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HEADER HYDROLASE 06-FEB-22 7TVW
TITLE CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DLK2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AT3G24420,HYDROLASE-LIKE PROTEIN,UNCHARACTERIZED PROTEIN
COMPND 5 AT3G24420, D14-LIKE2;
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: AT3G24420;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T3
KEYWDS SESQUITERPENE LACTONE PERCEPTION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BURGER,J.CHORY
REVDAT 1 28-SEP-22 7TVW 0
JRNL AUTH M.BURGER,K.HONDA,Y.KONDOH,S.HONG,N.WATANABE,H.OSADA,J.CHORY
JRNL TITL CRYSTAL STRUCTURE OF ARABIDOPSIS DWARF14-LIKE2 (DLK2)
JRNL TITL 2 REVEALS A DISTINCT SUBSTRATE BINDING POCKET ARCHITECTURE
JRNL REF PLANT DIRECT V. 6 2022
JRNL REFN ESSN 2475-4455
JRNL DOI 10.1002/PLD3.446
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 43368
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2180
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 42.2950 - 3.7286 1.00 2735 148 0.1321 0.1366
REMARK 3 2 3.7286 - 2.9598 0.99 2599 152 0.1502 0.2012
REMARK 3 3 2.9598 - 2.5857 1.00 2603 131 0.1694 0.1985
REMARK 3 4 2.5857 - 2.3493 0.99 2565 142 0.1635 0.1695
REMARK 3 5 2.3493 - 2.1809 0.99 2576 140 0.1564 0.1820
REMARK 3 6 2.1809 - 2.0523 1.00 2582 128 0.1613 0.1884
REMARK 3 7 2.0523 - 1.9496 1.00 2560 153 0.1631 0.1856
REMARK 3 8 1.9496 - 1.8647 1.00 2557 137 0.1723 0.2069
REMARK 3 9 1.8647 - 1.7929 1.00 2568 136 0.1776 0.1994
REMARK 3 10 1.7929 - 1.7310 1.00 2515 147 0.1747 0.2230
REMARK 3 11 1.7310 - 1.6769 1.00 2589 132 0.1796 0.2342
REMARK 3 12 1.6769 - 1.6290 1.00 2542 131 0.1868 0.2274
REMARK 3 13 1.6290 - 1.5861 1.00 2576 113 0.2060 0.2430
REMARK 3 14 1.5861 - 1.5474 1.00 2562 131 0.2283 0.2645
REMARK 3 15 1.5474 - 1.5122 1.00 2521 146 0.2436 0.2737
REMARK 3 16 1.5122 - 1.4800 0.99 2538 113 0.2801 0.2870
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.88
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 2141
REMARK 3 ANGLE : 1.104 2907
REMARK 3 CHIRALITY : 0.045 332
REMARK 3 PLANARITY : 0.005 371
REMARK 3 DIHEDRAL : 13.232 797
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 7TVW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1000263005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-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 : 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 : NULL
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 : 43371
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 42.295
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.07077
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.72960
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 4IH1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 1.9 M AMMONIUM SULFATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.44000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.44000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 39.78000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.29500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.78000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.29500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.44000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.78000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.29500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 38.44000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.78000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.29500
REMARK 290 SMTRY3 8 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 -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 VAL A 3
REMARK 465 ASN A 4
REMARK 465 GLN A 5
REMARK 465 LYS A 6
REMARK 465 ILE A 7
REMARK 465 SER A 8
