HEADER SIGNALING PROTEIN 03-SEP-18 6AKQ
TITLE THE PDZ TANDEM FRAGMENT OF A. AEOLICUS S2P HOMOLOG WITH THE PA12 TAG
TITLE 2 INSERTED BETWEEN THE RESIDUES 263 AND 267
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PDZ TANDEM FRAGMENT OF A. AEOLICUS SITE-2 PROTEASE HOMOLOG
COMPND 3 WITH THE PA TAG INSERTION;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 115-263 AND 267-292;
COMPND 6 EC: 3.4.24.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS VF5;
SOURCE 3 ORGANISM_TAXID: 224324;
SOURCE 4 STRAIN: VF5;
SOURCE 5 GENE: AQ_1964;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.TAMURA,R.OI,M.K.KANEKO,Y.KATO,T.NOGI
REVDAT 4 22-NOV-23 6AKQ 1 REMARK
REVDAT 3 15-NOV-23 6AKQ 1 LINK ATOM
REVDAT 2 03-APR-19 6AKQ 1 JRNL
REVDAT 1 13-FEB-19 6AKQ 0
JRNL AUTH R.TAMURA,R.OI,S.AKASHI,M.K.KANEKO,Y.KATO,T.NOGI
JRNL TITL APPLICATION OF THE NZ-1 FAB AS A CRYSTALLIZATION CHAPERONE
JRNL TITL 2 FOR PA TAG-INSERTED TARGET PROTEINS.
JRNL REF PROTEIN SCI. V. 28 823 2019
JRNL REFN ESSN 1469-896X
JRNL PMID 30666745
JRNL DOI 10.1002/PRO.3580
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0232
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 14388
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 717
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1037
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 51
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1447
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 99
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : -1.63000
REMARK 3 B33 (A**2) : 2.66000
REMARK 3 B12 (A**2) : 0.00000
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): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.319
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1513 ; 0.008 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2054 ; 1.671 ; 1.657
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 204 ; 5.890 ; 4.912
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 63 ;33.585 ;23.175
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 302 ;17.160 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;16.694 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 199 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1108 ; 0.009 ; 0.020
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): 752 ; 2.730 ; 2.896
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 941 ; 3.876 ; 4.316
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 761 ; 4.126 ; 3.375
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2269 ; 7.350 ;40.301
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6AKQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1300008930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-17
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15147
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 42.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.20
REMARK 200 R MERGE FOR SHELL (I) : 2.74600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3WKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23-25%(W/V) PEG 3350, 200MM BIS-TRIS
REMARK 280 -CL (PH 6.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.61700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.15800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.39950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.15800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.61700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.39950
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: 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 GLY A 113
REMARK 465 SER A 114
REMARK 465 GLU A 115
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 PRO A 263E 116.08 -39.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THREE RESIDUES OF THE HOST PROTEIN, THAT IS 264,
REMARK 999 265, AND 266, WERE DELETED AND 12 RESIDUES, GVAMPGAEDDVV, WERE
REMARK 999 INSERTED IN PLACE OF THEM.
