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HEADER TOXIN 08-AUG-24 9J3F
TITLE THE STRUCTURE OF PHOSPHOLIPASE TLEB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TLE1 PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS ORYZAE PV. ORYZAE PXO99A;
SOURCE 3 ORGANISM_TAXID: 360094;
SOURCE 4 GENE: PXO_02034;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS HYDROLYZED PHOSPHOLIPID, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.TAN
REVDAT 1 06-AUG-25 9J3F 0
JRNL AUTH Z.TAN
JRNL TITL THE STRUCTURE OF PHOSPHOLIPASE TLEB
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 56711
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.530
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 46.6500 - 4.5780 0.99 3994 146 0.1561 0.1596
REMARK 3 2 4.5780 - 3.6342 1.00 3956 144 0.1312 0.1582
REMARK 3 3 3.6342 - 3.1749 1.00 3908 144 0.1447 0.1616
REMARK 3 4 3.1749 - 2.8847 1.00 3922 143 0.1616 0.1886
REMARK 3 5 2.8847 - 2.6779 1.00 3907 143 0.1613 0.2010
REMARK 3 6 2.6779 - 2.5201 1.00 3906 143 0.1665 0.2046
REMARK 3 7 2.5201 - 2.3939 1.00 3891 141 0.1657 0.2264
REMARK 3 8 2.3939 - 2.2897 1.00 3927 144 0.1803 0.2360
REMARK 3 9 2.2897 - 2.2015 1.00 3870 142 0.1851 0.2262
REMARK 3 10 2.2015 - 2.1255 1.00 3907 143 0.1870 0.2398
REMARK 3 11 2.1255 - 2.0591 1.00 3878 141 0.1918 0.2093
REMARK 3 12 2.0591 - 2.0002 1.00 3911 143 0.2237 0.2794
REMARK 3 13 2.0002 - 1.9476 1.00 3881 143 0.2783 0.2817
REMARK 3 14 1.9476 - 1.9000 1.00 3853 140 0.3388 0.3486
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.800
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 : 0.008 5483
REMARK 3 ANGLE : 0.988 7420
REMARK 3 CHIRALITY : 0.052 779
REMARK 3 PLANARITY : 0.006 986
REMARK 3 DIHEDRAL : 3.171 3294
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 35:450 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.527 3.101 -10.920
REMARK 3 T TENSOR
REMARK 3 T11: 0.0714 T22: 0.0847
REMARK 3 T33: 0.0803 T12: 0.0005
REMARK 3 T13: -0.0012 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.1441 L22: 0.4243
REMARK 3 L33: 0.3536 L12: -0.1405
REMARK 3 L13: -0.0919 L23: 0.2219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0176 S12: -0.0226 S13: 0.0047
REMARK 3 S21: 0.0189 S22: 0.0540 S23: -0.0422
REMARK 3 S31: -0.0229 S32: 0.0326 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 451:681 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.796 -20.839 -33.708
REMARK 3 T TENSOR
REMARK 3 T11: 0.0918 T22: 0.0920
REMARK 3 T33: 0.1170 T12: 0.0120
REMARK 3 T13: -0.0056 T23: -0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 0.2901 L22: 0.3527
REMARK 3 L33: 0.2917 L12: -0.1664
REMARK 3 L13: -0.0512 L23: 0.1175
REMARK 3 S TENSOR
REMARK 3 S11: 0.0244 S12: 0.0271 S13: -0.0637
REMARK 3 S21: 0.0122 S22: -0.0124 S23: 0.0567
REMARK 3 S31: -0.0308 S32: -0.0197 S33: 0.0000
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 9J3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 15-AUG-24.
