HEADER MEMBRANE PROTEIN 19-AUG-10 3IZ1
TITLE C-ALPHA MODEL FITTED INTO THE EM STRUCTURE OF CX26M34A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAP JUNCTION BETA-2 PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: CONNEXIN-26, CX26;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GJB2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBLUEBAC4.5
KEYWDS MEMBRANE PROTEIN, GAP JUNCTION CHANNEL
EXPDTA ELECTRON CRYSTALLOGRAPHY
MDLTYP CA ATOMS ONLY, CHAIN A, B, C
AUTHOR A.OSHIMA,K.TANI,M.M.TOLOUE,Y.HIROAKI,A.SMOCK,S.INUKAI,A.CONE,
AUTHOR 2 B.J.NICHOLSON,G.E.SOSINSKY,Y.FUJIYOSHI
REVDAT 5 21-FEB-24 3IZ1 1 REMARK SEQADV
REVDAT 4 18-JUL-18 3IZ1 1 REMARK
REVDAT 3 09-FEB-11 3IZ1 1 JRNL
REVDAT 2 12-JAN-11 3IZ1 1 JRNL
REVDAT 1 03-NOV-10 3IZ1 0
JRNL AUTH A.OSHIMA,K.TANI,M.M.TOLOUE,Y.HIROAKI,A.SMOCK,S.INUKAI,
JRNL AUTH 2 A.CONE,B.J.NICHOLSON,G.E.SOSINSKY,Y.FUJIYOSHI
JRNL TITL ASYMMETRIC CONFIGURATIONS AND N-TERMINAL REARRANGEMENTS IN
JRNL TITL 2 CONNEXIN26 GAP JUNCTION CHANNELS.
JRNL REF J.MOL.BIOL. V. 405 724 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21094651
JRNL DOI 10.1016/J.JMB.2010.10.032
REMARK 2
REMARK 2 RESOLUTION. 6.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 6.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000160043.
REMARK 240
REMARK 240 EXPERIMENTAL DETAILS
REMARK 240 RECONSTRUCTION METHOD : CRYSTALLOGRAPHY
REMARK 240 SAMPLE TYPE : 2D ARRAY
REMARK 240 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 240 DATA ACQUISITION
REMARK 240 DATE OF DATA COLLECTION : NULL
REMARK 240 TEMPERATURE (KELVIN) : NULL
REMARK 240 PH : NULL
REMARK 240 NUMBER OF CRYSTALS USED : NULL
REMARK 240 MICROSCOPE MODEL : JEOL KYOTO-3000SFF
REMARK 240 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 240 ACCELERATION VOLTAGE (KV) : 300
REMARK 240 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 240 RESOLUTION RANGE HIGH (A) : NULL
REMARK 240 RESOLUTION RANGE LOW (A) : NULL
REMARK 240 DATA SCALING SOFTWARE : NULL
REMARK 240 COMPLETENESS FOR RANGE (%) : NULL
REMARK 240 DATA REDUNDANCY : NULL
REMARK 240 IN THE HIGHEST RESOLUTION SHELL
REMARK 240 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) :NULL
REMARK 240 HIGHEST RESOLUTION SHELL, RANGE LOW (A) :NULL
REMARK 240 COMPLETENESS FOR SHELL (%) : NULL
REMARK 240 DATA REDUNDANCY IN SHELL : NULL
REMARK 240 R MERGE FOR SHELL (I) : NULL
REMARK 240 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 240 SOFTWARE USED : NULL
REMARK 240 STARTING MODEL : NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 56.20000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.60000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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, B, C
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 1
REMARK 465 ASP A 2
REMARK 465 TRP A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 LEU A 6
REMARK 465 GLN A 7
REMARK 465 THR A 8
REMARK 465 ILE A 9
REMARK 465 LEU A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 VAL A 13
REMARK 465 ASN A 14
REMARK 465 LYS A 15
REMARK 465 HIS A 16
REMARK 465 SER A 17
REMARK 465 GLU A 110
REMARK 465 ILE A 111
REMARK 465 LYS A 112
