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HEADER HYDROLASE 25-AUG-25 9WGQ
TITLE CRYSTAL STRUCTURE OF OCKAI2D6 FROM OROBANCHE CUMANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OCKAI2D6 PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OROBANCHE CERNUA VAR. CUMANA;
SOURCE 3 ORGANISM_TAXID: 78542;
SOURCE 4 GENE: KAI2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS OCKAI2D6, DEHYDROCOSTUS LACTONE, ENZYME, OROBANCHE CUMANA, SEED
KEYWDS 2 GERMINATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.F.S.HAMEED,S.T.AROLD
REVDAT 1 20-MAY-26 9WGQ 0
JRNL AUTH U.F.SHAHUL HAMEED,M.JAMIL,R.ZARBAN,Y.SAITO,K.ALASHOOR,
JRNL AUTH 2 A.BALAKRISHNA,T.ASAMI,S.T.AROLD,S.AL-BABILI
JRNL TITL OROBANCHE CUMANA KAI2D2 MEDIATES PERCEPTION OF DEHYDROCOSTUS
JRNL TITL 2 LACTONE AND STRIGOLACTONES AND IS INHIBITED BY TRIAZOLE
JRNL TITL 3 UREAS.
JRNL REF PLANT COMMUN. 01889 2026
JRNL REFN ISSN 2590-3462
JRNL PMID 42104616
JRNL DOI 10.1016/J.XPLC.2026.101889
REMARK 2
REMARK 2 RESOLUTION. 1.85 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 49018
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 2346
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 4.7400 - 3.7700 1.00 2834 129 0.1508 0.1981
REMARK 3 2 3.7600 - 3.2900 1.00 2807 147 0.1687 0.1851
REMARK 3 3 3.2900 - 2.9900 1.00 2753 170 0.1974 0.2568
REMARK 3 4 2.9900 - 2.7800 1.00 2781 117 0.2112 0.2395
REMARK 3 5 2.7800 - 2.6100 1.00 2716 163 0.2178 0.2324
REMARK 3 6 2.6100 - 2.4800 1.00 2729 143 0.2084 0.2428
REMARK 3 7 2.4800 - 2.3700 1.00 2767 139 0.2114 0.2747
REMARK 3 8 2.3700 - 2.2800 1.00 2748 105 0.1943 0.2214
REMARK 3 9 2.2800 - 2.2000 1.00 2730 138 0.2041 0.2391
REMARK 3 10 2.2000 - 2.1300 1.00 2717 137 0.2376 0.2659
REMARK 3 11 2.1300 - 2.0700 1.00 2733 111 0.2243 0.2343
REMARK 3 12 2.0700 - 2.0200 1.00 2737 130 0.2139 0.2392
REMARK 3 13 2.0200 - 1.9700 1.00 2693 151 0.2363 0.2887
REMARK 3 14 1.9700 - 1.9200 1.00 2697 149 0.2861 0.3498
REMARK 3 15 1.9200 - 1.8800 1.00 2713 145 0.3318 0.3585
REMARK 3 16 1.8800 - 1.8500 0.95 2538 123 0.4082 0.4281
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 4217
REMARK 3 ANGLE : 0.937 5742
REMARK 3 CHIRALITY : 0.065 663
REMARK 3 PLANARITY : 0.009 748
REMARK 3 DIHEDRAL : 5.572 580
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 5:273)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9489 45.0860 70.8539
REMARK 3 T TENSOR
REMARK 3 T11: 0.2374 T22: 0.2371
REMARK 3 T33: 0.2331 T12: -0.0012
REMARK 3 T13: 0.0156 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.1177 L22: 1.1730
REMARK 3 L33: 0.6097 L12: 0.0845
REMARK 3 L13: 0.0398 L23: -0.1335
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: -0.0351 S13: 0.0892
REMARK 3 S21: 0.0664 S22: 0.0023 S23: 0.0163
REMARK 3 S31: 0.0146 S32: -0.0175 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESSEQ 8:274)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1995 82.2817 79.9478
REMARK 3 T TENSOR
REMARK 3 T11: 0.3135 T22: 0.3490
REMARK 3 T33: 0.2732 T12: -0.0144
REMARK 3 T13: -0.0122 T23: -0.0663
REMARK 3 L TENSOR
REMARK 3 L11: 1.7405 L22: 1.8679
REMARK 3 L33: 0.5845 L12: 0.0655
REMARK 3 L13: 0.0209 L23: 0.1538
REMARK 3 S TENSOR
REMARK 3 S11: -0.0621 S12: 0.2609 S13: -0.0580
REMARK 3 S21: -0.2478 S22: 0.0356 S23: 0.0107
REMARK 3 S31: -0.0430 S32: 0.0491 S33: 0.0003
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 9WGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-AUG-25.
