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HEADER HYDROLASE 11-SEP-17 6AZC
TITLE CRYSTAL STRUCTURE OF PHYSCOMITRELLA PATENS KAI2-LIKE E S166A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PP-KAI2-LIKE E;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.-.-.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHYSCOMITRELLA PATENS SUBSP. PATENS;
SOURCE 3 ORGANISM_COMMON: MOSS;
SOURCE 4 ORGANISM_TAXID: 3218;
SOURCE 5 GENE: PHYPADRAFT_215526;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T3
KEYWDS ALPHA/BETA HYDROLASE, STRIGOLACTONE BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BURGER,H.J.LEE,J.CHORY
REVDAT 1 06-FEB-19 6AZC 0
JRNL AUTH M.BURGER,K.MASHIGUCHI,H.J.LEE,M.NAKANO,K.TAKEMOTO,Y.SETO,
JRNL AUTH 2 S.YAMAGUCHI,J.CHORY
JRNL TITL STRUCTURAL BASIS OF KARRIKIN AND NON-NATURAL STRIGOLACTONE
JRNL TITL 2 PERCEPTION IN PHYSCOMITRELLA PATENS.
JRNL REF CELL REP V. 26 855 2019
JRNL REFN ESSN 2211-1247
JRNL PMID 30673608
JRNL DOI 10.1016/J.CELREP.2019.01.003
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 5.139
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 34314
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.263
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 1767
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 21.1134 - 4.5649 0.94 2768 149 0.2078 0.2462
REMARK 3 2 4.5649 - 3.6293 0.95 2751 145 0.1889 0.2450
REMARK 3 3 3.6293 - 3.1723 0.94 2736 151 0.2251 0.2483
REMARK 3 4 3.1723 - 2.8830 0.94 2715 150 0.2445 0.3091
REMARK 3 5 2.8830 - 2.6768 0.94 2728 140 0.2811 0.2622
REMARK 3 6 2.6768 - 2.5192 0.94 2715 150 0.2867 0.3278
REMARK 3 7 2.5192 - 2.3933 0.94 2714 138 0.2959 0.3400
REMARK 3 8 2.3933 - 2.2892 0.94 2682 140 0.3043 0.3592
REMARK 3 9 2.2892 - 2.2012 0.94 2715 133 0.3147 0.3532
REMARK 3 10 2.2012 - 2.1253 0.94 2706 145 0.3123 0.3617
REMARK 3 11 2.1253 - 2.0589 0.93 2697 141 0.3334 0.3599
REMARK 3 12 2.0589 - 2.0001 0.93 2639 138 0.3522 0.3800
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.791
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.36
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 : 0.003 4184
REMARK 3 ANGLE : 0.591 5697
REMARK 3 CHIRALITY : 0.047 655
REMARK 3 PLANARITY : 0.004 735
REMARK 3 DIHEDRAL : 2.201 2932
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'A' AND (RESID 6 THROUGH 100 OR
REMARK 3 RESID 102 THROUGH 268))
REMARK 3 SELECTION : (CHAIN 'B' AND (RESID 6 THROUGH 100 OR
REMARK 3 RESID 102 THROUGH 268))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6AZC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000229842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
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 : 35204
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07743
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.13200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 8.120
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 ENTRY 6AZB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5, 30% PEG8000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 60.91050
REMARK 290 SMTRY3 2 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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 3
REMARK 465 PRO A 4
REMARK 465 SER A 5
REMARK 465 SER A 269
REMARK 465 LEU A 270
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 PRO B 4
REMARK 465 SER B 5
REMARK 465 SER B 269
