HEADER VIRAL PROTEIN 22-SEP-16 5TEO
TITLE DIMER OF HIV-1 GAG CTD-SP1 FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 GAG CTD-SP1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PR160GAG-POL;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 GROUP M
SOURCE 3 SUBTYPE B (ISOLATE NY5);
SOURCE 4 ORGANISM_COMMON: HIV-1;
SOURCE 5 ORGANISM_TAXID: 11698;
SOURCE 6 STRAIN: ISOLATE NY5;
SOURCE 7 GENE: GAG-POL;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS VIRAL CAPSID PROTEIN, DIMER, HELIX, MOLECULAR SWITCH, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR O.PORNILLOS,J.M.WAGNER,K.K.ZADROZNY,B.K.GANSER-PORNILLOS
REVDAT 2 04-OCT-23 5TEO 1 REMARK
REVDAT 1 27-SEP-17 5TEO 0
JRNL AUTH O.PORNILLOS,J.M.WAGNER,K.K.ZADROZNY,B.K.GANSER-PORNILLOS
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.0
REMARK 3 NUMBER OF REFLECTIONS : 8044
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 394
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 31.3537 - 2.9506 0.99 3482 175 0.1829 0.2271
REMARK 3 2 2.9506 - 2.3422 0.89 3039 174 0.2348 0.2660
REMARK 3 3 2.3422 - 2.0462 0.33 1129 45 0.2477 0.3157
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.74
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 1284
REMARK 3 ANGLE : 0.436 1739
REMARK 3 CHIRALITY : 0.033 199
REMARK 3 PLANARITY : 0.003 228
REMARK 3 DIHEDRAL : 10.667 793
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3546 -0.1245 7.3063
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: 0.1560
REMARK 3 T33: 0.1532 T12: 0.0225
REMARK 3 T13: 0.0049 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.2643 L22: 0.6208
REMARK 3 L33: 0.6217 L12: -0.2309
REMARK 3 L13: -0.1847 L23: 0.3546
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: -0.0191 S13: -0.0664
REMARK 3 S21: 0.0308 S22: -0.1483 S23: 0.1601
REMARK 3 S31: 0.0203 S32: -0.0250 S33: -0.1657
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 149 THROUGH 219 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9688 -7.2537 24.9375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1931 T22: 0.1964
REMARK 3 T33: 0.2149 T12: 0.0031
REMARK 3 T13: -0.0018 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 0.3418 L22: 0.3405
REMARK 3 L33: 0.1479 L12: 0.0291
REMARK 3 L13: 0.0799 L23: -0.0159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0785 S12: 0.0072 S13: 0.0503
REMARK 3 S21: 0.1204 S22: 0.0177 S23: 0.1552
REMARK 3 S31: 0.0090 S32: -0.1453 S33: 0.0022
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 220 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0953 7.7832 43.9231
REMARK 3 T TENSOR
REMARK 3 T11: 0.2797 T22: 0.4252
REMARK 3 T33: 0.4149 T12: 0.0022
REMARK 3 T13: -0.0176 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 0.1183 L22: 0.0919
REMARK 3 L33: 1.9698 L12: -0.0772
REMARK 3 L13: -0.0094 L23: -0.2798
REMARK 3 S TENSOR
REMARK 3 S11: 0.1401 S12: 0.3603 S13: 0.4544
REMARK 3 S21: -0.1361 S22: -0.0548 S23: -0.2150
REMARK 3 S31: 0.3956 S32: 0.2379 S33: 0.0533
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000224116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9038
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.046
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.7
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.35800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.10.1_2155
REMARK 200 STARTING MODEL: 1A43
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1-0.2M DIBASIC
REMARK 280 AMMONIUM PHOSPHATE, VAPOR DIFFUSION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 20.23700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 HIS A 136
REMARK 465 MET A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 HIS A 141
REMARK 465 HIS A 142
REMARK 465 HIS A 143
REMARK 465 GLY A 144
REMARK 465 GLY A 145
REMARK 465 SER A 146
REMARK 465 PRO A 147
REMARK 465 GLY A 220
REMARK 465 VAL A 221
REMARK 465 GLY A 222
REMARK 465 GLY A 223
REMARK 465 PRO A 224
REMARK 465 GLY A 225
REMARK 465 HIS A 226
REMARK 465 LYS A 227
REMARK 465 ALA A 228
REMARK 465 ARG A 229
REMARK 465 VAL A 230
REMARK 465 LEU A 231
REMARK 465 ALA A 232
REMARK 465 GLU A 233
REMARK 465 ALA A 234
REMARK 465 MET A 235
REMARK 465 SER A 236
REMARK 465 GLN A 237
REMARK 465 VAL A 238
REMARK 465 THR A 239