REMARK 100 THE DEPOSITION ID IS D_1300063001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-18
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49018
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 38.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.840
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1 M HEPES PH 7.5, 25% W/V POLYETHYLENE GLYCOL 3,350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 18.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.17000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.17000
REMARK 290 SMTRY3 4 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 2
REMARK 465 LEU A 3
REMARK 465 GLY A 4
REMARK 465 ASP A 275
REMARK 465 ALA A 276
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 LEU B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 MET B 6
REMARK 465 SER B 7
REMARK 465 ASP B 275
REMARK 465 ALA B 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 O HOH B 309 O HOH B 353 2.05
REMARK 500 O HOH B 301 O HOH B 369 2.15
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 34 -156.75 -102.10
REMARK 500 SER A 101 -121.48 52.74
REMARK 500 ILE A 168 -61.87 -102.77
REMARK 500 SER B 21 -102.36 -130.53
REMARK 500 THR B 34 -166.11 -114.46
REMARK 500 SER B 101 -125.98 58.35
REMARK 500 GLU B 134 -87.73 -12.33
REMARK 500 LEU B 149 28.47 -79.75
REMARK 500 SER B 248 47.38 -86.72
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 ARG A 129 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 9WGO RELATED DB: PDB
DBREF1 9WGQ A 6 276 UNP A0A9E9EMW1_OROCE
DBREF2 9WGQ A A0A9E9EMW1 1 271
DBREF1 9WGQ B 6 276 UNP A0A9E9EMW1_OROCE
DBREF2 9WGQ B A0A9E9EMW1 1 271
SEQADV 9WGQ GLY A 1 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ PRO A 2 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ LEU A 3 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ GLY A 4 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ SER A 5 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ GLY B 1 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ PRO B 2 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ LEU B 3 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ GLY B 4 UNP A0A9E9EMW EXPRESSION TAG
SEQADV 9WGQ SER B 5 UNP A0A9E9EMW EXPRESSION TAG
SEQRES 1 A 276 GLY PRO LEU GLY SER MET SER SER ILE VAL GLY ALA ARG
SEQRES 2 A 276 HIS ASN VAL ARG VAL LEU GLY SER GLY PRO THR THR VAL
SEQRES 3 A 276 VAL LEU ALA HIS GLY PHE GLY THR ASP GLN SER VAL TRP
