HEADER SIGNALING PROTEIN/PROTEIN BINDING 19-APR-11 3AXY
TITLE STRUCTURE OF FLORIGEN ACTIVATION COMPLEX CONSISTING OF RICE FLORIGEN
TITLE 2 HD3A, 14-3-3 PROTEIN GF14 AND RICE FD HOMOLOG OSFD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN HEADING DATE 3A;
COMPND 3 CHAIN: A, B, G, H;
COMPND 4 FRAGMENT: UNP RESIDUES 6-170;
COMPND 5 SYNONYM: RICE FLORIGEN HD3A, FT-LIKE PROTEIN A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 14-3-3-LIKE PROTEIN GF14-C;
COMPND 10 CHAIN: C, D, I, J;
COMPND 11 FRAGMENT: UNP RESIDUES 1-235;
COMPND 12 SYNONYM: G-BOX FACTOR 14-3-3 HOMOLOG C;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: RICE FD HOMOLOG OSFD1;
COMPND 16 CHAIN: E, F, K, L;
COMPND 17 FRAGMENT: C-TERMINAL MOTIF;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE 3 ORGANISM_COMMON: JAPANESE RICE;
SOURCE 4 ORGANISM_TAXID: 39947;
SOURCE 5 GENE: HD3A, LOC_OS06G06320, OS06G0157700, OSJ_20191, P0046E09.30,
SOURCE 6 P0702F05.10;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCOLD;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE 14 ORGANISM_COMMON: JAPANESE RICE;
SOURCE 15 ORGANISM_TAXID: 39947;
SOURCE 16 GENE: GF14C, LOC_OS08G33370, OJ1124_B05.7, OS08G0430500;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PGEX6P3;
SOURCE 22 MOL_ID: 3;
SOURCE 23 SYNTHETIC: YES;
SOURCE 24 OTHER_DETAILS: OSFD1(187-195) FRAGMENT, PHOSPHORYLATED AT S192
KEYWDS PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN, 14-3-3 PROTEIN, BZIP
KEYWDS 2 PROTEIN, FLORAL INDUCTION, TRANSCRIPTIONAL ACTIVATOR, SIGNALING
KEYWDS 3 PROTEIN, DNA BINDING, PHOSPHORYLATION, NUCLEUS, SIGNALING PROTEIN-
KEYWDS 4 PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR I.OHKI,K.FURUITA,K.HAYASHI,K.TAOKA,H.TSUJI,A.NAKAGAWA,K.SHIMAMOTO,
AUTHOR 2 C.KOJIMA
REVDAT 3 01-NOV-23 3AXY 1 SEQADV LINK
REVDAT 2 12-OCT-11 3AXY 1 JRNL
REVDAT 1 03-AUG-11 3AXY 0
JRNL AUTH K.TAOKA,I.OHKI,H.TSUJI,K.FURUITA,K.HAYASHI,T.YANASE,
JRNL AUTH 2 M.YAMAGUCHI,C.NAKASHIMA,Y.A.PURWESTRI,S.TAMAKI,Y.OGAKI,
JRNL AUTH 3 C.SHIMADA,A.NAKAGAWA,C.KOJIMA,K.SHIMAMOTO
JRNL TITL 14-3-3 PROTEINS ACT AS INTRACELLULAR RECEPTORS FOR RICE HD3A
JRNL TITL 2 FLORIGEN
JRNL REF NATURE V. 476 332 2011
JRNL REFN ISSN 0028-0836
JRNL PMID 21804566
JRNL DOI 10.1038/NATURE10272
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 92311
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 7138
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6692
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 522
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12974
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 777
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : -1.29000
REMARK 3 B33 (A**2) : 0.07000
REMARK 3 B12 (A**2) : 1.04000
REMARK 3 B13 (A**2) : 1.33000
REMARK 3 B23 (A**2) : 0.71000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.342
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.264
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.188
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.325
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.917
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13222 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17909 ; 0.871 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1618 ; 7.830 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 628 ;40.001 ;24.013
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2325 ;21.547 ;15.026