REMARK 465 LEU B 270
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 O GLY A 27 O HOH A 301 1.81
REMARK 500 O HOH A 333 O HOH B 371 1.91
REMARK 500 O LEU B 214 O HOH B 301 1.97
REMARK 500 NH1 ARG A 130 O HOH A 302 1.99
REMARK 500 O HOH A 303 O HOH A 333 1.99
REMARK 500 ND1 HIS A 26 O HOH A 301 2.00
REMARK 500 O ARG A 68 O HOH A 303 2.07
REMARK 500 O LYS B 116 O HOH B 302 2.07
REMARK 500 O LEU A 6 O HOH A 304 2.08
REMARK 500 O HOH A 376 O HOH A 382 2.10
REMARK 500 N SER A 190 O HOH A 305 2.11
REMARK 500 O THR B 71 O HOH B 303 2.13
REMARK 500 N GLY B 57 O HOH B 304 2.14
REMARK 500 O LEU B 6 O HOH B 305 2.15
REMARK 500 O HOH B 321 O HOH B 351 2.16
REMARK 500 OD1 ASP B 228 O HOH B 306 2.16
REMARK 500 O PHE B 66 O HOH B 307 2.16
REMARK 500 O LEU A 105 O HOH A 306 2.18
REMARK 500 O HOH A 325 O HOH A 381 2.18
REMARK 500 OD1 ASP A 44 O HOH A 307 2.19
REMARK 500 O ASP A 186 O HOH A 305 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 348 O HOH A 355 1554 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 LEU A 7 -61.73 60.02
REMARK 500 THR A 30 -159.09 -120.56
REMARK 500 PRO A 61 51.35 -107.73
REMARK 500 PHE A 63 74.72 -112.04
REMARK 500 SER A 97 -120.93 57.47
REMARK 500 ALA A 166 -171.63 59.87
REMARK 500 LEU B 7 -60.75 60.76
REMARK 500 THR B 30 -160.47 -120.07
REMARK 500 SER B 97 -123.80 59.19
REMARK 500 ALA B 166 -177.82 59.65
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6AZC A 1 270 UNP A9ST85 A9ST85_PHYPA 1 270
DBREF 6AZC B 1 270 UNP A9ST85 A9ST85_PHYPA 1 270
SEQADV 6AZC GLY A -1 UNP A9ST85 CLONING ARTIFACT
SEQADV 6AZC PRO A 0 UNP A9ST85 CLONING ARTIFACT
SEQADV 6AZC ALA A 166 UNP A9ST85 SER 166 ENGINEERED MUTATION
SEQADV 6AZC GLY B -1 UNP A9ST85 CLONING ARTIFACT
SEQADV 6AZC PRO B 0 UNP A9ST85 CLONING ARTIFACT
SEQADV 6AZC ALA B 166 UNP A9ST85 SER 166 ENGINEERED MUTATION
SEQRES 1 A 272 GLY PRO MET GLU GLU PRO SER LEU LEU ASP ALA HIS ASN
SEQRES 2 A 272 VAL ARG VAL VAL GLY MET GLY SER GLU LEU VAL VAL LEU
SEQRES 3 A 272 GLY HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS HIS
SEQRES 4 A 272 VAL ILE PRO HIS LEU VAL ASP ASP TYR ARG VAL ILE LEU
SEQRES 5 A 272 PHE ASP ASN MET GLY ALA GLY THR THR ASP PRO GLU PHE
SEQRES 6 A 272 PHE SER PHE SER ARG TYR SER THR LEU HIS GLY TYR ALA
SEQRES 7 A 272 ASP ASP LEU LEU SER ILE LEU GLU GLU LEU GLU VAL GLU
SEQRES 8 A 272 SER CYS ILE TYR VAL GLY HIS SER VAL ALA GLY MET VAL
SEQRES 9 A 272 GLY CYS LEU ALA SER LEU GLU ARG PRO GLU ILE PHE THR
SEQRES 10 A 272 LYS ILE ILE THR LEU SER ALA SER PRO ARG TYR LEU ASN
SEQRES 11 A 272 ASP ARG ASP TYR PHE GLY GLY PHE GLU GLN ASP ASP LEU
SEQRES 12 A 272 ASN GLN LEU PHE GLU ALA MET GLN SER ASN PHE LYS ALA
SEQRES 13 A 272 TRP VAL SER GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP
SEQRES 14 A 272 ILE ASP SER MET ALA VAL GLN GLU PHE GLY ARG THR LEU
SEQRES 15 A 272 PHE ASN ILE ARG PRO ASP ILE ALA PHE SER VAL ALA LYS
SEQRES 16 A 272 THR ILE PHE GLN SER ASP LEU ARG ILE MET LEU PRO LYS
SEQRES 17 A 272 VAL THR VAL PRO CYS HIS ILE LEU GLN SER SER LYS ASP
SEQRES 18 A 272 LEU ALA VAL PRO LEU VAL VAL ALA ASP TYR LEU HIS HIS
SEQRES 19 A 272 ALA LEU GLY GLY PRO THR ILE VAL GLU VAL LEU PRO THR
SEQRES 20 A 272 GLU GLY HIS LEU PRO GLN LEU SER SER PRO ASP ILE ILE
SEQRES 21 A 272 ILE PRO VAL LEU LYS ARG HIS LEU ALA GLY SER LEU
SEQRES 1 B 272 GLY PRO MET GLU GLU PRO SER LEU LEU ASP ALA HIS ASN
SEQRES 2 B 272 VAL ARG VAL VAL GLY MET GLY SER GLU LEU VAL VAL LEU