SEQRES 4 A 276 ARG HIS LEU VAL PRO ARG LEU VAL ASP GLN TYR ARG VAL
SEQRES 5 A 276 VAL LEU TYR ASP ASN MET GLY ALA GLY THR THR ASN PRO
SEQRES 6 A 276 ASP SER TYR ASP PHE ASP ARG TYR ALA ILE LEU ASP GLY
SEQRES 7 A 276 HIS ALA ASN ASP LEU LEU ALA ILE LEU GLU GLU PHE SER
SEQRES 8 A 276 VAL GLU LYS CYS ILE HIS VAL GLY HIS SER LEU SER ALA
SEQRES 9 A 276 MET VAL GLY ALA MET ALA SER ILE LEU ARG PRO ASP LEU
SEQRES 10 A 276 PHE HIS LYS LEU VAL MET ILE SER ALA THR PRO ARG VAL
SEQRES 11 A 276 VAL ASN THR GLU ASP TYR TYR GLY GLY LEU ASN GLN GLU
SEQRES 12 A 276 ASP LEU ASP GLN ILE LEU GLU ALA MET GLU THR ASN TYR
SEQRES 13 A 276 ASN SER MET VAL HIS GLY MET ALA THR LEU ALA ILE GLY
SEQRES 14 A 276 GLY ASP MET ASP SER GLU VAL VAL GLN GLU TYR SER ARG
SEQRES 15 A 276 THR LEU PHE ASN MET GLN PRO ASP ILE ALA LEU SER VAL
SEQRES 16 A 276 ALA ARG MET ILE CYS ALA TYR ASP MET ARG PRO LEU LEU
SEQRES 17 A 276 GLY SER VAL VAL VAL PRO CYS HIS ILE ILE HIS SER CYS
SEQRES 18 A 276 LYS ASP PRO VAL VAL PRO VAL THR ALA ALA GLU TYR ILE
SEQRES 19 A 276 HIS GLN ASN VAL GLY GLY LYS SER VAL MET GLU VAL MET
SEQRES 20 A 276 SER VAL GLU GLY HIS LEU PRO HIS PHE SER ALA PRO GLU
SEQRES 21 A 276 GLY THR ILE PRO VAL LEU LEU ARG HIS ILE ASN HIS ASP
SEQRES 22 A 276 ILE ASP ALA
SEQRES 1 B 276 GLY PRO LEU GLY SER MET SER SER ILE VAL GLY ALA ARG
SEQRES 2 B 276 HIS ASN VAL ARG VAL LEU GLY SER GLY PRO THR THR VAL
SEQRES 3 B 276 VAL LEU ALA HIS GLY PHE GLY THR ASP GLN SER VAL TRP
SEQRES 4 B 276 ARG HIS LEU VAL PRO ARG LEU VAL ASP GLN TYR ARG VAL
SEQRES 5 B 276 VAL LEU TYR ASP ASN MET GLY ALA GLY THR THR ASN PRO
SEQRES 6 B 276 ASP SER TYR ASP PHE ASP ARG TYR ALA ILE LEU ASP GLY
SEQRES 7 B 276 HIS ALA ASN ASP LEU LEU ALA ILE LEU GLU GLU PHE SER
SEQRES 8 B 276 VAL GLU LYS CYS ILE HIS VAL GLY HIS SER LEU SER ALA
SEQRES 9 B 276 MET VAL GLY ALA MET ALA SER ILE LEU ARG PRO ASP LEU
SEQRES 10 B 276 PHE HIS LYS LEU VAL MET ILE SER ALA THR PRO ARG VAL
SEQRES 11 B 276 VAL ASN THR GLU ASP TYR TYR GLY GLY LEU ASN GLN GLU
SEQRES 12 B 276 ASP LEU ASP GLN ILE LEU GLU ALA MET GLU THR ASN TYR
SEQRES 13 B 276 ASN SER MET VAL HIS GLY MET ALA THR LEU ALA ILE GLY
SEQRES 14 B 276 GLY ASP MET ASP SER GLU VAL VAL GLN GLU TYR SER ARG
SEQRES 15 B 276 THR LEU PHE ASN MET GLN PRO ASP ILE ALA LEU SER VAL
SEQRES 16 B 276 ALA ARG MET ILE CYS ALA TYR ASP MET ARG PRO LEU LEU
SEQRES 17 B 276 GLY SER VAL VAL VAL PRO CYS HIS ILE ILE HIS SER CYS
SEQRES 18 B 276 LYS ASP PRO VAL VAL PRO VAL THR ALA ALA GLU TYR ILE