REMARK 465 SER A 113
REMARK 465 GLU A 114
REMARK 465 PHE A 115
REMARK 465 LYS A 116
REMARK 465 ASP A 117
REMARK 465 ILE A 118
REMARK 465 GLU A 119
REMARK 465 GLU A 120
REMARK 465 ILE A 121
REMARK 465 LYS A 122
REMARK 465 THR A 123
REMARK 465 GLN A 124
REMARK 465 CYS A 218
REMARK 465 SER A 219
REMARK 465 GLY A 220
REMARK 465 LYS A 221
REMARK 465 SER A 222
REMARK 465 LYS A 223
REMARK 465 LYS A 224
REMARK 465 PRO A 225
REMARK 465 VAL A 226
REMARK 465 LEU A 227
REMARK 465 VAL A 228
REMARK 465 PRO A 229
REMARK 465 ARG A 230
REMARK 465 GLY A 231
REMARK 465 SER A 232
REMARK 465 HIS A 233
REMARK 465 HIS A 234
REMARK 465 HIS A 235
REMARK 465 HIS A 236
REMARK 465 HIS A 237
REMARK 465 HIS A 238
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 TRP B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 LEU B 6
REMARK 465 GLN B 7
REMARK 465 THR B 8
REMARK 465 ILE B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 GLY B 12
REMARK 465 VAL B 13
REMARK 465 ASN B 14
REMARK 465 LYS B 15
REMARK 465 HIS B 16
REMARK 465 SER B 17
REMARK 465 GLU B 110
REMARK 465 ILE B 111
REMARK 465 LYS B 112
REMARK 465 SER B 113
REMARK 465 GLU B 114
REMARK 465 PHE B 115
REMARK 465 LYS B 116
REMARK 465 ASP B 117
REMARK 465 ILE B 118
REMARK 465 GLU B 119
REMARK 465 GLU B 120
REMARK 465 ILE B 121
REMARK 465 LYS B 122
REMARK 465 THR B 123
REMARK 465 GLN B 124
REMARK 465 CYS B 218
REMARK 465 SER B 219
REMARK 465 GLY B 220
REMARK 465 LYS B 221
REMARK 465 SER B 222
REMARK 465 LYS B 223
REMARK 465 LYS B 224
REMARK 465 PRO B 225
REMARK 465 VAL B 226
REMARK 465 LEU B 227
REMARK 465 VAL B 228
REMARK 465 PRO B 229
REMARK 465 ARG B 230
REMARK 465 GLY B 231
REMARK 465 SER B 232
REMARK 465 HIS B 233
REMARK 465 HIS B 234
REMARK 465 HIS B 235
REMARK 465 HIS B 236
REMARK 465 HIS B 237
REMARK 465 HIS B 238
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 TRP C 3
REMARK 465 GLY C 4
REMARK 465 THR C 5
REMARK 465 LEU C 6
REMARK 465 GLN C 7
REMARK 465 THR C 8
REMARK 465 ILE C 9
REMARK 465 LEU C 10
REMARK 465 GLY C 11
REMARK 465 GLY C 12
REMARK 465 VAL C 13
REMARK 465 ASN C 14
REMARK 465 LYS C 15
REMARK 465 HIS C 16
REMARK 465 SER C 17
REMARK 465 GLU C 110
REMARK 465 ILE C 111
REMARK 465 LYS C 112
REMARK 465 SER C 113
REMARK 465 GLU C 114
REMARK 465 PHE C 115
REMARK 465 LYS C 116
REMARK 465 ASP C 117
REMARK 465 ILE C 118
REMARK 465 GLU C 119
REMARK 465 GLU C 120
REMARK 465 ILE C 121
REMARK 465 LYS C 122
REMARK 465 THR C 123
REMARK 465 GLN C 124
REMARK 465 CYS C 218
REMARK 465 SER C 219
REMARK 465 GLY C 220
REMARK 465 LYS C 221
REMARK 465 SER C 222
REMARK 465 LYS C 223
REMARK 465 LYS C 224
REMARK 465 PRO C 225
REMARK 465 VAL C 226
REMARK 465 LEU C 227
REMARK 465 VAL C 228
REMARK 465 PRO C 229
REMARK 465 ARG C 230
REMARK 465 GLY C 231
REMARK 465 SER C 232
REMARK 465 HIS C 233
REMARK 465 HIS C 234
REMARK 465 HIS C 235
REMARK 465 HIS C 236
REMARK 465 HIS C 237
REMARK 465 HIS C 238
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-1748 RELATED DB: EMDB
REMARK 900 EM DENSITY MAP AT 6A RESOLUTION
DBREF 3IZ1 A 1 226 UNP P29033 CXB2_HUMAN 1 226
DBREF 3IZ1 B 1 226 UNP P29033 CXB2_HUMAN 1 226
DBREF 3IZ1 C 1 226 UNP P29033 CXB2_HUMAN 1 226