REMARK 100 THE DEPOSITION ID IS D_1300050262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-20
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 : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56744
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 46.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.18700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 1.71800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.8, 23% PEG3350,
REMARK 280 VAPOR DIFFUSION, 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 35.18300
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: 240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 HIS A 20
REMARK 465 MET A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 MET A 24
REMARK 465 THR A 25
REMARK 465 GLY A 26
REMARK 465 GLY A 27
REMARK 465 GLN A 28
REMARK 465 GLN A 29
REMARK 465 MET A 30
REMARK 465 GLY A 31
REMARK 465 ARG A 32
REMARK 465 GLY A 33
REMARK 465 SER A 34
REMARK 465 SER A 718
REMARK 465 ALA A 719
REMARK 465 LEU A 720
REMARK 465 ALA A 721
REMARK 465 HIS A 722
REMARK 465 SER A 723
REMARK 465 ILE A 724
REMARK 465 ASP A 725
REMARK 465 ALA A 726
REMARK 465 VAL A 727
REMARK 465 ASP A 728
REMARK 465 GLU A 729
REMARK 465 THR A 730
REMARK 465 LEU A 731
REMARK 465 GLU A 732
REMARK 465 GLN A 733
REMARK 465 ILE A 734
REMARK 465 LYS A 735
REMARK 465 GLN A 736
REMARK 465 LEU A 737
REMARK 465 PRO A 738
REMARK 465 GLY A 739
REMARK 465 LYS A 740
REMARK 465 ALA A 741
REMARK 465 LYS A 742
REMARK 465 GLN A 743
REMARK 465 ALA A 744
REMARK 465 VAL A 745
REMARK 465 GLY A 746
REMARK 465 ASP A 747
REMARK 465 ALA A 748
REMARK 465 VAL A 749
REMARK 465 GLU A 750
REMARK 465 SER A 751
REMARK 465 ALA A 752
REMARK 465 VAL A 753
REMARK 465 ASP A 754
REMARK 465 SER A 755
REMARK 465 ALA A 756
REMARK 465 VAL A 757
REMARK 465 GLU A 758
REMARK 465 ALA A 759
REMARK 465 GLY A 760
REMARK 465 LYS A 761
REMARK 465 ASP A 762
REMARK 465 PHE A 763
REMARK 465 VAL A 764
REMARK 465 GLY A 765
REMARK 465 ASP A 766
REMARK 465 GLN A 767
REMARK 465 VAL A 768
REMARK 465 ARG A 769
REMARK 465 LYS A 770
REMARK 465 LEU A 771
REMARK 465 ILE A 772
REMARK 465 PRO A 773
REMARK 465 SER A 774
REMARK 465 GLY A 775
REMARK 465 LEU A 776
REMARK 465 PRO A 777
REMARK 465 ARG A 778
REMARK 465 MET A 779
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 35 CG CD OE1 OE2
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 PHE A 129 54.19 -146.56
REMARK 500 SER A 276 -131.53 66.50
REMARK 500 ASP A 316 72.47 38.17
REMARK 500 ALA A 319 -76.34 -94.12
REMARK 500 HIS A 333 53.14 -104.25
REMARK 500 LYS A 509 118.11 -161.18
REMARK 500 TYR A 598 -51.51 -128.48
REMARK 500 ASP A 696 -158.24 -144.68
REMARK 500 PHE A 704 -99.53 -112.20
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 A1413 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1414 DISTANCE = 7.26 ANGSTROMS
DBREF1 9J3F A 60 779 UNP A0A0K0GNK3_XANOP
DBREF2 9J3F A A0A0K0GNK3 1 720
SEQADV 9J3F MET A 1 UNP A0A0K0GNK INITIATING METHIONINE
