HEADER HYDROLASE 02-AUG-18 6ADW
TITLE CRYSTAL STRUCTURE OF THE ZIKA VIRUS NS3 HELICASE (APO FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE NS3;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.91, 3.6.1.15, 3.6.4.13;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZIKA VIRUS (STRAIN MR 766);
SOURCE 3 ORGANISM_COMMON: ZIKV;
SOURCE 4 ORGANISM_TAXID: 64320;
SOURCE 5 STRAIN: MR 766;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET26B
KEYWDS ZIKA VIRUS NS3 HELICASE, APO FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FANG,G.LU,P.GONG
REVDAT 2 22-NOV-23 6ADW 1 REMARK
REVDAT 1 13-MAR-19 6ADW 0
JRNL AUTH J.FANG,X.JING,G.LU,Y.XU,P.GONG
JRNL TITL CRYSTALLOGRAPHIC SNAPSHOTS OF THE ZIKA VIRUS NS3 HELICASE
JRNL TITL 2 HELP VISUALIZE THE REACTANT WATER REPLENISHMENT.
JRNL REF ACS INFECT DIS V. 5 177 2019
JRNL REFN ESSN 2373-8227
JRNL PMID 30672289
JRNL DOI 10.1021/ACSINFECDIS.8B00214
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 20478
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 1009
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 43.7565 - 4.2021 1.00 2881 184 0.1477 0.1551
REMARK 3 2 4.2021 - 3.3357 0.99 2888 97 0.1471 0.2032
REMARK 3 3 3.3357 - 2.9142 1.00 2891 133 0.1764 0.2385
REMARK 3 4 2.9142 - 2.6478 1.00 2824 168 0.1939 0.2720
REMARK 3 5 2.6478 - 2.4580 1.00 2811 157 0.1935 0.2760
REMARK 3 6 2.4580 - 2.3131 0.98 2798 146 0.1983 0.2636
REMARK 3 7 2.3131 - 2.1972 0.84 2376 124 0.2052 0.2743
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.51
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 : 0.007 3502
REMARK 3 ANGLE : 0.936 4761
REMARK 3 CHIRALITY : 0.053 530
REMARK 3 PLANARITY : 0.006 618
REMARK 3 DIHEDRAL : 9.058 2885
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6ADW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1300005719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21028
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2VBC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, LITHIUM SULFATE, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 34.26700
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 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 170
REMARK 465 HIS A 171
REMARK 465 HIS A 172
REMARK 465 HIS A 173
REMARK 465 HIS A 174
REMARK 465 HIS A 175
REMARK 465 HIS A 176
REMARK 465 SER A 177
REMARK 465 SER A 178
REMARK 465 SER A 179
REMARK 465 GLY A 180
REMARK 465 PRO A 181
REMARK 465 SER A 182
REMARK 465 THR A 251
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 A 185 CG CD CE NZ
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 HIS A 252 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 274 CG1 CG2 CD1
REMARK 470 ARG A 275 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 278 CG OD1 ND2
REMARK 470 GLU A 306 CG CD OE1 OE2
REMARK 470 ARG A 367 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 389 CG CD CE NZ
REMARK 470 LYS A 419 CG CD CE NZ
REMARK 470 LYS A 466 CG CD CE NZ
REMARK 470 GLU A 479 CG CD OE1 OE2
REMARK 470 ARG A 509 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 525 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 537 CG CD CE NZ