DBREF 6AKQ A 115 263 UNP O67776 Y1964_AQUAE 115 263
DBREF 6AKQ A 267 292 UNP O67776 Y1964_AQUAE 267 292
SEQADV 6AKQ GLY A 113 UNP O67776 EXPRESSION TAG
SEQADV 6AKQ SER A 114 UNP O67776 EXPRESSION TAG
SEQADV 6AKQ GLY A 263A UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ VAL A 263B UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ ALA A 263C UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ MET A 263D UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ PRO A 263E UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ GLY A 263F UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ ALA A 263G UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ GLU A 263H UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ ASP A 263I UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ ASP A 263J UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ VAL A 263K UNP O67776 SEE SEQUENCE DETAILS
SEQADV 6AKQ VAL A 263L UNP O67776 SEE SEQUENCE DETAILS
SEQRES 1 A 189 GLY SER GLU VAL PRO LYS TYR LEU LYS GLU PRO VAL VAL
SEQRES 2 A 189 VAL GLY TYR VAL GLN ARG ASP SER ILE ALA GLN LYS ILE
SEQRES 3 A 189 GLY ILE LYS PRO GLY ASP LYS ILE ILE LYS ILE SNN GLY
SEQRES 4 A 189 TYR GLU VAL ARG THR TRP GLU ASP LEU ARG ASP ALA LEU
SEQRES 5 A 189 ILE ARG LEU SER LEU ASP GLY VAL LYS GLU THR THR LEU
SEQRES 6 A 189 PHE LEU GLU ARG ASN GLY GLU VAL LEU HIS LEU THR ILE
SEQRES 7 A 189 LYS VAL PRO ASN VAL GLN LYS GLY GLU GLU LEU GLY ILE
SEQRES 8 A 189 ALA PRO LEU VAL LYS PRO VAL VAL GLY GLY VAL LYS LYS
SEQRES 9 A 189 GLY SER PRO ALA ASP GLN VAL GLY ILE LYS PRO GLY ASP
SEQRES 10 A 189 LEU ILE LEU GLU VAL ASN GLY LYS LYS ILE ASN THR TRP
SEQRES 11 A 189 TYR GLU LEU VAL GLU GLU VAL ARG LYS SER GLN GLY LYS
SEQRES 12 A 189 ALA ILE LYS LEU LYS ILE LEU ARG GLY VAL ALA MET PRO
SEQRES 13 A 189 GLY ALA GLU ASP ASP VAL VAL MET ILE GLU LYS GLU LEU
SEQRES 14 A 189 ILE PRO ALA LYS ASP PRO LYS THR GLY THR TYR PHE ILE
SEQRES 15 A 189 GLY LEU PHE PRO LYS THR GLU
MODRES 6AKQ SNN A 150 ASN MODIFIED RESIDUE
HET SNN A 150 8
HETNAM SNN L-3-AMINOSUCCINIMIDE
FORMUL 1 SNN C4 H6 N2 O2
FORMUL 2 HOH *99(H2 O)
HELIX 1 AA1 PRO A 117 GLU A 122 5 6
HELIX 2 AA2 SER A 133 GLY A 139 1 7
HELIX 3 AA3 THR A 156 ASP A 170 1 15
HELIX 4 AA4 ASN A 194 GLY A 198 5 5
HELIX 5 AA5 SER A 218 VAL A 223 1 6
HELIX 6 AA6 THR A 241 LYS A 251 1 11
SHEET 1 AA1 4 VAL A 124 VAL A 125 0
SHEET 2 AA1 4 LYS A 145 LYS A 148 -1 O ILE A 146 N VAL A 124
SHEET 3 AA1 4 GLU A 174 ARG A 181 -1 O PHE A 178 N LYS A 148
SHEET 4 AA1 4 GLU A 184 LYS A 191 -1 O ILE A 190 N THR A 175
SHEET 1 AA2 2 TYR A 128 VAL A 129 0
SHEET 2 AA2 2 ILE A 203 ALA A 204 -1 O ALA A 204 N TYR A 128
SHEET 1 AA3 2 VAL A 211 VAL A 214 0
SHEET 2 AA3 2 LEU A 287 PRO A 289 -1 O PHE A 288 N GLY A 212
SHEET 1 AA4 4 LYS A 237 LYS A 238 0
SHEET 2 AA4 4 LEU A 230 VAL A 234 -1 N VAL A 234 O LYS A 237
SHEET 3 AA4 4 ILE A 257 MET A 263D-1 O LEU A 262 N LEU A 230
SHEET 4 AA4 4 ALA A 263G LEU A 272 -1 O ASP A 263J N VAL A 263B
SHEET 1 AA5 2 ALA A 275 LYS A 276 0
SHEET 2 AA5 2 TYR A 283 PHE A 284 -1 O PHE A 284 N ALA A 275
LINK C ILE A 149 N SNN A 150 1555 1555 1.32
LINK N1 SNN A 150 CA GLY A 151 1555 1555 1.47
CRYST1 49.234 54.799 68.316 90.00 90.00 90.00 P 21 21 21 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 0.020311 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014638 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