SEQADV 9J3F GLY A 2 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 3 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 4 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F HIS A 5 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F HIS A 6 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F HIS A 7 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F HIS A 8 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F HIS A 9 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F HIS A 10 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 11 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 12 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLY A 13 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F LEU A 14 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F VAL A 15 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F PRO A 16 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ARG A 17 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLY A 18 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 19 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F HIS A 20 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F MET A 21 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ALA A 22 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 23 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F MET A 24 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F THR A 25 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLY A 26 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLY A 27 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLN A 28 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLN A 29 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F MET A 30 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLY A 31 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ARG A 32 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLY A 33 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 34 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLU A 35 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F PHE A 36 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F MET A 37 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLN A 38 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F VAL A 39 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 40 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F PHE A 41 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ALA A 42 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F PRO A 43 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F LEU A 44 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F CYS A 45 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F PRO A 46 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLU A 47 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ASN A 48 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F PRO A 49 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F LEU A 50 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLN A 51 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F LEU A 52 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F SER A 53 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ARG A 54 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ALA A 55 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLN A 56 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLN A 57 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F ALA A 58 UNP A0A0K0GNK EXPRESSION TAG
SEQADV 9J3F GLU A 59 UNP A0A0K0GNK EXPRESSION TAG
SEQRES 1 A 779 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 779 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 779 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET GLN VAL
SEQRES 4 A 779 SER PHE ALA PRO LEU CYS PRO GLU ASN PRO LEU GLN LEU
SEQRES 5 A 779 SER ARG ALA GLN GLN ALA GLU MET MET SER ALA GLY LEU
SEQRES 6 A 779 GLY ARG PRO GLN ASP SER CYS CYS ILE ASP LEU ARG TRP
SEQRES 7 A 779 GLY PHE PHE PHE ASP GLY THR ASN ASN ASN PHE HIS ARG
SEQRES 8 A 779 ASP GLN PRO LYS LYS ALA HIS SER ASN VAL ALA ARG LEU
SEQRES 9 A 779 TYR ASP ILE PHE GLU ALA ASP ARG ARG LYS PRO GLU PHE
SEQRES 10 A 779 VAL GLY ARG TYR ALA ALA GLY VAL GLY THR ALA PHE LYS
SEQRES 11 A 779 ASP GLU VAL GLY ASP GLN GLY LEU GLY ILE GLN GLU LYS
SEQRES 12 A 779 ALA GLY LEU ALA ALA GLY TRP GLY GLY GLU ALA ARG ILE
SEQRES 13 A 779 CYS TRP ALA LEU LEU LYS PHE LEU ASP ASN LEU ASN TYR
SEQRES 14 A 779 TYR PHE GLU ARG ILE ASP LEU GLY GLU ALA LEU GLY GLN
SEQRES 15 A 779 LYS ASP PRO ALA THR VAL ARG ARG MET ALA GLN ASP MET
SEQRES 16 A 779 THR ILE PRO SER MET GLU LEU ARG LYS ILE ALA GLY ASP
SEQRES 17 A 779 GLU THR GLU MET LEU ARG GLN ILE SER MET MET ALA SER
SEQRES 18 A 779 LEU GLN SER LEU THR ALA THR ALA LEU ASN LEU PRO ASN
SEQRES 19 A 779 HIS ARG GLY ARG ARG ALA VAL LEU ALA GLU ARG ARG ALA
SEQRES 20 A 779 GLN LEU ARG GLN ARG VAL GLN THR TRP GLN ARG ALA GLN
SEQRES 21 A 779 PRO LYS PRO LYS LEU ARG SER ILE ARG VAL SER VAL PHE
SEQRES 22 A 779 GLY PHE SER ARG GLY ALA ALA GLU ALA ARG VAL PHE CYS
SEQRES 23 A 779 SER TRP LEU LYS ASP ALA CYS ASP GLY GLY GLY GLY GLU
SEQRES 24 A 779 LEU THR LEU CYS GLY ILE PRO VAL GLN LEU ASP LEU LEU
SEQRES 25 A 779 GLY ILE PHE ASP THR VAL ALA SER VAL GLY LEU ALA ASN
SEQRES 26 A 779 SER SER ARG LEU TRP SER GLY HIS GLY GLY TYR ALA SER
SEQRES 27 A 779 GLU ASP ASP LEU ARG ILE ALA PRO TYR VAL ARG ARG CYS
SEQRES 28 A 779 VAL HIS LEU VAL ALA ALA HIS GLU VAL ARG GLY SER PHE
SEQRES 29 A 779 PRO LEU ASP ALA ALA ALA GLY VAL ASN GLY GLU GLU VAL
SEQRES 30 A 779 VAL TYR PRO GLY VAL HIS SER ASP VAL GLY GLY GLY TYR
SEQRES 31 A 779 GLU PRO GLY GLU GLN GLY LYS ALA PHE ILE GLY ASP SER
SEQRES 32 A 779 ILE ASP ASP SER ALA LYS LEU SER GLN ILE ALA LEU CYS
SEQRES 33 A 779 HIS MET TYR ARG GLU ALA MET ALA ALA GLY VAL PRO LEU
SEQRES 34 A 779 ASN LEU SER ALA SER ARG LEU SER LYS GLU THR LYS ALA
SEQRES 35 A 779 ALA PHE LYS VAL ASP LYS GLY LEU ILE ASP ALA PHE ASN
SEQRES 36 A 779 GLY TYR VAL ALA ALA THR GLY SER ILE LYS ALA SER THR
SEQRES 37 A 779 THR VAL ALA LEU THR GLN ALA HIS TYR ALA LEU TYR LEU
SEQRES 38 A 779 ARG TRP ARG ARG LEU ARG LEU ASP ASP THR ALA PRO ASP
SEQRES 39 A 779 GLY MET ALA GLN GLN PRO PHE VAL THR ARG ALA ARG THR
SEQRES 40 A 779 TYR LYS ALA GLN ASP VAL THR ASP LEU LEU GLN THR ASN
SEQRES 41 A 779 ALA GLU LEU ARG GLN GLU TRP ALA ALA LEU GLN GLN ASP
SEQRES 42 A 779 GLU LYS ASP ALA ALA TYR SER SER GLU ALA SER VAL ALA
SEQRES 43 A 779 HIS VAL LEU ARG SER THR LEU ALA PRO ILE ALA ALA ARG
SEQRES 44 A 779 ASP ASP ILE VAL ALA LEU VAL TRP GLY GLU LYS MET THR
SEQRES 45 A 779 GLN TRP ARG GLU VAL LYS PRO ALA TRP ASN ASP LEU SER
SEQRES 46 A 779 PRO LEU ASP ARG ARG ILE VAL ARG LEU HIS ASP ASP TYR
SEQRES 47 A 779 SER HIS ASP SER ARG ALA TRP PHE LYS PRO PHE GLY ALA
SEQRES 48 A 779 ALA SER GLU GLU ALA TRP LYS ARG GLN TYR ARG GLN ARG