REMARK 465 ASN A 240
REMARK 465 THR A 241
REMARK 465 ALA A 242
REMARK 465 THR A 243
REMARK 465 ILE A 244
REMARK 465 MET A 245
REMARK 465 HIS B 136
REMARK 465 MET B 137
REMARK 465 HIS B 138
REMARK 465 HIS B 139
REMARK 465 HIS B 140
REMARK 465 HIS B 141
REMARK 465 HIS B 142
REMARK 465 HIS B 143
REMARK 465 GLY B 144
REMARK 465 GLY B 145
REMARK 465 SER B 146
REMARK 465 PRO B 147
REMARK 465 THR B 148
REMARK 465 ALA B 242
REMARK 465 THR B 243
REMARK 465 ILE B 244
REMARK 465 MET B 245
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 158 CG CD CE NZ
REMARK 470 GLN B 176 CG CD OE1 NE2
REMARK 470 LYS B 227 CG CD CE NZ
REMARK 470 ARG B 229 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 233 CG CD OE1 OE2
REMARK 470 THR B 241 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP B 166 O HOH B 301 1.98
REMARK 500 O PRO B 207 O HOH B 302 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 301 O HOH B 302 2746 1.98
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5TEO A 146 245 UNP P12497 POL_HV1N5 278 377
DBREF 5TEO B 146 245 UNP P12497 POL_HV1N5 278 377
SEQADV 5TEO HIS A 136 UNP P12497 EXPRESSION TAG
SEQADV 5TEO MET A 137 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS A 138 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS A 139 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS A 140 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS A 141 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS A 142 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS A 143 UNP P12497 EXPRESSION TAG
SEQADV 5TEO GLY A 144 UNP P12497 EXPRESSION TAG
SEQADV 5TEO GLY A 145 UNP P12497 EXPRESSION TAG
SEQADV 5TEO THR A 241 UNP P12497 PRO 373 ENGINEERED MUTATION
SEQADV 5TEO HIS B 136 UNP P12497 EXPRESSION TAG
SEQADV 5TEO MET B 137 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS B 138 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS B 139 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS B 140 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS B 141 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS B 142 UNP P12497 EXPRESSION TAG
SEQADV 5TEO HIS B 143 UNP P12497 EXPRESSION TAG
SEQADV 5TEO GLY B 144 UNP P12497 EXPRESSION TAG
SEQADV 5TEO GLY B 145 UNP P12497 EXPRESSION TAG
SEQADV 5TEO THR B 241 UNP P12497 PRO 373 ENGINEERED MUTATION
SEQRES 1 A 110 HIS MET HIS HIS HIS HIS HIS HIS GLY GLY SER PRO THR
SEQRES 2 A 110 SER ILE LEU ASP ILE ARG GLN GLY PRO LYS GLU PRO PHE
SEQRES 3 A 110 ARG ASP TYR VAL ASP ARG PHE TYR LYS THR LEU ARG ALA
SEQRES 4 A 110 GLU GLN ALA SER GLN GLU VAL LYS ASN TRP MET THR GLU
SEQRES 5 A 110 THR LEU LEU VAL GLN ASN ALA ASN PRO ASP CYS LYS THR
SEQRES 6 A 110 ILE LEU LYS ALA LEU GLY PRO GLY ALA THR LEU GLU GLU
SEQRES 7 A 110 MET MET THR ALA CYS GLN GLY VAL GLY GLY PRO GLY HIS
SEQRES 8 A 110 LYS ALA ARG VAL LEU ALA GLU ALA MET SER GLN VAL THR
SEQRES 9 A 110 ASN THR ALA THR ILE MET
SEQRES 1 B 110 HIS MET HIS HIS HIS HIS HIS HIS GLY GLY SER PRO THR
SEQRES 2 B 110 SER ILE LEU ASP ILE ARG GLN GLY PRO LYS GLU PRO PHE
SEQRES 3 B 110 ARG ASP TYR VAL ASP ARG PHE TYR LYS THR LEU ARG ALA
SEQRES 4 B 110 GLU GLN ALA SER GLN GLU VAL LYS ASN TRP MET THR GLU
SEQRES 5 B 110 THR LEU LEU VAL GLN ASN ALA ASN PRO ASP CYS LYS THR
SEQRES 6 B 110 ILE LEU LYS ALA LEU GLY PRO GLY ALA THR LEU GLU GLU
SEQRES 7 B 110 MET MET THR ALA CYS GLN GLY VAL GLY GLY PRO GLY HIS
SEQRES 8 B 110 LYS ALA ARG VAL LEU ALA GLU ALA MET SER GLN VAL THR
SEQRES 9 B 110 ASN THR ALA THR ILE MET
FORMUL 3 HOH *15(H2 O)
HELIX 1 AA1 SER A 149 ILE A 153 5 5
HELIX 2 AA2 PRO A 160 GLU A 175 1 16
HELIX 3 AA3 SER A 178 THR A 188 1 11
HELIX 4 AA4 THR A 188 ASN A 193 1 6
HELIX 5 AA5 ASN A 195 GLY A 206 1 12
HELIX 6 AA6 THR A 210 CYS A 218 1 9
HELIX 7 AA7 SER B 149 ILE B 153 5 5
HELIX 8 AA8 PRO B 160 ARG B 173 1 14
HELIX 9 AA9 SER B 178 THR B 188 1 11
HELIX 10 AB1 THR B 188 ASN B 193 1 6
HELIX 11 AB2 ASN B 195 GLY B 206 1 12
HELIX 12 AB3 THR B 210 CYS B 218 1 9
HELIX 13 AB4 GLY B 223 THR B 241 1 19
CRYST1 42.741 40.474 50.450 90.00 100.74 90.00 P 1 21 1 4
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 0.023397 0.000000 0.004437 0.00000
SCALE2 0.000000 0.024707 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020175 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