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 100 ;19.867 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1998 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10008 ; 0.014 ; 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): 8133 ; 1.202 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13127 ; 2.117 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5089 ; 3.574 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4782 ; 5.388 ; 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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 170
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0710 34.6860 -15.2890
REMARK 3 T TENSOR
REMARK 3 T11: 0.0255 T22: 0.0155
REMARK 3 T33: 0.0570 T12: 0.0153
REMARK 3 T13: 0.0136 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.9919 L22: 0.8924
REMARK 3 L33: 0.6179 L12: -0.4615
REMARK 3 L13: -0.1300 L23: 0.2512
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: 0.0076 S13: -0.0740
REMARK 3 S21: -0.0336 S22: -0.0479 S23: 0.0782
REMARK 3 S31: -0.0457 S32: -0.0026 S33: 0.0473
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 170
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6600 -10.2760 21.7640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0183 T22: 0.0310
REMARK 3 T33: 0.0422 T12: 0.0232
REMARK 3 T13: 0.0221 T23: 0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 0.7437 L22: 1.1519
REMARK 3 L33: 0.8537 L12: -0.0766
REMARK 3 L13: 0.0011 L23: -0.2299
REMARK 3 S TENSOR
REMARK 3 S11: 0.0328 S12: 0.0391 S13: 0.0750
REMARK 3 S21: 0.0030 S22: 0.0430 S23: 0.1158
REMARK 3 S31: -0.0140 S32: -0.0418 S33: -0.0757
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 235
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6230 24.0890 -20.3590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0412 T22: 0.0389
REMARK 3 T33: 0.0232 T12: 0.0193
REMARK 3 T13: 0.0232 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.2037 L22: 0.2869
REMARK 3 L33: 0.9523 L12: -0.0837
REMARK 3 L13: 0.3373 L23: -0.2286
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: 0.0732 S13: 0.0316
REMARK 3 S21: 0.0007 S22: -0.0662 S23: 0.0037
REMARK 3 S31: 0.0154 S32: 0.1308 S33: 0.0508
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 235
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7420 4.9460 11.0480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0294 T22: 0.0414
REMARK 3 T33: 0.0246 T12: -0.0200
REMARK 3 T13: -0.0071 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.1248 L22: 0.7285
REMARK 3 L33: 0.9976 L12: 0.0389
REMARK 3 L13: -0.1530 L23: -0.3562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0388 S12: -0.0505 S13: -0.0489
REMARK 3 S21: 0.0549 S22: -0.1345 S23: -0.0254
REMARK 3 S31: 0.0036 S32: 0.1096 S33: 0.0958
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 5 G 169
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9900 -27.1640 32.9620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0341 T22: 0.0243
REMARK 3 T33: 0.0073 T12: 0.0040
REMARK 3 T13: 0.0040 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.5549 L22: 0.4892
REMARK 3 L33: 1.3989 L12: 0.1021
REMARK 3 L13: -0.4107 L23: -0.0198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0048 S12: -0.0539 S13: -0.0418
REMARK 3 S21: 0.0213 S22: -0.0089 S23: 0.0126
REMARK 3 S31: -0.0771 S32: 0.0757 S33: 0.0040
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 5 H 170
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6920 23.2120 9.2330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0575 T22: 0.0128
REMARK 3 T33: 0.0091 T12: 0.0147
REMARK 3 T13: 0.0122 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.1331 L22: 1.1118
REMARK 3 L33: 0.6815 L12: 0.1540
REMARK 3 L13: -0.0783 L23: -0.3084
REMARK 3 S TENSOR
REMARK 3 S11: 0.0430 S12: -0.0414 S13: 0.0203