SEQADV 3IZ1 LEU A 227 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 VAL A 228 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 PRO A 229 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 ARG A 230 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 GLY A 231 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 SER A 232 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS A 233 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS A 234 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS A 235 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS A 236 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS A 237 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS A 238 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 LEU B 227 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 VAL B 228 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 PRO B 229 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 ARG B 230 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 GLY B 231 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 SER B 232 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS B 233 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS B 234 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS B 235 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS B 236 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS B 237 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS B 238 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 LEU C 227 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 VAL C 228 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 PRO C 229 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 ARG C 230 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 GLY C 231 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 SER C 232 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS C 233 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS C 234 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS C 235 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS C 236 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS C 237 UNP P29033 EXPRESSION TAG
SEQADV 3IZ1 HIS C 238 UNP P29033 EXPRESSION TAG
SEQRES 1 A 238 MET ASP TRP GLY THR LEU GLN THR ILE LEU GLY GLY VAL
SEQRES 2 A 238 ASN LYS HIS SER THR SER ILE GLY LYS ILE TRP LEU THR
SEQRES 3 A 238 VAL LEU PHE ILE PHE ARG ILE MET ILE LEU VAL VAL ALA
SEQRES 4 A 238 ALA LYS GLU VAL TRP GLY ASP GLU GLN ALA ASP PHE VAL
SEQRES 5 A 238 CYS ASN THR LEU GLN PRO GLY CYS LYS ASN VAL CYS TYR
SEQRES 6 A 238 ASP HIS TYR PHE PRO ILE SER HIS ILE ARG LEU TRP ALA
SEQRES 7 A 238 LEU GLN LEU ILE PHE VAL SER THR PRO ALA LEU LEU VAL
SEQRES 8 A 238 ALA MET HIS VAL ALA TYR ARG ARG HIS GLU LYS LYS ARG
SEQRES 9 A 238 LYS PHE ILE LYS GLY GLU ILE LYS SER GLU PHE LYS ASP
SEQRES 10 A 238 ILE GLU GLU ILE LYS THR GLN LYS VAL ARG ILE GLU GLY
SEQRES 11 A 238 SER LEU TRP TRP THR TYR THR SER SER ILE PHE PHE ARG
SEQRES 12 A 238 VAL ILE PHE GLU ALA ALA PHE MET TYR VAL PHE TYR VAL
SEQRES 13 A 238 MET TYR ASP GLY PHE SER MET GLN ARG LEU VAL LYS CYS