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 NZ LYS A 200 OD1 ASP A 285 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 193 52.10 -117.34
REMARK 500 MET A 244 56.74 -93.53
REMARK 500 THR A 255 49.28 -97.01
REMARK 500 SER A 346 -60.66 -104.45
REMARK 500 THR A 409 -169.70 -78.33
REMARK 500 MET A 414 62.85 -110.35
REMARK 500 ASP A 501 108.90 -35.34
REMARK 500 LYS A 537 -77.58 -84.11
REMARK 500 CYS A 600 25.18 -142.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 704
DBREF 6ADW A 181 617 UNP Q32ZE1 POLG_ZIKV 1679 2115
SEQADV 6ADW MET A 170 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW HIS A 171 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW HIS A 172 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW HIS A 173 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW HIS A 174 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW HIS A 175 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW HIS A 176 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW SER A 177 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW SER A 178 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW SER A 179 UNP Q32ZE1 EXPRESSION TAG
SEQADV 6ADW GLY A 180 UNP Q32ZE1 EXPRESSION TAG
SEQRES 1 A 448 MET HIS HIS HIS HIS HIS HIS SER SER SER GLY PRO SER
SEQRES 2 A 448 MET LEU LYS LYS LYS GLN LEU THR VAL LEU ASP LEU HIS
SEQRES 3 A 448 PRO GLY ALA GLY LYS THR ARG ARG VAL LEU PRO GLU ILE
SEQRES 4 A 448 VAL ARG GLU ALA ILE LYS LYS ARG LEU ARG THR VAL ILE
SEQRES 5 A 448 LEU ALA PRO THR ARG VAL VAL ALA ALA GLU MET GLU GLU
SEQRES 6 A 448 ALA LEU ARG GLY LEU PRO VAL ARG TYR MET THR THR ALA
SEQRES 7 A 448 VAL ASN VAL THR HIS SER GLY THR GLU ILE VAL ASP LEU
SEQRES 8 A 448 MET CYS HIS ALA THR PHE THR SER ARG LEU LEU GLN PRO
SEQRES 9 A 448 ILE ARG VAL PRO ASN TYR ASN LEU ASN ILE MET ASP GLU
SEQRES 10 A 448 ALA HIS PHE THR ASP PRO SER SER ILE ALA ALA ARG GLY
SEQRES 11 A 448 TYR ILE SER THR ARG VAL GLU MET GLY GLU ALA ALA ALA
SEQRES 12 A 448 ILE PHE MET THR ALA THR PRO PRO GLY THR ARG ASP ALA
SEQRES 13 A 448 PHE PRO ASP SER ASN SER PRO ILE MET ASP THR GLU VAL
SEQRES 14 A 448 GLU VAL PRO GLU ARG ALA TRP SER SER GLY PHE ASP TRP
SEQRES 15 A 448 VAL THR ASP HIS SER GLY LYS THR VAL TRP PHE VAL PRO
SEQRES 16 A 448 SER VAL ARG ASN GLY ASN GLU ILE ALA ALA CYS LEU THR
SEQRES 17 A 448 LYS ALA GLY LYS ARG VAL ILE GLN LEU SER ARG LYS THR
SEQRES 18 A 448 PHE GLU THR GLU PHE GLN LYS THR LYS ASN GLN GLU TRP
SEQRES 19 A 448 ASP PHE VAL ILE THR THR ASP ILE SER GLU MET GLY ALA
SEQRES 20 A 448 ASN PHE LYS ALA ASP ARG VAL ILE ASP SER ARG ARG CYS
SEQRES 21 A 448 LEU LYS PRO VAL ILE LEU ASP GLY GLU ARG VAL ILE LEU
SEQRES 22 A 448 ALA GLY PRO MET PRO VAL THR HIS ALA SER ALA ALA GLN
SEQRES 23 A 448 ARG ARG GLY ARG ILE GLY ARG ASN PRO ASN LYS PRO GLY
SEQRES 24 A 448 ASP GLU TYR MET TYR GLY GLY GLY CYS ALA GLU THR ASP
SEQRES 25 A 448 GLU GLY HIS ALA HIS TRP LEU GLU ALA ARG MET LEU LEU
SEQRES 26 A 448 ASP ASN ILE TYR LEU GLN ASP GLY LEU ILE ALA SER LEU
SEQRES 27 A 448 TYR ARG PRO GLU ALA ASP LYS VAL ALA ALA ILE GLU GLY