REMARK 3 S21: 0.1696 S22: -0.0208 S23: 0.0081
REMARK 3 S31: 0.0137 S32: 0.0401 S33: -0.0223
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
REMARK 4
REMARK 4 3AXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000029834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-09
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101603
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
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: PDB CODE 1WKP FOR HD3A, 2O98 FOR GF14C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.5), 0.2M AMMONIUM
REMARK 280 SULFATE, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
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 1
REMARK 465 PRO A 2
REMARK 465 GLY A 3
REMARK 465 HIS A 4
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 HIS B 4
REMARK 465 GLY C -4
REMARK 465 PRO C -3
REMARK 465 LEU C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 GLY D -4
REMARK 465 PRO D -3
REMARK 465 LEU D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 LEU E 187
REMARK 465 GLN E 188
REMARK 465 LEU F 187
REMARK 465 GLN F 188
REMARK 465 GLY G 1
REMARK 465 PRO G 2
REMARK 465 GLY G 3
REMARK 465 HIS G 4
REMARK 465 ALA G 170
REMARK 465 GLY H 1
REMARK 465 PRO H 2
REMARK 465 GLY H 3
REMARK 465 HIS H 4
REMARK 465 GLY I -4
REMARK 465 PRO I -3
REMARK 465 LEU I -2
REMARK 465 GLY I -1
REMARK 465 SER I 0
REMARK 465 GLY J -4
REMARK 465 PRO J -3
REMARK 465 LEU J -2
REMARK 465 GLY J -1
REMARK 465 SER J 0
REMARK 465 MET J 1
REMARK 465 LEU K 187
REMARK 465 GLN K 188
REMARK 465 LEU L 187
REMARK 465 GLN L 188
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 NH2 ARG J 58 O1P SEP L 192 2.08
REMARK 500 O GLU J 77 OG1 THR J 81 2.10
REMARK 500 O ASP C 34 O HOH C 752 2.16
REMARK 500 OE1 GLU B 106 O HOH B 344 2.18
REMARK 500 OE1 GLU J 72 O HOH J 747 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 ARG A 15 16.56 59.54
REMARK 500 SER A 27 -0.79 -140.33
REMARK 500 ASN A 41 110.80 -39.96
REMARK 500 ASP A 81 79.28 -151.87
REMARK 500 THR A 98 -9.48 92.46
REMARK 500 THR A 99 -148.43 -111.30
REMARK 500 ARG A 168 128.14 -27.43
REMARK 500 ASP B 81 66.65 -152.48
REMARK 500 TRP B 90 137.64 -176.22
REMARK 500 THR B 99 -138.69 -121.95
REMARK 500 PRO B 138 157.11 -43.36
REMARK 500 ASP C 34 -128.49 -81.12
REMARK 500 GLU C 37 112.03 30.37
REMARK 500 HIS C 108 -63.66 -125.00
REMARK 500 LYS D 31 27.73 -73.57
REMARK 500 VAL D 35 29.53 45.24
REMARK 500 GLU D 36 75.75 -170.87
REMARK 500 HIS D 108 -55.77 -122.37
REMARK 500 PHE D 136 -32.85 -138.36
REMARK 500 THR G 99 -147.05 -114.70
REMARK 500 PRO G 138 149.26 -35.55
REMARK 500 ARG G 168 128.62 -20.01
REMARK 500 TRP H 90 138.57 -171.59
REMARK 500 THR H 99 -144.55 -116.55
REMARK 500 GLN H 133 135.08 -170.83
REMARK 500 PRO H 138 150.01 -46.65
REMARK 500 ARG I 18 75.29 -111.75
REMARK 500 THR I 32 -99.18 -122.87
REMARK 500 VAL I 33 87.13 2.71
REMARK 500 VAL I 35 25.30 -75.14
REMARK 500 GLU I 36 -137.83 46.31
REMARK 500 GLU I 37 77.26 21.58
REMARK 500 LEU I 38 138.08 -15.43
REMARK 500 HIS I 108 -54.25 -120.64
REMARK 500 ARG J 3 -52.76 -129.67
REMARK 500 ASP J 34 77.05 43.76
REMARK 500 GLU J 37 122.49 71.43
REMARK 500 ARG J 74 16.23 -154.11
REMARK 500 ASN J 76 72.45 -110.62
REMARK 500 HIS J 108 -60.75 -126.32
REMARK 500 THR J 114 -64.62 -109.54
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 C 36 GLU C 37 137.32
REMARK 500 GLU C 37 LEU C 38 148.58
REMARK 500 VAL I 33 ASP I 34 -131.16
REMARK 500 ASP I 34 VAL I 35 141.62
REMARK 500 GLU I 37 LEU I 38 141.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR C 129 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3AXY A 6 170 UNP Q93WI9 HD3A_ORYSJ 6 170