SEQRES 49 A 779 MET ASN ARG LEU GLU ALA GLN ASP ASN ALA TRP GLN GLN
SEQRES 50 A 779 TRP ASN ARG ASP VAL GLN PRO VAL ILE ASP ASP ALA VAL
SEQRES 51 A 779 ARG LYS ALA GLN LYS HIS PRO GLY SER PHE GLN PRO THR
SEQRES 52 A 779 PRO GLU VAL ARG PRO MET PRO PRO LEU VAL ALA GLY GLN
SEQRES 53 A 779 ASP LEU LYS ASP LEU LYS GLN TRP ARG SER ASN GLY GLY
SEQRES 54 A 779 VAL ILE PRO THR GLU GLN ASP GLY ARG GLU SER TYR GLY
SEQRES 55 A 779 MET PHE GLY PHE LEU ARG TRP ARG THR ILE PHE VAL PRO
SEQRES 56 A 779 GLU LYS SER ALA LEU ALA HIS SER ILE ASP ALA VAL ASP
SEQRES 57 A 779 GLU THR LEU GLU GLN ILE LYS GLN LEU PRO GLY LYS ALA
SEQRES 58 A 779 LYS GLN ALA VAL GLY ASP ALA VAL GLU SER ALA VAL ASP
SEQRES 59 A 779 SER ALA VAL GLU ALA GLY LYS ASP PHE VAL GLY ASP GLN
SEQRES 60 A 779 VAL ARG LYS LEU ILE PRO SER GLY LEU PRO ARG MET
HET GOL A 801 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *514(H2 O)
HELIX 1 AA1 SER A 53 GLY A 64 1 12
HELIX 2 AA2 ASN A 88 GLN A 93 1 6
HELIX 3 AA3 PRO A 94 LYS A 96 5 3
HELIX 4 AA4 SER A 99 PHE A 108 1 10
HELIX 5 AA5 PHE A 129 GLY A 134 1 6
HELIX 6 AA6 LEU A 138 GLY A 149 1 12
HELIX 7 AA7 GLY A 151 ARG A 173 1 23
HELIX 8 AA8 ASP A 175 LEU A 180 1 6
HELIX 9 AA9 LYS A 183 ALA A 192 1 10
HELIX 10 AB1 GLN A 193 ILE A 197 5 5
HELIX 11 AB2 PRO A 198 GLY A 207 1 10
HELIX 12 AB3 GLY A 207 SER A 221 1 15
HELIX 13 AB4 ASN A 234 GLN A 260 1 27
HELIX 14 AB5 SER A 276 CYS A 293 1 18
HELIX 15 AB6 SER A 338 ARG A 343 1 6
HELIX 16 AB7 VAL A 382 GLY A 388 1 7
HELIX 17 AB8 GLY A 393 LYS A 397 5 5
HELIX 18 AB9 ASP A 406 LYS A 409 5 4
HELIX 19 AC1 LEU A 410 ALA A 425 1 16
HELIX 20 AC2 SER A 437 ALA A 443 1 7
HELIX 21 AC3 ASP A 447 THR A 461 1 15
HELIX 22 AC4 THR A 468 ARG A 487 1 20
HELIX 23 AC5 GLY A 495 GLN A 498 5 4
HELIX 24 AC6 GLN A 499 LYS A 509 1 11
HELIX 25 AC7 LYS A 509 GLU A 534 1 26
HELIX 26 AC8 ALA A 543 LEU A 553 1 11
HELIX 27 AC9 ALA A 554 ALA A 557 5 4
HELIX 28 AD1 ARG A 559 ASN A 582 1 24
HELIX 29 AD2 ASP A 588 TYR A 598 1 11
HELIX 30 AD3 ASP A 601 PHE A 606 1 6
HELIX 31 AD4 SER A 613 HIS A 656 1 44
HELIX 32 AD5 ALA A 674 GLY A 688 1 15
SHEET 1 AA1 7 MET A 37 PHE A 41 0
SHEET 2 AA1 7 GLY A 374 TYR A 379 1 O VAL A 378 N SER A 40
SHEET 3 AA1 7 CYS A 351 ALA A 356 1 N VAL A 355 O TYR A 379
SHEET 4 AA1 7 ILE A 305 PHE A 315 1 N LEU A 312 O VAL A 352
SHEET 5 AA1 7 LYS A 264 PHE A 275 1 N VAL A 270 O GLN A 308
SHEET 6 AA1 7 CYS A 73 PHE A 82 1 N LEU A 76 O ARG A 269
SHEET 7 AA1 7 PHE A 117 ALA A 122 1 O ALA A 122 N PHE A 81
SHEET 1 AA2 5 MET A 37 PHE A 41 0
SHEET 2 AA2 5 GLY A 374 TYR A 379 1 O VAL A 378 N SER A 40
SHEET 3 AA2 5 CYS A 351 ALA A 356 1 N VAL A 355 O TYR A 379
SHEET 4 AA2 5 ILE A 305 PHE A 315 1 N LEU A 312 O VAL A 352
SHEET 5 AA2 5 THR A 301 LEU A 302 -1 N LEU A 302 O ILE A 305
SHEET 1 AA3 2 LEU A 366 ASP A 367 0
SHEET 2 AA3 2 ILE A 712 PHE A 713 1 O PHE A 713 N LEU A 366
SHEET 1 AA4 2 PHE A 399 ILE A 400 0
SHEET 2 AA4 2 SER A 403 ILE A 404 -1 O SER A 403 N ILE A 400
SSBOND 1 CYS A 72 CYS A 73 1555 1555 2.57
CISPEP 1 LYS A 262 PRO A 263 0 -2.65
CRYST1 66.640 70.366 78.775 90.00 99.26 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 0.015006 0.000000 0.002447 0.00000
SCALE2 0.000000 0.014211 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012862 0.00000
TER 5364 LYS A 717
MASTER 377 0 1 32 16 0 0 6 5883 1 8 60
END |