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 VAL A 213 O HOH A 301 2.04
REMARK 500 ND2 ASN A 222 O HOH A 302 2.06
REMARK 500 O HOH A 522 O HOH A 532 2.12
REMARK 500 O HOH A 317 O HOH A 589 2.16
REMARK 500 O HOH A 601 O HOH A 605 2.16
REMARK 500 OG SER A 242 O HOH A 303 2.17
REMARK 500 O PRO A 220 O HOH A 304 2.17
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 553 O HOH A 574 7444 2.18
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 SER A 102 -118.71 58.50
REMARK 500 ARG A 130 134.34 -170.94
REMARK 500 SER A 259 51.89 -141.63
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 617 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 618 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A 619 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 620 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 621 DISTANCE = 7.71 ANGSTROMS
DBREF 7TVW A 1 273 UNP Q9LK01 Q9LK01_ARATH 1 273
SEQADV 7TVW GLY A -1 UNP Q9LK01 EXPRESSION TAG
SEQADV 7TVW PRO A 0 UNP Q9LK01 EXPRESSION TAG
SEQRES 1 A 275 GLY PRO MET VAL VAL ASN GLN LYS ILE SER GLY LEU ALA
SEQRES 2 A 275 SER ALA MET ASN ALA LYS ILE ILE GLY SER GLY GLU ARG
SEQRES 3 A 275 SER MET VAL LEU ALA HIS GLY PHE GLY GLY ASP GLN SER
SEQRES 4 A 275 VAL TRP ASP LYS ILE ILE PRO VAL LEU SER GLN SER PHE
SEQRES 5 A 275 LYS VAL LEU VAL PHE ASP TRP LEU PHE SER GLY ALA ILE
SEQRES 6 A 275 LYS ASP GLN THR LEU TYR ASP PRO SER LYS TYR ASN SER
SEQRES 7 A 275 LEU ASP VAL PHE SER ASP ASP LEU ILE ALA LEU MET GLU
SEQRES 8 A 275 GLU LEU LYS PHE GLY PRO VAL VAL PHE VAL GLY HIS SER
SEQRES 9 A 275 MET SER GLY VAL ILE GLY CYS ALA ALA SER ILE LYS ARG
SEQRES 10 A 275 PRO ASP LEU PHE THR ASN LEU LEU LEU ILE ALA ALA SER
SEQRES 11 A 275 PRO ARG TYR ILE ASN SER GLU ASP TYR LYS GLY GLY PHE
SEQRES 12 A 275 GLU SER LYS ASP ILE ASP THR ILE ILE THR SER ILE GLY
SEQRES 13 A 275 SER ASN TYR GLU ALA TRP ALA VAL ASP PHE SER SER PHE
SEQRES 14 A 275 VAL VAL ASP SER ARG ASP SER LEU SER VAL GLN ARG PHE
SEQRES 15 A 275 GLU LYS SER LEU LYS LYS MET LYS PRO GLU THR ALA LEU
SEQRES 16 A 275 ALA LEU ALA LYS ILE VAL PHE GLY SER ASP GLU ARG GLU
SEQRES 17 A 275 ILE LEU GLY GLN VAL SER VAL PRO CYS HIS VAL ILE GLN
SEQRES 18 A 275 PRO GLY ASN ASP VAL VAL VAL PRO VAL SER VAL ALA TYR
SEQRES 19 A 275 PHE MET GLN GLU LYS ILE LYS GLY LYS SER THR VAL GLU
SEQRES 20 A 275 ILE ILE GLU ASP ALA ILE GLY HIS PHE PRO GLN MET THR
SEQRES 21 A 275 SER HIS LEU GLU LEU LEU GLY VAL MET ARG ARG LEU LEU
SEQRES 22 A 275 GLU PHE
FORMUL 2 HOH *321(H2 O)
HELIX 1 AA1 GLY A 9 MET A 14 1 6
HELIX 2 AA2 ASP A 35 ASP A 40 5 6
HELIX 3 AA3 ILE A 42 PHE A 50 1 9
HELIX 4 AA4 LEU A 77 LEU A 91 1 15
HELIX 5 AA5 SER A 102 ARG A 115 1 14
HELIX 6 AA6 GLU A 142 GLY A 154 1 13
HELIX 7 AA7 ASN A 156 VAL A 169 1 14
HELIX 8 AA8 ASP A 173 MET A 187 1 15
HELIX 9 AA9 LYS A 188 GLY A 201 1 14
HELIX 10 AB1 GLU A 204 VAL A 211 5 8
HELIX 11 AB2 PRO A 227 ILE A 238 1 12
HELIX 12 AB3 PHE A 254 SER A 259 1 6
HELIX 13 AB4 SER A 259 GLU A 272 1 14
SHEET 1 AA1 7 LYS A 17 GLY A 20 0
SHEET 2 AA1 7 LYS A 51 VAL A 54 -1 O VAL A 52 N ILE A 19
SHEET 3 AA1 7 SER A 25 ALA A 29 1 N MET A 26 O LEU A 53
SHEET 4 AA1 7 VAL A 96 HIS A 101 1 O VAL A 99 N VAL A 27
SHEET 5 AA1 7 PHE A 119 ILE A 125 1 O LEU A 123 N PHE A 98
SHEET 6 AA1 7 CYS A 215 ASN A 222 1 O ILE A 218 N LEU A 124
SHEET 7 AA1 7 SER A 242 ILE A 251 1 O GLU A 245 N VAL A 217
CISPEP 1 GLY A 94 PRO A 95 0 -0.31
CRYST1 79.560 84.590 76.880 90.00 90.00 90.00 C 2 2 21 8
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 0.012569 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011822 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013007 0.00000
TER 2091 PHE A 273
MASTER 307 0 0 13 7 0 0 6 2370 1 0 22
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