DBREF 3AXY B 6 170 UNP Q93WI9 HD3A_ORYSJ 6 170
DBREF 3AXY C 1 235 UNP Q6ZKC0 14333_ORYSJ 1 235
DBREF 3AXY D 1 235 UNP Q6ZKC0 14333_ORYSJ 1 235
DBREF 3AXY G 6 170 UNP Q93WI9 HD3A_ORYSJ 6 170
DBREF 3AXY H 6 170 UNP Q93WI9 HD3A_ORYSJ 6 170
DBREF 3AXY I 1 235 UNP Q6ZKC0 14333_ORYSJ 1 235
DBREF 3AXY J 1 235 UNP Q6ZKC0 14333_ORYSJ 1 235
DBREF 3AXY E 187 195 PDB 3AXY 3AXY 187 195
DBREF 3AXY F 187 195 PDB 3AXY 3AXY 187 195
DBREF 3AXY K 187 195 PDB 3AXY 3AXY 187 195
DBREF 3AXY L 187 195 PDB 3AXY 3AXY 187 195
SEQADV 3AXY GLY A 1 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY PRO A 2 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY GLY A 3 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY HIS A 4 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY MET A 5 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY LEU A 43 UNP Q93WI9 CYS 43 ENGINEERED MUTATION
SEQADV 3AXY SER A 109 UNP Q93WI9 CYS 109 ENGINEERED MUTATION
SEQADV 3AXY SER A 166 UNP Q93WI9 CYS 166 ENGINEERED MUTATION
SEQADV 3AXY GLY B 1 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY PRO B 2 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY GLY B 3 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY HIS B 4 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY MET B 5 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY LEU B 43 UNP Q93WI9 CYS 43 ENGINEERED MUTATION
SEQADV 3AXY SER B 109 UNP Q93WI9 CYS 109 ENGINEERED MUTATION
SEQADV 3AXY SER B 166 UNP Q93WI9 CYS 166 ENGINEERED MUTATION
SEQADV 3AXY GLY C -4 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY PRO C -3 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY LEU C -2 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY GLY C -1 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY SER C 0 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY GLY D -4 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY PRO D -3 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY LEU D -2 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY GLY D -1 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY SER D 0 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY GLY G 1 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY PRO G 2 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY GLY G 3 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY HIS G 4 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY MET G 5 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY LEU G 43 UNP Q93WI9 CYS 43 ENGINEERED MUTATION
SEQADV 3AXY SER G 109 UNP Q93WI9 CYS 109 ENGINEERED MUTATION
SEQADV 3AXY SER G 166 UNP Q93WI9 CYS 166 ENGINEERED MUTATION
SEQADV 3AXY GLY H 1 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY PRO H 2 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY GLY H 3 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY HIS H 4 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY MET H 5 UNP Q93WI9 EXPRESSION TAG
SEQADV 3AXY LEU H 43 UNP Q93WI9 CYS 43 ENGINEERED MUTATION
SEQADV 3AXY SER H 109 UNP Q93WI9 CYS 109 ENGINEERED MUTATION
SEQADV 3AXY SER H 166 UNP Q93WI9 CYS 166 ENGINEERED MUTATION
SEQADV 3AXY GLY I -4 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY PRO I -3 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY LEU I -2 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY GLY I -1 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY SER I 0 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY GLY J -4 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY PRO J -3 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY LEU J -2 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY GLY J -1 UNP Q6ZKC0 EXPRESSION TAG