SEQRES 3 B 272 GLY HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS HIS
SEQRES 4 B 272 VAL ILE PRO HIS LEU VAL ASP ASP TYR ARG VAL ILE LEU
SEQRES 5 B 272 PHE ASP ASN MET GLY ALA GLY THR THR ASP PRO GLU PHE
SEQRES 6 B 272 PHE SER PHE SER ARG TYR SER THR LEU HIS GLY TYR ALA
SEQRES 7 B 272 ASP ASP LEU LEU SER ILE LEU GLU GLU LEU GLU VAL GLU
SEQRES 8 B 272 SER CYS ILE TYR VAL GLY HIS SER VAL ALA GLY MET VAL
SEQRES 9 B 272 GLY CYS LEU ALA SER LEU GLU ARG PRO GLU ILE PHE THR
SEQRES 10 B 272 LYS ILE ILE THR LEU SER ALA SER PRO ARG TYR LEU ASN
SEQRES 11 B 272 ASP ARG ASP TYR PHE GLY GLY PHE GLU GLN ASP ASP LEU
SEQRES 12 B 272 ASN GLN LEU PHE GLU ALA MET GLN SER ASN PHE LYS ALA
SEQRES 13 B 272 TRP VAL SER GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP
SEQRES 14 B 272 ILE ASP SER MET ALA VAL GLN GLU PHE GLY ARG THR LEU
SEQRES 15 B 272 PHE ASN ILE ARG PRO ASP ILE ALA PHE SER VAL ALA LYS
SEQRES 16 B 272 THR ILE PHE GLN SER ASP LEU ARG ILE MET LEU PRO LYS
SEQRES 17 B 272 VAL THR VAL PRO CYS HIS ILE LEU GLN SER SER LYS ASP
SEQRES 18 B 272 LEU ALA VAL PRO LEU VAL VAL ALA ASP TYR LEU HIS HIS
SEQRES 19 B 272 ALA LEU GLY GLY PRO THR ILE VAL GLU VAL LEU PRO THR
SEQRES 20 B 272 GLU GLY HIS LEU PRO GLN LEU SER SER PRO ASP ILE ILE
SEQRES 21 B 272 ILE PRO VAL LEU LYS ARG HIS LEU ALA GLY SER LEU
FORMUL 3 HOH *160(H2 O)
HELIX 1 AA1 ASP A 31 LYS A 36 5 6
HELIX 2 AA2 VAL A 38 LEU A 42 5 5
HELIX 3 AA3 LEU A 72 LEU A 86 1 15
HELIX 4 AA4 SER A 97 ARG A 110 1 14
HELIX 5 AA5 GLU A 137 ASN A 151 1 15
HELIX 6 AA6 ASN A 151 GLY A 165 1 15
HELIX 7 AA7 SER A 170 ASN A 182 1 13
HELIX 8 AA8 ARG A 184 GLN A 197 1 14
HELIX 9 AA9 MET A 203 VAL A 207 5 5
HELIX 10 AB1 PRO A 223 LEU A 234 1 12
HELIX 11 AB2 LEU A 249 SER A 254 1 6
HELIX 12 AB3 SER A 254 GLY A 268 1 15
HELIX 13 AB4 ASP B 31 LYS B 36 5 6
HELIX 14 AB5 VAL B 38 LEU B 42 5 5
HELIX 15 AB6 LEU B 72 LEU B 86 1 15
HELIX 16 AB7 SER B 97 ARG B 110 1 14
HELIX 17 AB8 GLU B 137 ASN B 151 1 15
HELIX 18 AB9 ASN B 151 GLY B 165 1 15
HELIX 19 AC1 SER B 170 ASN B 182 1 13
HELIX 20 AC2 ARG B 184 GLN B 197 1 14
HELIX 21 AC3 MET B 203 VAL B 207 5 5
HELIX 22 AC4 LEU B 224 LEU B 234 1 11
HELIX 23 AC5 LEU B 249 SER B 254 1 6
HELIX 24 AC6 SER B 254 GLY B 268 1 15
SHEET 1 AA1 7 ARG A 13 GLY A 16 0
SHEET 2 AA1 7 TYR A 46 LEU A 50 -1 O VAL A 48 N VAL A 15
SHEET 3 AA1 7 GLU A 20 GLY A 25 1 N GLU A 20 O ARG A 47
SHEET 4 AA1 7 CYS A 91 HIS A 96 1 O VAL A 94 N VAL A 23
SHEET 5 AA1 7 PHE A 114 LEU A 120 1 O ILE A 118 N GLY A 95
SHEET 6 AA1 7 CYS A 211 LYS A 218 1 O LEU A 214 N THR A 119
SHEET 7 AA1 7 THR A 238 GLU A 246 1 O ILE A 239 N ILE A 213
SHEET 1 AA2 7 ARG B 13 GLY B 16 0
SHEET 2 AA2 7 TYR B 46 LEU B 50 -1 O LEU B 50 N ARG B 13
SHEET 3 AA2 7 GLU B 20 GLY B 25 1 N GLU B 20 O ARG B 47
SHEET 4 AA2 7 CYS B 91 HIS B 96 1 O ILE B 92 N VAL B 23
SHEET 5 AA2 7 PHE B 114 LEU B 120 1 O ILE B 118 N GLY B 95
SHEET 6 AA2 7 CYS B 211 LYS B 218 1 O LEU B 214 N THR B 119
SHEET 7 AA2 7 THR B 238 GLU B 246 1 O LEU B 243 N GLN B 215
CRYST1 45.932 121.821 46.909 90.00 91.54 90.00 P 1 21 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 0.021771 0.000000 0.000585 0.00000
SCALE2 0.000000 0.008209 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021326 0.00000
TER 2040 GLY A 268
TER 4085 GLY B 268
MASTER 306 0 0 24 14 0 0 6 4238 2 0 42
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