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HEADER SIGNALING PROTEIN 11-JUN-24 8ZVO
TITLE ATKAI2 APO STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE ESTERASE KAI2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN DWARF-14-LIKE,PROTEIN D14-LIKE,PROTEIN HYPOSENSITIVE
COMPND 5 TO LIGHT,PROTEIN KARRIKIN INSENSITIVE 2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: KAI2, D14L, HTL, AT4G37470, F6G17.120;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 37762
KEYWDS KARRIKIN INSENSITIVE 2, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAKEGAMIE,J.TAKEUCHI,A.NAKAMURA
REVDAT 1 19-FEB-25 8ZVO 0
JRNL AUTH R.KUSHIHARA,A.NAKAMURA,K.TAKEGAMIE,Y.SETO,H.DORA,T.OHNISHI,
JRNL AUTH 2 Y.TODOROKI,J.TAKEUCHI
JRNL TITL STRUCTURAL REQUIREMENT OF KAI2 LIGANDS FOR ACTIVATION OF ITS
JRNL TITL 2 SIGNAL TRANSDUCTION
JRNL REF PROC.NATL.ACAD.SCI.USA 2025
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.2414779122
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 42770
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.690
REMARK 3 FREE R VALUE TEST SET COUNT : 2005
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 47.5400 - 3.5800 1.00 3063 148 0.1364 0.1428
REMARK 3 2 3.5800 - 2.8400 1.00 3004 144 0.1345 0.1586
REMARK 3 3 2.8400 - 2.4800 1.00 2979 147 0.1455 0.1822
REMARK 3 4 2.4800 - 2.2600 0.99 2974 148 0.1426 0.1856
REMARK 3 5 2.2600 - 2.0900 0.99 2936 144 0.1420 0.1556
REMARK 3 6 2.0900 - 1.9700 0.99 2954 149 0.1435 0.1694
REMARK 3 7 1.9700 - 1.8700 0.99 2928 145 0.1389 0.1709
REMARK 3 8 1.8700 - 1.7900 0.98 2928 144 0.1449 0.1698
REMARK 3 9 1.7900 - 1.7200 0.98 2919 141 0.1572 0.2054
REMARK 3 10 1.7200 - 1.6600 0.98 2910 142 0.1807 0.2197
REMARK 3 11 1.6600 - 1.6100 0.98 2899 154 0.1676 0.2039
REMARK 3 12 1.6100 - 1.5600 0.97 2876 127 0.1649 0.1857
REMARK 3 13 1.5600 - 1.5200 0.97 2911 150 0.1762 0.2143
REMARK 3 14 1.5200 - 1.4900 0.85 2484 122 0.2310 0.2610
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.125
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.472
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.93
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 2316
REMARK 3 ANGLE : 0.913 3158
REMARK 3 CHIRALITY : 0.088 353
REMARK 3 PLANARITY : 0.006 414
REMARK 3 DIHEDRAL : 14.158 847
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 8ZVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048601.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0-9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AICHISR
REMARK 200 BEAMLINE : BL2S1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42773
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 47.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.9500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.450
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: 4JYM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL (PH 7.0 TO 9.0) WITH
REMARK 280 1.25 TO 2.0 M AMMONIUM SULFATE AND 12% (V/V) GLYCEROL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 27.89500
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: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11050 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 ALA A 269
REMARK 465 MET A 270
REMARK 465 GLU A 271
REMARK 465 ASN A 272
REMARK 465 LEU A 273
REMARK 465 TYR A 274
REMARK 465 PHE A 275
REMARK 465 GLN A 276
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 OE1 GLU A 6 O HOH A 401 2.00
REMARK 500 O HOH A 444 O HOH A 619 2.07
REMARK 500 NH2 ARG A 176 O HOH A 402 2.12
REMARK 500 O HOH A 528 O HOH A 686 2.13
REMARK 500 O HOH A 606 O HOH A 744 2.14
REMARK 500 O HOH A 652 O HOH A 692 2.14
REMARK 500 O HOH A 697 O HOH A 723 2.16
REMARK 500 O HOH A 497 O HOH A 658 2.17
REMARK 500 OE2 GLU A 6 O HOH A 403 2.17
REMARK 500 O HOH A 517 O HOH A 728 2.19
