HEADER UNKNOWN FUNCTION 15-JUN-10 3NI8
TITLE CRYSTAL STRUCTURE OF PFC0360W, AN HSP90 ACTIVATOR FROM PLASMODIUM
TITLE 2 FALCIPARUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PFC0360W PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 5833;
SOURCE 4 GENE: PFC0360W;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15MLH
KEYWDS HEAT SHOCK, MALARIA, ATPASE, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,A.HUTCHINSON,H.SULLIVAN,F.MACKENZIE,I.KOZIERADZKI,
AUTHOR 2 D.COSSAR,A.BOCHKAREV,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,
AUTHOR 3 R.HUI,J.C.PIZZARO,T.HILLS,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 21-FEB-24 3NI8 1 REMARK SEQADV
REVDAT 2 08-NOV-17 3NI8 1 REMARK
REVDAT 1 11-AUG-10 3NI8 0
JRNL AUTH A.K.WERNIMONT,A.HUTCHINSON,H.SULLIVAN,F.MACKENZIE,
JRNL AUTH 2 I.KOZIERADZKI,D.COSSAR,A.BOCHKAREV,C.H.ARROWSMITH,
JRNL AUTH 3 A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,R.HUI,J.C.PIZZARO,T.HILLS
JRNL TITL CRYSTAL STRUCTURE OF PFC0360W, AN HSP90 ACTIVATOR FROM
JRNL TITL 2 PLASMODIUM FALCIPARUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 8402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 394
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 587
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 27
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : 0.20000
REMARK 3 B12 (A**2) : -0.07000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.266
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.205
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.811
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1256 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1708 ; 1.392 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 155 ; 6.739 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 61 ;37.376 ;24.754
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 216 ;16.642 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;27.167 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 179 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 971 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 742 ; 0.609 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1215 ; 1.201 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 514 ; 1.851 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 493 ; 3.175 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3NI8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059861.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8517
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 32.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : 0.15900
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 9.00
REMARK 200 R MERGE FOR SHELL (I) : 0.83600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.420
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ISOPROPANOL, 20% PEG 4000, 0.1M NA
REMARK 280 CITRATE PH 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 14.76267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.52533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.52533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 14.76267
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 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 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 ARG A 11
REMARK 465 GLU A 12
REMARK 465 ASN A 13
REMARK 465 LEU A 14
REMARK 465 TYR A 15
REMARK 465 PHE A 16
REMARK 465 GLN A 17
REMARK 465 LYS A 158
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 ND1 HIS A 81 O HOH A 198 2.19
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 ASN A 143 -74.15 -115.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 85 LYS A 86 149.37
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 IPA A 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 161
DBREF 3NI8 A 19 158 UNP Q689C4 Q689C4_PLAFA 1 140
SEQADV 3NI8 MET A 1 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 HIS A 2 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 HIS A 3 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 HIS A 4 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 HIS A 5 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 HIS A 6 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 HIS A 7 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 SER A 8 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 SER A 9 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 GLY A 10 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 ARG A 11 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 GLU A 12 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 ASN A 13 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 LEU A 14 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 TYR A 15 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 PHE A 16 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 GLN A 17 UNP Q689C4 EXPRESSION TAG
SEQADV 3NI8 GLY A 18 UNP Q689C4 EXPRESSION TAG
SEQRES 1 A 158 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 158 LEU TYR PHE GLN GLY MET SER PHE GLU ILE THR GLU GLU
SEQRES 3 A 158 TYR TYR VAL PRO PRO GLU VAL LEU PHE ASN ALA PHE THR
SEQRES 4 A 158 ASP ALA TYR THR LEU THR ARG LEU SER ARG GLY SER LEU
SEQRES 5 A 158 ALA GLU VAL ASP LEU LYS VAL GLY GLY LYS PHE SER LEU
SEQRES 6 A 158 PHE SER GLY SER ILE LEU GLY GLU PHE THR GLU ILE THR
SEQRES 7 A 158 LYS PRO HIS LYS ILE VAL GLU LYS TRP LYS PHE ARG ASP
SEQRES 8 A 158 TRP ASN GLU CYS ASP TYR SER THR VAL THR VAL GLU PHE
SEQRES 9 A 158 ILE SER VAL LYS GLU ASN HIS THR LYS LEU LYS LEU THR
SEQRES 10 A 158 HIS ASN ASN ILE PRO ALA SER ASN LYS TYR ASN GLU GLY
SEQRES 11 A 158 GLY VAL LEU GLU ARG CYS LYS ASN GLY TRP THR GLN ASN
SEQRES 12 A 158 PHE LEU HIS ASN ILE GLU VAL ILE LEU GLY TYR PRO LYS
SEQRES 13 A 158 LYS LYS
HET IPA A 159 4
HET IPA A 160 4
HET GOL A 161 6
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM GOL GLYCEROL
HETSYN IPA 2-PROPANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 IPA 2(C3 H8 O)
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *59(H2 O)
HELIX 1 1 PRO A 30 ASP A 40 1 11
HELIX 2 2 ASP A 40 SER A 48 1 9
HELIX 3 3 GLY A 131 ASN A 143 1 13
HELIX 4 4 ASN A 143 ILE A 151 1 9
SHEET 1 A 7 PHE A 21 TYR A 27 0
SHEET 2 A 7 HIS A 111 ASN A 119 -1 O LEU A 114 N GLU A 25
SHEET 3 A 7 SER A 98 LYS A 108 -1 N ILE A 105 O LYS A 113
SHEET 4 A 7 LYS A 82 PHE A 89 -1 N TRP A 87 O SER A 98
SHEET 5 A 7 ILE A 70 THR A 78 -1 N LEU A 71 O LYS A 88
SHEET 6 A 7 LYS A 62 LEU A 65 -1 N LEU A 65 O ILE A 70
SHEET 7 A 7 GLU A 54 VAL A 55 -1 N GLU A 54 O SER A 64
CISPEP 1 LYS A 79 PRO A 80 0 -3.84
SITE 1 AC1 2 PHE A 38 GLU A 85
SITE 1 AC2 2 PHE A 21 LYS A 137
SITE 1 AC3 5 TYR A 42 ARG A 46 ARG A 49 HIS A 146
SITE 2 AC3 5 ILE A 151
CRYST1 96.658 96.658 44.288 90.00 90.00 120.00 P 31 2 1 6
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 0.010346 0.005973 0.000000 0.00000
SCALE2 0.000000 0.011946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022579 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
