 1.00 89.86 N
ATOM 174 CA LEU A 42 163.557 189.844 212.604 1.00 87.61 C
ATOM 175 C LEU A 42 163.248 190.880 213.673 1.00 87.51 C
ATOM 176 O LEU A 42 163.933 190.946 214.699 1.00 90.69 O
ATOM 177 CB LEU A 42 164.328 190.487 211.458 1.00 88.07 C
ATOM 178 CG LEU A 42 165.522 191.338 211.871 1.00 87.20 C
ATOM 179 CD1 LEU A 42 166.638 190.472 212.430 1.00 88.34 C
ATOM 180 CD2 LEU A 42 165.984 192.165 210.697 1.00 88.73 C
ATOM 181 N CYS A 43 162.232 191.712 213.442 1.00 89.54 N
ATOM 182 CA CYS A 43 161.859 192.708 214.438 1.00 89.23 C
ATOM 183 C CYS A 43 161.390 192.044 215.723 1.00 94.21 C
ATOM 184 O CYS A 43 161.737 192.490 216.822 1.00 98.73 O
ATOM 185 CB CYS A 43 160.776 193.630 213.884 1.00 90.11 C
ATOM 186 SG CYS A 43 161.366 194.767 212.619 1.00106.06 S
ATOM 187 N LEU A 44 160.607 190.970 215.604 1.00 94.56 N
ATOM 188 CA LEU A 44 160.160 190.255 216.794 1.00 93.74 C
ATOM 189 C LEU A 44 161.343 189.696 217.577 1.00 95.68 C
ATOM 190 O LEU A 44 161.420 189.859 218.802 1.00 98.81 O
ATOM 191 CB LEU A 44 159.199 189.136 216.394 1.00 90.45 C
ATOM 192 CG LEU A 44 158.440 188.405 217.501 1.00 90.95 C
ATOM 193 CD1 LEU A 44 158.100 189.343 218.645 1.00 91.99 C
ATOM 194 CD2 LEU A 44 157.184 187.767 216.940 1.00 94.48 C
ATOM 195 N ASN A 45 162.285 189.051 216.884 1.00 94.37 N
ATOM 196 CA ASN A 45 163.441 188.473 217.562 1.00 91.27 C
ATOM 197 C ASN A 45 164.301 189.546 218.218 1.00 94.91 C
ATOM 198 O ASN A 45 164.767 189.373 219.351 1.00 98.10 O
ATOM 199 CB ASN A 45 164.271 187.655 216.574 1.00 91.59 C
ATOM 200 CG ASN A 45 163.597 186.358 216.183 1.00 94.37 C
ATOM 201 OD1 ASN A 45 162.529 186.023 216.690 1.00 91.98 O
ATOM 202 ND2 ASN A 45 164.222 185.618 215.278 1.00 98.43 N
ATOM 203 N LEU A 46 164.529 190.661 217.519 1.00 99.37 N
ATOM 204 CA LEU A 46 165.337 191.736 218.083 1.00 97.19 C
ATOM 205 C LEU A 46 164.666 192.357 219.299 1.00100.30 C
ATOM 206 O LEU A 46 165.335 192.665 220.291 1.00103.27 O
ATOM 207 CB LEU A 46 165.615 192.798 217.022 1.00 97.05 C
ATOM 208 CG LEU A 46 166.601 192.399 215.926 1.00100.65 C
ATOM 209 CD1 LEU A 46 166.998 193.609 215.102 1.00101.14 C
ATOM 210 CD2 LEU A 46 167.824 191.734 216.528 1.00 98.10 C
ATOM 211 N SER A 47 163.347 192.557 219.244 1.00100.16 N
ATOM 212 CA SER A 47 162.640 193.092 220.402 1.00 99.89 C
ATOM 213 C SER A 47 162.715 192.135 221.583 1.00101.28 C
ATOM 214 O SER A 47 162.901 192.564 222.729 1.00103.98 O
ATOM 215 CB SER A 47 161.185 193.385 220.041 1.00100.98 C
ATOM 216 OG SER A 47 160.657 192.378 219.197 1.00107.10 O
ATOM 217 N PHE A 48 162.571 190.833 221.327 1.00101.96 N
ATOM 218 CA PHE A 48 162.671 189.856 222.407 1.00103.17 C
ATOM 219 C PHE A 48 164.058 189.883 223.038 1.00106.24 C
ATOM 220 O PHE A 48 164.196 189.869 224.266 1.00108.06 O
ATOM 221 CB PHE A 48 162.338 188.460 221.881 1.00103.67 C
ATOM 222 CG PHE A 48 162.050 187.456 222.961 1.00104.93 C
ATOM 223 CD1 PHE A 48 163.072 186.920 223.726 1.00105.65 C
ATOM 224 CD2 PHE A 48 160.753 187.049 223.213 1.00106.37 C
ATOM 225 CE1 PHE A 48 162.807 186.000 224.718 1.00105.08 C
ATOM 226 CE2 PHE A 48 160.483 186.130 224.204 1.00108.60 C
ATOM 227 CZ PHE A 48 161.512 185.604 224.957 1.00107.48 C
ATOM 228 N ALA A 49 165.102 189.929 222.207 1.00109.05 N
ATOM 229 CA ALA A 49 166.462 189.975 222.734 1.00106.38 C
ATOM 230 C ALA A 49 166.712 191.260 223.515 1.00109.04 C
ATOM 231 O ALA A 49 167.387 191.243 224.551 1.00111.81 O
ATOM 232 CB ALA A 49 167.468 189.831 221.595 1.00105.32 C
ATOM 233 N PHE A 50 166.182 192.385 223.030 1.00112.84 N
ATOM 234 CA PHE A 50 166.335 193.652 223.738 1.00112.38 C
ATOM 235 C PHE A 50 165.665 193.601 225.106 1.00111.64 C
ATOM 236 O PHE A 50 166.239 194.048 226.107 1.00113.30 O
ATOM 237 CB PHE A 50 165.749 194.783 222.893 1.00112.27 C
ATOM 238 CG PHE A 50 166.166 196.157 223.330 1.00115.33 C
ATOM 239 CD1 PHE A 50 167.191 196.336 224.243 1.00114.99 C
ATOM 240 CD2 PHE A 50 165.520 197.275 222.831 1.00115.36 C
ATOM 241 CE1 PHE A 50 167.568 197.603 224.644 1.00114.38 C
ATOM 242 CE2 PHE A 50 165.891 198.544 223.228 1.00116.50 C