SEQADV 3AXY SER J 0 UNP Q6ZKC0 EXPRESSION TAG
SEQRES 1 A 170 GLY PRO GLY HIS MET ARG ASP ARG ASP PRO LEU VAL VAL
SEQRES 2 A 170 GLY ARG VAL VAL GLY ASP VAL LEU ASP ALA PHE VAL ARG
SEQRES 3 A 170 SER THR ASN LEU LYS VAL THR TYR GLY SER LYS THR VAL
SEQRES 4 A 170 SER ASN GLY LEU GLU LEU LYS PRO SER MET VAL THR HIS
SEQRES 5 A 170 GLN PRO ARG VAL GLU VAL GLY GLY ASN ASP MET ARG THR
SEQRES 6 A 170 PHE TYR THR LEU VAL MET VAL ASP PRO ASP ALA PRO SER
SEQRES 7 A 170 PRO SER ASP PRO ASN LEU ARG GLU TYR LEU HIS TRP LEU
SEQRES 8 A 170 VAL THR ASP ILE PRO GLY THR THR ALA ALA SER PHE GLY
SEQRES 9 A 170 GLN GLU VAL MET SER TYR GLU SER PRO ARG PRO THR MET
SEQRES 10 A 170 GLY ILE HIS ARG LEU VAL PHE VAL LEU PHE GLN GLN LEU
SEQRES 11 A 170 GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN ASN
SEQRES 12 A 170 PHE ASN THR LYS ASP PHE ALA GLU LEU TYR ASN LEU GLY
SEQRES 13 A 170 SER PRO VAL ALA ALA VAL TYR PHE ASN SER GLN ARG GLU
SEQRES 14 A 170 ALA
SEQRES 1 B 170 GLY PRO GLY HIS MET ARG ASP ARG ASP PRO LEU VAL VAL
SEQRES 2 B 170 GLY ARG VAL VAL GLY ASP VAL LEU ASP ALA PHE VAL ARG
SEQRES 3 B 170 SER THR ASN LEU LYS VAL THR TYR GLY SER LYS THR VAL
SEQRES 4 B 170 SER ASN GLY LEU GLU LEU LYS PRO SER MET VAL THR HIS
SEQRES 5 B 170 GLN PRO ARG VAL GLU VAL GLY GLY ASN ASP MET ARG THR
SEQRES 6 B 170 PHE TYR THR LEU VAL MET VAL ASP PRO ASP ALA PRO SER
SEQRES 7 B 170 PRO SER ASP PRO ASN LEU ARG GLU TYR LEU HIS TRP LEU
SEQRES 8 B 170 VAL THR ASP ILE PRO GLY THR THR ALA ALA SER PHE GLY
SEQRES 9 B 170 GLN GLU VAL MET SER TYR GLU SER PRO ARG PRO THR MET
SEQRES 10 B 170 GLY ILE HIS ARG LEU VAL PHE VAL LEU PHE GLN GLN LEU
SEQRES 11 B 170 GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN ASN
SEQRES 12 B 170 PHE ASN THR LYS ASP PHE ALA GLU LEU TYR ASN LEU GLY
SEQRES 13 B 170 SER PRO VAL ALA ALA VAL TYR PHE ASN SER GLN ARG GLU
SEQRES 14 B 170 ALA
SEQRES 1 C 240 GLY PRO LEU GLY SER MET SER ARG GLU GLU ASN VAL TYR
SEQRES 2 C 240 MET ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU GLU
SEQRES 3 C 240 MET VAL GLU TYR MET GLU LYS VAL ALA LYS THR VAL ASP
SEQRES 4 C 240 VAL GLU GLU LEU THR VAL GLU GLU ARG ASN LEU LEU SER
SEQRES 5 C 240 VAL ALA TYR LYS ASN VAL ILE GLY ALA ARG ARG ALA SER
SEQRES 6 C 240 TRP ARG ILE VAL SER SER ILE GLU GLN LYS GLU GLU GLY
SEQRES 7 C 240 ARG GLY ASN GLU GLU HIS VAL THR LEU ILE LYS GLU TYR
SEQRES 8 C 240 ARG GLY LYS ILE GLU ALA GLU LEU SER LYS ILE CYS ASP
SEQRES 9 C 240 GLY ILE LEU LYS LEU LEU ASP SER HIS LEU VAL PRO SER
SEQRES 10 C 240 SER THR ALA ALA GLU SER LYS VAL PHE TYR LEU LYS MET
SEQRES 11 C 240 LYS GLY ASP TYR HIS ARG TYR LEU ALA GLU PHE LYS THR
SEQRES 12 C 240 GLY ALA GLU ARG LYS GLU ALA ALA GLU SER THR MET VAL
SEQRES 13 C 240 ALA TYR LYS ALA ALA GLN ASP ILE ALA LEU ALA ASP LEU
SEQRES 14 C 240 ALA PRO THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN
SEQRES 15 C 240 PHE SER VAL PHE TYR TYR GLU ILE LEU ASN SER PRO ASP
SEQRES 16 C 240 LYS ALA CYS ASN LEU ALA LYS GLN ALA PHE ASP GLU ALA
SEQRES 17 C 240 ILE SER GLU LEU ASP THR LEU GLY GLU GLU SER TYR LYS
SEQRES 18 C 240 ASP SER THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU
SEQRES 19 C 240 THR LEU TRP THR SER ASP
SEQRES 1 D 240 GLY PRO LEU GLY SER MET SER ARG GLU GLU ASN VAL TYR
SEQRES 2 D 240 MET ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU GLU
SEQRES 3 D 240 MET VAL GLU TYR MET GLU LYS VAL ALA LYS THR VAL ASP
SEQRES 4 D 240 VAL GLU GLU LEU THR VAL GLU GLU ARG ASN LEU LEU SER
SEQRES 5 D 240 VAL ALA TYR LYS ASN VAL ILE GLY ALA ARG ARG ALA SER
