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HEADER TRANSFERASE 27-APR-20 6YUQ
TITLE CAPSULE O-ACETYLTRANSFERASE OF NEISSERIA MENINGITIDIS SEROGROUP A IN
TITLE 2 COMPLEX WITH POLYSACCHARIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SACC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP A;
SOURCE 3 ORGANISM_TAXID: 65699;
SOURCE 4 GENE: SACC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS O-ACETYLTRANSFERASE, A/B HYDROLASE FOLD, SERINE TRANSFERASE,
KEYWDS 2 CATALYTIC TRIAD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.CRAMER,T.FIEBIG,R.FEDOROV,M.MUEHLENHOFF
REVDAT 1 19-AUG-20 6YUQ 0
JRNL AUTH T.FIEBIG,J.T.CRAMER,A.BETHE,P.BARUCH,U.CURTH,J.I.FUEHRING,
JRNL AUTH 2 F.F.R.BUETTNER,U.VOGEL,M.SCHUBERT,R.FEDOROV,M.MUEHLENHOFF
JRNL TITL CAPSULE O-ACETYLTRANSFERASE OF NEISSERIA MENINGITIDIS
JRNL TITL 2 SEROGROUP A IN COMPLEX WITH POLYSACCHARIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18_3845
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 49462
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2475
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 46.2700 - 5.1100 1.00 2833 149 0.1749 0.1772
REMARK 3 2 5.1100 - 4.0600 1.00 2678 140 0.1651 0.1990
REMARK 3 3 4.0600 - 3.5400 1.00 2656 141 0.1948 0.1818
REMARK 3 4 3.5400 - 3.2200 1.00 2626 138 0.2360 0.2208
REMARK 3 5 3.2200 - 2.9900 1.00 2633 138 0.2614 0.3049
REMARK 3 6 2.9900 - 2.8100 1.00 2591 137 0.2524 0.2504
REMARK 3 7 2.8100 - 2.6700 1.00 2615 139 0.2595 0.2724
REMARK 3 8 2.6700 - 2.5600 1.00 2600 136 0.2569 0.3313
REMARK 3 9 2.5600 - 2.4600 1.00 2586 137 0.2605 0.2736
REMARK 3 10 2.4600 - 2.3700 1.00 2569 134 0.2565 0.2759
REMARK 3 11 2.3700 - 2.3000 1.00 2599 137 0.2574 0.3030
REMARK 3 12 2.3000 - 2.2300 1.00 2589 138 0.2688 0.2777
REMARK 3 13 2.2300 - 2.1700 1.00 2573 134 0.2685 0.2958
REMARK 3 14 2.1700 - 2.1200 1.00 2569 136 0.2919 0.3198
REMARK 3 15 2.1200 - 2.0700 1.00 2566 134 0.3006 0.3496
REMARK 3 16 2.0700 - 2.0300 1.00 2576 136 0.3298 0.3607
REMARK 3 17 2.0300 - 1.9900 1.00 2572 136 0.3523 0.3591
REMARK 3 18 1.9900 - 1.9500 1.00 2556 135 0.3892 0.4257
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) : 0.277
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.689
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.33
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 : 0.006 4070
REMARK 3 ANGLE : 0.754 5518
REMARK 3 CHIRALITY : 0.052 634
REMARK 3 PLANARITY : 0.004 683
REMARK 3 DIHEDRAL : 18.657 1451
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 1:245)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6631 39.8527 -29.4478
REMARK 3 T TENSOR
REMARK 3 T11: 0.4311 T22: 0.4341
REMARK 3 T33: 0.3397 T12: -0.0384
REMARK 3 T13: 0.0119 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 5.2528 L22: 3.1059
REMARK 3 L33: 4.2816 L12: -0.0215
REMARK 3 L13: 1.4353 L23: 0.4163
REMARK 3 S TENSOR
REMARK 3 S11: -0.0808 S12: 0.6078 S13: -0.1853
REMARK 3 S21: -0.2665 S22: 0.2112 S23: -0.1687
REMARK 3 S31: 0.0854 S32: 0.5261 S33: -0.1094
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESSEQ 1:245)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2634 31.1219 3.2555
REMARK 3 T TENSOR
REMARK 3 T11: 0.4901 T22: 0.4355
REMARK 3 T33: 0.4451 T12: 0.0367
REMARK 3 T13: -0.0618 T23: -0.0692
REMARK 3 L TENSOR
REMARK 3 L11: 2.9868 L22: 3.0883
REMARK 3 L33: 4.1075 L12: 1.0861
REMARK 3 L13: -1.6686 L23: -1.5984
REMARK 3 S TENSOR
REMARK 3 S11: -0.0834 S12: -0.2718 S13: -0.3498
REMARK 3 S21: 0.1699 S22: -0.1306 S23: -0.2306
REMARK 3 S31: 0.5112 S32: 0.3065 S33: 0.2087
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 6YUQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1292108308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49502
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 48.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 26.20
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 25.60
REMARK 200 R MERGE FOR SHELL (I) : 2.81800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.200
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: 6YUO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NATIVE WILD TYPE CSAC CRYSTALLIZED IN
REMARK 280 SITTING DROP SETUPS AT CONCENTRATIONS OF APPROX. 18MG/ML. FINE
REMARK 280 SCREENS AROUND INITIAL SCREENING CONDITIONS RESULTED IN MANY
REMARK 280 ISOMORPHOUS CRYSTALS. MOTHER LIQUOR CONTAINED 50MM HEPES PH 7.0,
REMARK 280 100 MM HEPES PH 7.6, 100MM NACL, 5MM MGCL2, 1MM EDTA, AND 31-42%