SEQRES 14 A 238 ASN ALA TRP PRO CYS PRO ASN THR VAL ASP CYS PHE VAL
SEQRES 15 A 238 SER ARG PRO THR GLU LYS THR VAL PHE THR VAL PHE MET
SEQRES 16 A 238 ILE ALA VAL SER GLY ILE CYS ILE LEU LEU ASN VAL THR
SEQRES 17 A 238 GLU LEU CYS TYR LEU LEU ILE ARG TYR CYS SER GLY LYS
SEQRES 18 A 238 SER LYS LYS PRO VAL LEU VAL PRO ARG GLY SER HIS HIS
SEQRES 19 A 238 HIS HIS HIS HIS
SEQRES 1 B 238 MET ASP TRP GLY THR LEU GLN THR ILE LEU GLY GLY VAL
SEQRES 2 B 238 ASN LYS HIS SER THR SER ILE GLY LYS ILE TRP LEU THR
SEQRES 3 B 238 VAL LEU PHE ILE PHE ARG ILE MET ILE LEU VAL VAL ALA
SEQRES 4 B 238 ALA LYS GLU VAL TRP GLY ASP GLU GLN ALA ASP PHE VAL
SEQRES 5 B 238 CYS ASN THR LEU GLN PRO GLY CYS LYS ASN VAL CYS TYR
SEQRES 6 B 238 ASP HIS TYR PHE PRO ILE SER HIS ILE ARG LEU TRP ALA
SEQRES 7 B 238 LEU GLN LEU ILE PHE VAL SER THR PRO ALA LEU LEU VAL
SEQRES 8 B 238 ALA MET HIS VAL ALA TYR ARG ARG HIS GLU LYS LYS ARG
SEQRES 9 B 238 LYS PHE ILE LYS GLY GLU ILE LYS SER GLU PHE LYS ASP
SEQRES 10 B 238 ILE GLU GLU ILE LYS THR GLN LYS VAL ARG ILE GLU GLY
SEQRES 11 B 238 SER LEU TRP TRP THR TYR THR SER SER ILE PHE PHE ARG
SEQRES 12 B 238 VAL ILE PHE GLU ALA ALA PHE MET TYR VAL PHE TYR VAL
SEQRES 13 B 238 MET TYR ASP GLY PHE SER MET GLN ARG LEU VAL LYS CYS
SEQRES 14 B 238 ASN ALA TRP PRO CYS PRO ASN THR VAL ASP CYS PHE VAL
SEQRES 15 B 238 SER ARG PRO THR GLU LYS THR VAL PHE THR VAL PHE MET
SEQRES 16 B 238 ILE ALA VAL SER GLY ILE CYS ILE LEU LEU ASN VAL THR
SEQRES 17 B 238 GLU LEU CYS TYR LEU LEU ILE ARG TYR CYS SER GLY LYS
SEQRES 18 B 238 SER LYS LYS PRO VAL LEU VAL PRO ARG GLY SER HIS HIS
SEQRES 19 B 238 HIS HIS HIS HIS
SEQRES 1 C 238 MET ASP TRP GLY THR LEU GLN THR ILE LEU GLY GLY VAL
SEQRES 2 C 238 ASN LYS HIS SER THR SER ILE GLY LYS ILE TRP LEU THR
SEQRES 3 C 238 VAL LEU PHE ILE PHE ARG ILE MET ILE LEU VAL VAL ALA
SEQRES 4 C 238 ALA LYS GLU VAL TRP GLY ASP GLU GLN ALA ASP PHE VAL
SEQRES 5 C 238 CYS ASN THR LEU GLN PRO GLY CYS LYS ASN VAL CYS TYR
SEQRES 6 C 238 ASP HIS TYR PHE PRO ILE SER HIS ILE ARG LEU TRP ALA
SEQRES 7 C 238 LEU GLN LEU ILE PHE VAL SER THR PRO ALA LEU LEU VAL
SEQRES 8 C 238 ALA MET HIS VAL ALA TYR ARG ARG HIS GLU LYS LYS ARG
SEQRES 9 C 238 LYS PHE ILE LYS GLY GLU ILE LYS SER GLU PHE LYS ASP
SEQRES 10 C 238 ILE GLU GLU ILE LYS THR GLN LYS VAL ARG ILE GLU GLY
SEQRES 11 C 238 SER LEU TRP TRP THR TYR THR SER SER ILE PHE PHE ARG
SEQRES 12 C 238 VAL ILE PHE GLU ALA ALA PHE MET TYR VAL PHE TYR VAL
SEQRES 13 C 238 MET TYR ASP GLY PHE SER MET GLN ARG LEU VAL LYS CYS
SEQRES 14 C 238 ASN ALA TRP PRO CYS PRO ASN THR VAL ASP CYS PHE VAL
SEQRES 15 C 238 SER ARG PRO THR GLU LYS THR VAL PHE THR VAL PHE MET
SEQRES 16 C 238 ILE ALA VAL SER GLY ILE CYS ILE LEU LEU ASN VAL THR
SEQRES 17 C 238 GLU LEU CYS TYR LEU LEU ILE ARG TYR CYS SER GLY LYS
SEQRES 18 C 238 SER LYS LYS PRO VAL LEU VAL PRO ARG GLY SER HIS HIS
SEQRES 19 C 238 HIS HIS HIS HIS
CRYST1 112.400 111.200 300.000 90.00 90.00 90.00 P 21 21 2 12
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 0.008900 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008990 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003330 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