SEQRES 6 D 240 TRP ARG ILE VAL SER SER ILE GLU GLN LYS GLU GLU GLY
SEQRES 7 D 240 ARG GLY ASN GLU GLU HIS VAL THR LEU ILE LYS GLU TYR
SEQRES 8 D 240 ARG GLY LYS ILE GLU ALA GLU LEU SER LYS ILE CYS ASP
SEQRES 9 D 240 GLY ILE LEU LYS LEU LEU ASP SER HIS LEU VAL PRO SER
SEQRES 10 D 240 SER THR ALA ALA GLU SER LYS VAL PHE TYR LEU LYS MET
SEQRES 11 D 240 LYS GLY ASP TYR HIS ARG TYR LEU ALA GLU PHE LYS THR
SEQRES 12 D 240 GLY ALA GLU ARG LYS GLU ALA ALA GLU SER THR MET VAL
SEQRES 13 D 240 ALA TYR LYS ALA ALA GLN ASP ILE ALA LEU ALA ASP LEU
SEQRES 14 D 240 ALA PRO THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN
SEQRES 15 D 240 PHE SER VAL PHE TYR TYR GLU ILE LEU ASN SER PRO ASP
SEQRES 16 D 240 LYS ALA CYS ASN LEU ALA LYS GLN ALA PHE ASP GLU ALA
SEQRES 17 D 240 ILE SER GLU LEU ASP THR LEU GLY GLU GLU SER TYR LYS
SEQRES 18 D 240 ASP SER THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU
SEQRES 19 D 240 THR LEU TRP THR SER ASP
SEQRES 1 E 9 LEU GLN ARG VAL LEU SEP ALA PRO PHE
SEQRES 1 F 9 LEU GLN ARG VAL LEU SEP ALA PRO PHE
SEQRES 1 G 170 GLY PRO GLY HIS MET ARG ASP ARG ASP PRO LEU VAL VAL
SEQRES 2 G 170 GLY ARG VAL VAL GLY ASP VAL LEU ASP ALA PHE VAL ARG
SEQRES 3 G 170 SER THR ASN LEU LYS VAL THR TYR GLY SER LYS THR VAL
SEQRES 4 G 170 SER ASN GLY LEU GLU LEU LYS PRO SER MET VAL THR HIS
SEQRES 5 G 170 GLN PRO ARG VAL GLU VAL GLY GLY ASN ASP MET ARG THR
SEQRES 6 G 170 PHE TYR THR LEU VAL MET VAL ASP PRO ASP ALA PRO SER
SEQRES 7 G 170 PRO SER ASP PRO ASN LEU ARG GLU TYR LEU HIS TRP LEU
SEQRES 8 G 170 VAL THR ASP ILE PRO GLY THR THR ALA ALA SER PHE GLY
SEQRES 9 G 170 GLN GLU VAL MET SER TYR GLU SER PRO ARG PRO THR MET
SEQRES 10 G 170 GLY ILE HIS ARG LEU VAL PHE VAL LEU PHE GLN GLN LEU
SEQRES 11 G 170 GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN ASN
SEQRES 12 G 170 PHE ASN THR LYS ASP PHE ALA GLU LEU TYR ASN LEU GLY
SEQRES 13 G 170 SER PRO VAL ALA ALA VAL TYR PHE ASN SER GLN ARG GLU
SEQRES 14 G 170 ALA
SEQRES 1 H 170 GLY PRO GLY HIS MET ARG ASP ARG ASP PRO LEU VAL VAL
SEQRES 2 H 170 GLY ARG VAL VAL GLY ASP VAL LEU ASP ALA PHE VAL ARG
SEQRES 3 H 170 SER THR ASN LEU LYS VAL THR TYR GLY SER LYS THR VAL
SEQRES 4 H 170 SER ASN GLY LEU GLU LEU LYS PRO SER MET VAL THR HIS
SEQRES 5 H 170 GLN PRO ARG VAL GLU VAL GLY GLY ASN ASP MET ARG THR
SEQRES 6 H 170 PHE TYR THR LEU VAL MET VAL ASP PRO ASP ALA PRO SER
SEQRES 7 H 170 PRO SER ASP PRO ASN LEU ARG GLU TYR LEU HIS TRP LEU
SEQRES 8 H 170 VAL THR ASP ILE PRO GLY THR THR ALA ALA SER PHE GLY
SEQRES 9 H 170 GLN GLU VAL MET SER TYR GLU SER PRO ARG PRO THR MET
SEQRES 10 H 170 GLY ILE HIS ARG LEU VAL PHE VAL LEU PHE GLN GLN LEU
SEQRES 11 H 170 GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN ASN
SEQRES 12 H 170 PHE ASN THR LYS ASP PHE ALA GLU LEU TYR ASN LEU GLY
SEQRES 13 H 170 SER PRO VAL ALA ALA VAL TYR PHE ASN SER GLN ARG GLU
SEQRES 14 H 170 ALA
SEQRES 1 I 240 GLY PRO LEU GLY SER MET SER ARG GLU GLU ASN VAL TYR
SEQRES 2 I 240 MET ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU GLU
SEQRES 3 I 240 MET VAL GLU TYR MET GLU LYS VAL ALA LYS THR VAL ASP
SEQRES 4 I 240 VAL GLU GLU LEU THR VAL GLU GLU ARG ASN LEU LEU SER
SEQRES 5 I 240 VAL ALA TYR LYS ASN VAL ILE GLY ALA ARG ARG ALA SER
SEQRES 6 I 240 TRP ARG ILE VAL SER SER ILE GLU GLN LYS GLU GLU GLY
SEQRES 7 I 240 ARG GLY ASN GLU GLU HIS VAL THR LEU ILE LYS GLU TYR
SEQRES 8 I 240 ARG GLY LYS ILE GLU ALA GLU LEU SER LYS ILE CYS ASP
SEQRES 9 I 240 GLY ILE LEU LYS LEU LEU ASP SER HIS LEU VAL PRO SER
SEQRES 10 I 240 SER THR ALA ALA GLU SER LYS VAL PHE TYR LEU LYS MET