SEQRES 28 A 448 GLU PHE LYS LEU ARG THR GLU GLN ARG LYS THR PHE VAL
SEQRES 29 A 448 GLU LEU MET LYS ARG GLY ASP LEU PRO VAL TRP LEU ALA
SEQRES 30 A 448 TYR GLN VAL ALA SER ALA GLY ILE THR TYR THR ASP ARG
SEQRES 31 A 448 ARG TRP CYS PHE ASP GLY THR THR ASN ASN THR ILE MET
SEQRES 32 A 448 GLU ASP SER VAL PRO ALA GLU VAL TRP THR LYS TYR GLY
SEQRES 33 A 448 GLU LYS ARG VAL LEU LYS PRO ARG TRP MET ASP ALA ARG
SEQRES 34 A 448 VAL CYS SER ASP HIS ALA ALA LEU LYS SER PHE LYS GLU
SEQRES 35 A 448 PHE ALA ALA GLY LYS ARG
HET SO4 A 701 5
HET SO4 A 702 5
HET SO4 A 703 5
HET EPE A 704 15
HETNAM SO4 SULFATE ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 EPE C8 H18 N2 O4 S
FORMUL 6 HOH *181(H2 O)
HELIX 1 AA1 ARG A 203 LYS A 215 1 13
HELIX 2 AA2 THR A 225 LEU A 236 1 12
HELIX 3 AA3 HIS A 263 GLN A 272 1 10
HELIX 4 AA4 ASP A 291 MET A 307 1 17
HELIX 5 AA5 PHE A 349 ASP A 354 1 6
HELIX 6 AA6 SER A 365 ALA A 379 1 15
HELIX 7 AA7 SER A 387 PHE A 395 1 9
HELIX 8 AA8 PHE A 395 GLN A 401 1 7
HELIX 9 AA9 ASP A 410 MET A 414 5 5
HELIX 10 AB1 THR A 449 GLY A 458 1 10
HELIX 11 AB2 HIS A 484 ASP A 495 1 12
HELIX 12 AB3 TYR A 508 ASP A 513 1 6
HELIX 13 AB4 ARG A 525 LYS A 537 1 13
HELIX 14 AB5 PRO A 542 ALA A 552 1 11
HELIX 15 AB6 ARG A 559 PHE A 563 5 5
HELIX 16 AB7 THR A 566 THR A 570 5 5
HELIX 17 AB8 ARG A 598 CYS A 600 5 3
HELIX 18 AB9 ASP A 602 ALA A 614 1 13
SHEET 1 AA1 6 GLN A 188 LEU A 192 0
SHEET 2 AA1 6 ALA A 311 MET A 315 1 O PHE A 314 N LEU A 192
SHEET 3 AA1 6 LEU A 281 ASP A 285 1 N MET A 284 O MET A 315
SHEET 4 AA1 6 THR A 219 ALA A 223 1 N LEU A 222 O ILE A 283
SHEET 5 AA1 6 VAL A 258 CYS A 262 1 O ASP A 259 N THR A 219
SHEET 6 AA1 6 VAL A 241 TYR A 243 1 N ARG A 242 O VAL A 258
SHEET 1 AA2 6 ILE A 333 GLU A 337 0
SHEET 2 AA2 6 ASP A 469 TYR A 473 1 O TYR A 471 N MET A 334
SHEET 3 AA2 6 ARG A 422 ASP A 425 1 N ASP A 425 O MET A 472
SHEET 4 AA2 6 THR A 359 PHE A 362 1 N VAL A 360 O ILE A 424
SHEET 5 AA2 6 PHE A 405 THR A 408 1 O VAL A 406 N TRP A 361
SHEET 6 AA2 6 VAL A 383 LEU A 386 1 N ILE A 384 O ILE A 407
SHEET 1 AA3 3 ARG A 428 LEU A 435 0
SHEET 2 AA3 3 ARG A 439 PRO A 447 -1 O ALA A 443 N LYS A 431
SHEET 3 AA3 3 MET A 595 ASP A 596 1 O MET A 595 N VAL A 440
SHEET 1 AA4 2 MET A 572 GLU A 573 0
SHEET 2 AA4 2 VAL A 576 PRO A 577 -1 O VAL A 576 N GLU A 573
SHEET 1 AA5 2 GLU A 579 TRP A 581 0
SHEET 2 AA5 2 LYS A 587 VAL A 589 -1 O ARG A 588 N VAL A 580
CISPEP 1 GLY A 444 PRO A 445 0 0.50
SITE 1 AC1 6 VAL A 366 ARG A 388 THR A 409 HOH A 846
SITE 2 AC1 6 HOH A 911 HOH A 912
SITE 1 AC2 6 ARG A 226 THR A 245 THR A 246 CYS A 262
SITE 2 AC2 6 THR A 265 HOH A 845
SITE 1 AC3 2 HIS A 603 HOH A 804
SITE 1 AC4 12 PRO A 196 GLY A 197 ALA A 198 GLY A 199
SITE 2 AC4 12 LYS A 200 THR A 201 ARG A 202 GLU A 286
SITE 3 AC4 12 ALA A 317 ARG A 459 ARG A 462 HOH A 899
CRYST1 53.532 68.534 56.883 90.00 92.40 90.00 P 1 21 1 2
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 0.018680 0.000000 0.000782 0.00000
SCALE2 0.000000 0.014591 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017595 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