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 A 406 O HOH A 470 2544 2.03
REMARK 500 O HOH A 685 O HOH A 692 2555 2.16
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 THR A 28 -164.12 -119.92
REMARK 500 SER A 95 -125.82 59.29
REMARK 500 ARG A 123 123.00 -171.15
REMARK 500 LEU A 247 56.40 -119.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 762 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A 763 DISTANCE = 7.02 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8ZVN RELATED DB: PDB
DBREF 8ZVO A 1 270 UNP Q9SZU7 KAI2_ARATH 1 270
SEQADV 8ZVO GLU A 271 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8ZVO ASN A 272 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8ZVO LEU A 273 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8ZVO TYR A 274 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8ZVO PHE A 275 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8ZVO GLN A 276 UNP Q9SZU7 EXPRESSION TAG
SEQRES 1 A 276 MET GLY VAL VAL GLU GLU ALA HIS ASN VAL LYS VAL ILE
SEQRES 2 A 276 GLY SER GLY GLU ALA THR ILE VAL LEU GLY HIS GLY PHE
SEQRES 3 A 276 GLY THR ASP GLN SER VAL TRP LYS HIS LEU VAL PRO HIS
SEQRES 4 A 276 LEU VAL ASP ASP TYR ARG VAL VAL LEU TYR ASP ASN MET
SEQRES 5 A 276 GLY ALA GLY THR THR ASN PRO ASP TYR PHE ASP PHE ASP
SEQRES 6 A 276 ARG TYR SER ASN LEU GLU GLY TYR SER PHE ASP LEU ILE
SEQRES 7 A 276 ALA ILE LEU GLU ASP LEU LYS ILE GLU SER CYS ILE PHE
SEQRES 8 A 276 VAL GLY HIS SER VAL SER ALA MET ILE GLY VAL LEU ALA
SEQRES 9 A 276 SER LEU ASN ARG PRO ASP LEU PHE SER LYS ILE VAL MET
SEQRES 10 A 276 ILE SER ALA SER PRO ARG TYR VAL ASN ASP VAL ASP TYR
SEQRES 11 A 276 GLN GLY GLY PHE GLU GLN GLU ASP LEU ASN GLN LEU PHE
SEQRES 12 A 276 GLU ALA ILE ARG SER ASN TYR LYS ALA TRP CYS LEU GLY
SEQRES 13 A 276 PHE ALA PRO LEU ALA VAL GLY GLY ASP MET ASP SER ILE
SEQRES 14 A 276 ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 A 276 PRO ASP ILE ALA LEU SER VAL GLY GLN THR ILE PHE GLN
SEQRES 16 A 276 SER ASP MET ARG GLN ILE LEU PRO PHE VAL THR VAL PRO
SEQRES 17 A 276 CYS HIS ILE LEU GLN SER VAL LYS ASP LEU ALA VAL PRO
SEQRES 18 A 276 VAL VAL VAL SER GLU TYR LEU HIS ALA ASN LEU GLY CYS
SEQRES 19 A 276 GLU SER VAL VAL GLU VAL ILE PRO SER ASP GLY HIS LEU
SEQRES 20 A 276 PRO GLN LEU SER SER PRO ASP SER VAL ILE PRO VAL ILE
SEQRES 21 A 276 LEU ARG HIS ILE ARG ASN ASP ILE ALA MET GLU ASN LEU
SEQRES 22 A 276 TYR PHE GLN
HET GOL A 301 12
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 12
HET SO4 A 308 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 7(C3 H8 O3)
FORMUL 9 SO4 O4 S 2-
FORMUL 10 HOH *363(H2 O)
HELIX 1 AA1 GLY A 2 HIS A 8 1 7
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 ASN A 58 PHE A 62 5 5
HELIX 5 AA5 ASP A 65 SER A 68 5 4
HELIX 6 AA6 ASN A 69 LEU A 84 1 16
HELIX 7 AA7 SER A 95 ARG A 108 1 14
HELIX 8 AA8 GLU A 135 ASN A 149 1 15
HELIX 9 AA9 ASN A 149 GLY A 163 1 15
HELIX 10 AB1 SER A 168 MET A 181 1 14
HELIX 11 AB2 ARG A 182 GLN A 195 1 14
HELIX 12 AB3 MET A 198 VAL A 205 5 8
HELIX 13 AB4 PRO A 221 LEU A 232 1 12
HELIX 14 AB5 LEU A 247 SER A 252 1 6
HELIX 15 AB6 SER A 252 ASN A 266 1 15
SHEET 1 AA1 7 LYS A 11 ILE A 13 0
SHEET 2 AA1 7 ARG A 45 LEU A 48 -1 O VAL A 46 N ILE A 13
SHEET 3 AA1 7 THR A 19 GLY A 23 1 N ILE A 20 O VAL A 47
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O HIS A 94 N GLY A 23
SHEET 5 AA1 7 PHE A 112 ILE A 118 1 O VAL A 116 N PHE A 91
SHEET 6 AA1 7 CYS A 209 LYS A 216 1 O HIS A 210 N MET A 117
SHEET 7 AA1 7 SER A 236 ASP A 244 1 O VAL A 237 N ILE A 211
CRYST1 50.700 55.790 52.870 90.00 115.94 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 0.019724 0.000000 0.009594 0.00000
SCALE2 0.000000 0.017924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021033 0.00000
TER 2208 ILE A 268
MASTER 290 0 8 15 7 0 0 6 2492 1 59 22
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