SEQRES 19 B 276 HIS GLN ASN VAL GLY GLY LYS SER VAL MET GLU VAL MET
SEQRES 20 B 276 SER VAL GLU GLY HIS LEU PRO HIS PHE SER ALA PRO GLU
SEQRES 21 B 276 GLY THR ILE PRO VAL LEU LEU ARG HIS ILE ASN HIS ASP
SEQRES 22 B 276 ILE ASP ALA
FORMUL 3 HOH *193(H2 O)
HELIX 1 AA1 MET A 6 ASN A 15 1 10
HELIX 2 AA2 ASP A 35 ARG A 40 5 6
HELIX 3 AA3 LEU A 42 VAL A 47 1 6
HELIX 4 AA4 ASN A 64 TYR A 68 5 5
HELIX 5 AA5 ASP A 71 ALA A 74 5 4
HELIX 6 AA6 ILE A 75 PHE A 90 1 16
HELIX 7 AA7 SER A 101 ARG A 114 1 14
HELIX 8 AA8 ASN A 141 ASN A 155 1 15
HELIX 9 AA9 ASN A 155 ILE A 168 1 14
HELIX 10 AB1 SER A 174 ASN A 186 1 13
HELIX 11 AB2 GLN A 188 TYR A 202 1 15
HELIX 12 AB3 MET A 204 VAL A 211 5 8
HELIX 13 AB4 PRO A 227 VAL A 238 1 12
HELIX 14 AB5 LEU A 253 ALA A 258 1 6
HELIX 15 AB6 ALA A 258 HIS A 272 1 15
HELIX 16 AB7 ILE B 9 ASN B 15 1 7
HELIX 17 AB8 ASP B 35 ARG B 40 5 6
HELIX 18 AB9 LEU B 42 VAL B 47 1 6
HELIX 19 AC1 ASN B 64 TYR B 68 5 5
HELIX 20 AC2 ASP B 71 ALA B 74 5 4
HELIX 21 AC3 ILE B 75 PHE B 90 1 16
HELIX 22 AC4 SER B 101 ARG B 114 1 14
HELIX 23 AC5 ASN B 141 ASN B 155 1 15
HELIX 24 AC6 ASN B 155 GLY B 169 1 15
HELIX 25 AC7 SER B 174 ASN B 186 1 13
HELIX 26 AC8 GLN B 188 TYR B 202 1 15
HELIX 27 AC9 MET B 204 VAL B 211 5 8
HELIX 28 AD1 PRO B 227 VAL B 238 1 12
HELIX 29 AD2 LEU B 253 ALA B 258 1 6
HELIX 30 AD3 ALA B 258 ASN B 271 1 14
SHEET 1 AA1 7 ARG A 17 GLY A 20 0
SHEET 2 AA1 7 TYR A 50 LEU A 54 -1 O VAL A 52 N LEU A 19
SHEET 3 AA1 7 THR A 24 ALA A 29 1 N VAL A 26 O ARG A 51
SHEET 4 AA1 7 CYS A 95 HIS A 100 1 O VAL A 98 N VAL A 27
SHEET 5 AA1 7 PHE A 118 ILE A 124 1 O VAL A 122 N HIS A 97
SHEET 6 AA1 7 CYS A 215 LYS A 222 1 O ILE A 218 N MET A 123
SHEET 7 AA1 7 SER A 242 GLU A 250 1 O MET A 247 N HIS A 219
SHEET 1 AA2 7 ARG B 17 GLY B 20 0
SHEET 2 AA2 7 ARG B 51 LEU B 54 -1 O VAL B 52 N LEU B 19
SHEET 3 AA2 7 THR B 25 ALA B 29 1 N VAL B 26 O ARG B 51
SHEET 4 AA2 7 CYS B 95 HIS B 100 1 O VAL B 98 N VAL B 27
SHEET 5 AA2 7 PHE B 118 ILE B 124 1 O VAL B 122 N HIS B 97
SHEET 6 AA2 7 CYS B 215 LYS B 222 1 O HIS B 216 N MET B 123
SHEET 7 AA2 7 SER B 242 GLU B 250 1 O MET B 247 N HIS B 219
CISPEP 1 GLY B 22 PRO B 23 0 14.25
CRYST1 36.900 122.340 123.600 90.00 90.00 90.00 P 21 21 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 0.027100 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008174 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008091 0.00000
TER 2074 ILE A 274
TER 4128 ILE B 274
MASTER 318 0 0 30 14 0 0 6 4319 2 0 44
END |