SEQRES 11 I 240 LYS GLY ASP TYR HIS ARG TYR LEU ALA GLU PHE LYS THR
SEQRES 12 I 240 GLY ALA GLU ARG LYS GLU ALA ALA GLU SER THR MET VAL
SEQRES 13 I 240 ALA TYR LYS ALA ALA GLN ASP ILE ALA LEU ALA ASP LEU
SEQRES 14 I 240 ALA PRO THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN
SEQRES 15 I 240 PHE SER VAL PHE TYR TYR GLU ILE LEU ASN SER PRO ASP
SEQRES 16 I 240 LYS ALA CYS ASN LEU ALA LYS GLN ALA PHE ASP GLU ALA
SEQRES 17 I 240 ILE SER GLU LEU ASP THR LEU GLY GLU GLU SER TYR LYS
SEQRES 18 I 240 ASP SER THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU
SEQRES 19 I 240 THR LEU TRP THR SER ASP
SEQRES 1 J 240 GLY PRO LEU GLY SER MET SER ARG GLU GLU ASN VAL TYR
SEQRES 2 J 240 MET ALA LYS LEU ALA GLU GLN ALA GLU ARG TYR GLU GLU
SEQRES 3 J 240 MET VAL GLU TYR MET GLU LYS VAL ALA LYS THR VAL ASP
SEQRES 4 J 240 VAL GLU GLU LEU THR VAL GLU GLU ARG ASN LEU LEU SER
SEQRES 5 J 240 VAL ALA TYR LYS ASN VAL ILE GLY ALA ARG ARG ALA SER
SEQRES 6 J 240 TRP ARG ILE VAL SER SER ILE GLU GLN LYS GLU GLU GLY
SEQRES 7 J 240 ARG GLY ASN GLU GLU HIS VAL THR LEU ILE LYS GLU TYR
SEQRES 8 J 240 ARG GLY LYS ILE GLU ALA GLU LEU SER LYS ILE CYS ASP
SEQRES 9 J 240 GLY ILE LEU LYS LEU LEU ASP SER HIS LEU VAL PRO SER
SEQRES 10 J 240 SER THR ALA ALA GLU SER LYS VAL PHE TYR LEU LYS MET
SEQRES 11 J 240 LYS GLY ASP TYR HIS ARG TYR LEU ALA GLU PHE LYS THR
SEQRES 12 J 240 GLY ALA GLU ARG LYS GLU ALA ALA GLU SER THR MET VAL
SEQRES 13 J 240 ALA TYR LYS ALA ALA GLN ASP ILE ALA LEU ALA ASP LEU
SEQRES 14 J 240 ALA PRO THR HIS PRO ILE ARG LEU GLY LEU ALA LEU ASN
SEQRES 15 J 240 PHE SER VAL PHE TYR TYR GLU ILE LEU ASN SER PRO ASP
SEQRES 16 J 240 LYS ALA CYS ASN LEU ALA LYS GLN ALA PHE ASP GLU ALA
SEQRES 17 J 240 ILE SER GLU LEU ASP THR LEU GLY GLU GLU SER TYR LYS
SEQRES 18 J 240 ASP SER THR LEU ILE MET GLN LEU LEU ARG ASP ASN LEU
SEQRES 19 J 240 THR LEU TRP THR SER ASP
SEQRES 1 K 9 LEU GLN ARG VAL LEU SEP ALA PRO PHE
SEQRES 1 L 9 LEU GLN ARG VAL LEU SEP ALA PRO PHE
MODRES 3AXY SEP E 192 SER PHOSPHOSERINE
MODRES 3AXY SEP F 192 SER PHOSPHOSERINE
MODRES 3AXY SEP K 192 SER PHOSPHOSERINE
MODRES 3AXY SEP L 192 SER PHOSPHOSERINE
HET SEP E 192 10
HET SEP F 192 10
HET SEP K 192 10
HET SEP L 192 10
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 5 SEP 4(C3 H8 N O6 P)
FORMUL 13 HOH *777(H2 O)
HELIX 1 1 ASP A 9 GLY A 14 1 6
HELIX 2 2 ARG A 15 VAL A 20 1 6
HELIX 3 3 LYS A 46 VAL A 50 5 5
HELIX 4 4 ALA A 100 GLY A 104 5 5
HELIX 5 5 ASN A 145 TYR A 153 1 9
HELIX 6 6 ASP B 9 GLY B 14 1 6
HELIX 7 7 ARG B 15 VAL B 20 1 6
HELIX 8 8 LYS B 46 THR B 51 5 6
HELIX 9 9 ALA B 100 GLY B 104 5 5
HELIX 10 10 ASN B 145 TYR B 153 1 9
HELIX 11 11 SER C 2 ALA C 16 1 15
HELIX 12 12 ARG C 18 VAL C 33 1 16
HELIX 13 13 THR C 39 GLY C 75 1 37
HELIX 14 14 ASN C 76 HIS C 108 1 33
HELIX 15 15 HIS C 108 SER C 113 1 6
HELIX 16 16 ALA C 115 LYS C 137 1 23
HELIX 17 17 THR C 138 LEU C 164 1 27
HELIX 18 18 HIS C 168 ILE C 185 1 18
HELIX 19 19 SER C 188 SER C 205 1 18
HELIX 20 20 GLU C 206 LEU C 210 5 5
HELIX 21 21 GLY C 211 TRP C 232 1 22
HELIX 22 22 SER D 2 GLU D 17 1 16
HELIX 23 23 ARG D 18 LYS D 31 1 14
HELIX 24 24 THR D 39 GLY D 73 1 35
HELIX 25 25 ASN D 76 HIS D 108 1 33
HELIX 26 26 ALA D 115 GLU D 135 1 21
HELIX 27 27 THR D 138 LEU D 164 1 27
HELIX 28 28 HIS D 168 ILE D 185 1 18
HELIX 29 29 SER D 188 LEU D 207 1 20
HELIX 30 30 ASP D 208 LEU D 210 5 3
HELIX 31 31 GLY D 211 THR D 233 1 23
HELIX 32 32 ASP G 9 GLY G 14 1 6
HELIX 33 33 ARG G 15 VAL G 20 1 6
HELIX 34 34 LYS G 46 VAL G 50 5 5
HELIX 35 35 ALA G 100 GLY G 104 5 5
HELIX 36 36 ASN G 145 TYR G 153 1 9
HELIX 37 37 ASP H 9 GLY H 14 1 6
HELIX 38 38 ARG H 15 VAL H 20 1 6
HELIX 39 39 LYS H 46 THR H 51 5 6
HELIX 40 40 ALA H 100 GLY H 104 5 5
HELIX 41 41 ASN H 145 TYR H 153 1 9
HELIX 42 42 SER I 2 GLU I 17 1 16
HELIX 43 43 ARG I 18 LYS I 31 1 14
HELIX 44 44 THR I 39 ARG I 74 1 36
HELIX 45 45 ASN I 76 HIS I 108 1 33
HELIX 46 46 HIS I 108 SER I 113 1 6
HELIX 47 47 ALA I 115 LYS I 137 1 23
HELIX 48 48 THR I 138 LEU I 164 1 27
HELIX 49 49 HIS I 168 ILE I 185 1 18
HELIX 50 50 SER I 188 LEU I 207 1 20
HELIX 51 51 ASP I 208 LEU I 210 5 3
HELIX 52 52 GLY I 211 THR I 233 1 23
HELIX 53 53 ARG J 3 ALA J 16 1 14
HELIX 54 54 ARG J 18 ASP J 34 1 17
HELIX 55 55 THR J 39 GLY J 73 1 35
HELIX 56 56 ASN J 76 HIS J 108 1 33
HELIX 57 57 HIS J 108 SER J 113 1 6
HELIX 58 58 ALA J 115 GLU J 135 1 21
HELIX 59 59 THR J 138 LEU J 164 1 27
HELIX 60 60 HIS J 168 ILE J 185 1 18
HELIX 61 61 SER J 188 LEU J 207 1 20
HELIX 62 62 ASP J 208 LEU J 210 5 3
HELIX 63 63 GLY J 211 THR J 233 1 23
SHEET 1 A 3 LYS A 37 THR A 38 0
SHEET 2 A 3 LEU A 30 TYR A 34 -1 N TYR A 34 O LYS A 37
SHEET 3 A 3 ARG A 55 VAL A 58 -1 O ARG A 55 N THR A 33
SHEET 1 B 6 LEU A 43 GLU A 44 0
SHEET 2 B 6 ALA A 160 SER A 166 1 O ASN A 165 N LEU A 43
SHEET 3 B 6 HIS A 120 GLN A 128 -1 N PHE A 124 O VAL A 162
SHEET 4 B 6 PHE A 66 ASP A 73 -1 N VAL A 70 O VAL A 125
SHEET 5 B 6 TYR A 87 PRO A 96 -1 O VAL A 92 N LEU A 69
SHEET 6 B 6 GLN A 105 MET A 108 -1 O GLN A 105 N THR A 93
SHEET 1 C 3 LYS B 37 THR B 38 0
SHEET 2 C 3 LEU B 30 TYR B 34 -1 N TYR B 34 O LYS B 37
SHEET 3 C 3 ARG B 55 VAL B 58 -1 O ARG B 55 N THR B 33
SHEET 1 D 6 LEU B 43 GLU B 44 0
SHEET 2 D 6 ALA B 160 SER B 166 1 O ASN B 165 N LEU B 43
SHEET 3 D 6 HIS B 120 GLN B 128 -1 N PHE B 124 O VAL B 162
SHEET 4 D 6 PHE B 66 ASP B 73 -1 N VAL B 70 O VAL B 125
SHEET 5 D 6 TYR B 87 PRO B 96 -1 O VAL B 92 N LEU B 69
SHEET 6 D 6 GLN B 105 MET B 108 -1 O GLN B 105 N THR B 93
SHEET 1 E 3 LYS G 37 THR G 38 0
SHEET 2 E 3 LEU G 30 TYR G 34 -1 N TYR G 34 O LYS G 37
SHEET 3 E 3 ARG G 55 VAL G 58 -1 O ARG G 55 N THR G 33
SHEET 1 F 5 GLN G 105 MET G 108 0
SHEET 2 F 5 TYR G 87 PRO G 96 -1 N THR G 93 O GLN G 105
SHEET 3 F 5 PHE G 66 ASP G 73 -1 N LEU G 69 O VAL G 92
SHEET 4 F 5 HIS G 120 GLN G 128 -1 O VAL G 125 N VAL G 70
SHEET 5 F 5 ALA G 160 SER G 166 -1 O VAL G 162 N PHE G 124
SHEET 1 G 3 LYS H 37 THR H 38 0
SHEET 2 G 3 LEU H 30 TYR H 34 -1 N TYR H 34 O LYS H 37
SHEET 3 G 3 ARG H 55 VAL H 58 -1 O ARG H 55 N THR H 33
SHEET 1 H 6 LEU H 43 GLU H 44 0
SHEET 2 H 6 ALA H 160 SER H 166 1 O ASN H 165 N LEU H 43
SHEET 3 H 6 HIS H 120 GLN H 128 -1 N PHE H 124 O VAL H 162
SHEET 4 H 6 PHE H 66 ASP H 73 -1 N THR H 68 O PHE H 127
SHEET 5 H 6 TYR H 87 PRO H 96 -1 O VAL H 92 N LEU H 69
SHEET 6 H 6 GLN H 105 MET H 108 -1 O GLN H 105 N THR H 93
LINK C LEU E 191 N SEP E 192 1555 1555 1.34
LINK C SEP E 192 N ALA E 193 1555 1555 1.33
LINK C LEU F 191 N SEP F 192 1555 1555 1.33
LINK C SEP F 192 N ALA F 193 1555 1555 1.33
LINK C LEU K 191 N SEP K 192 1555 1555 1.34
LINK C SEP K 192 N ALA K 193 1555 1555 1.33
LINK C LEU L 191 N SEP L 192 1555 1555 1.33
LINK C SEP L 192 N ALA L 193 1555 1555 1.33
CISPEP 1 ALA A 76 PRO A 77 0 -3.75
CISPEP 2 ARG A 85 GLU A 86 0 -15.35
CISPEP 3 ALA B 76 PRO B 77 0 2.73
CISPEP 4 ARG B 85 GLU B 86 0 -12.87
CISPEP 5 ALA G 76 PRO G 77 0 -4.02
CISPEP 6 ARG G 85 GLU G 86 0 -15.45
CISPEP 7 ALA H 76 PRO H 77 0 7.31
CISPEP 8 ARG H 85 GLU H 86 0 -16.02
CRYST1 76.735 96.647 99.510 68.23 87.90 77.94 P 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 0.013032 -0.002784 0.000600 0.00000
SCALE2 0.000000 0.010580 -0.004236 0.00000
SCALE3 0.000000 0.000000 0.010832 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