REMARK 280 PEG200. GOOD QUALITY CRYSTALS GREW AT 4, 12, AND 18C., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 35.12650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 68.74150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 68.74150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.56325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 68.74150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 68.74150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.68975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 68.74150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.74150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 17.56325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 68.74150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.74150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.68975
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 35.12650
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -35.12650
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 ASN A 246
REMARK 465 ILE A 247
REMARK 465 LEU A 248
REMARK 465 GLU A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 ASN B 246
REMARK 465 ILE B 247
REMARK 465 LEU B 248
REMARK 465 GLU B 249
REMARK 465 HIS B 250
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 465 HIS B 255
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 LYS A 48 CG CD CE NZ
REMARK 470 GLU A 72 CG CD OE1 OE2
REMARK 470 GLU A 106 CD OE1 OE2
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 LYS A 220 CG CD CE NZ
REMARK 470 LYS A 241 CD CE NZ
REMARK 470 GLN A 245 CG CD OE1 NE2
REMARK 470 GLU B 31 CG CD OE1 OE2
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 LYS B 161 CG CD CE NZ
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 LYS B 220 CG CD CE NZ
REMARK 470 GLN B 245 CG CD OE1 NE2
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 GLU A 31 -52.53 70.33
REMARK 500 ASP A 74 70.95 -155.19
REMARK 500 SER A 114 -122.50 59.80
REMARK 500 ALA A 136 57.56 36.42
REMARK 500 SER A 149 114.28 -162.55
REMARK 500 GLU B 31 -53.06 72.42
REMARK 500 ASP B 74 74.84 -156.10
REMARK 500 SER B 114 -122.00 63.47
REMARK 500 SER B 149 112.98 -163.51
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6YUQ A 1 247 UNP O68216 O68216_NEIMD 1 247
DBREF 6YUQ B 1 247 UNP O68216 O68216_NEIMD 1 247
SEQADV 6YUQ LEU A 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ GLU A 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS A 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS A 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS A 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS A 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS A 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS A 255 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ LEU B 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ GLU B 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS B 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS B 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS B 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS B 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS B 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUQ HIS B 255 UNP O68216 EXPRESSION TAG
SEQRES 1 A 255 MET LEU SER ASN LEU LYS THR GLY ASN ASN ILE LEU GLY
SEQRES 2 A 255 LEU PRO GLU PHE GLU LEU ASN GLY CYS ARG PHE LEU TYR
SEQRES 3 A 255 LYS LYS GLY ILE GLU LYS THR ILE ILE THR PHE SER ALA
SEQRES 4 A 255 PHE PRO PRO LYS ASP ILE ALA GLN LYS TYR ASN TYR ILE
SEQRES 5 A 255 LYS ASP PHE LEU SER SER ASN TYR THR PHE LEU ALA PHE
SEQRES 6 A 255 LEU ASP THR LYS TYR PRO GLU ASP ASP ALA ARG GLY THR
SEQRES 7 A 255 TYR TYR ILE THR ASN GLU LEU ASP ASN GLY TYR LEU GLN
SEQRES 8 A 255 THR ILE HIS CYS ILE ILE GLN LEU LEU SER ASN THR ASN
SEQRES 9 A 255 GLN GLU ASP THR TYR LEU LEU GLY SER SER LYS GLY GLY
SEQRES 10 A 255 VAL GLY ALA LEU LEU LEU GLY LEU THR TYR ASN TYR PRO
SEQRES 11 A 255 ASN ILE ILE ILE ASN ALA PRO GLN ALA LYS LEU ALA ASP
SEQRES 12 A 255 TYR ILE LYS THR ARG SER LYS THR ILE LEU SER TYR MET
SEQRES 13 A 255 LEU GLY THR SER LYS ARG PHE GLN ASP ILE ASN TYR ASP
SEQRES 14 A 255 TYR ILE ASN ASP PHE LEU LEU SER LYS ILE LYS THR CYS
SEQRES 15 A 255 ASP SER SER LEU LYS TRP ASN ILE HIS ILE THR CYS GLY
SEQRES 16 A 255 LYS ASP ASP SER TYR HIS LEU ASN GLU LEU GLU ILE LEU
SEQRES 17 A 255 LYS ASN GLU PHE ASN ILE LYS ALA ILE THR ILE LYS THR
SEQRES 18 A 255 LYS LEU ILE SER GLY GLY HIS ASP ASN GLU ALA ILE ALA
SEQRES 19 A 255 HIS TYR ARG GLU TYR PHE LYS THR ILE ILE GLN ASN ILE
SEQRES 20 A 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 255 MET LEU SER ASN LEU LYS THR GLY ASN ASN ILE LEU GLY
SEQRES 2 B 255 LEU PRO GLU PHE GLU LEU ASN GLY CYS ARG PHE LEU TYR
SEQRES 3 B 255 LYS LYS GLY ILE GLU LYS THR ILE ILE THR PHE SER ALA
SEQRES 4 B 255 PHE PRO PRO LYS ASP ILE ALA GLN LYS TYR ASN TYR ILE
SEQRES 5 B 255 LYS ASP PHE LEU SER SER ASN TYR THR PHE LEU ALA PHE
SEQRES 6 B 255 LEU ASP THR LYS TYR PRO GLU ASP ASP ALA ARG GLY THR
SEQRES 7 B 255 TYR TYR ILE THR ASN GLU LEU ASP ASN GLY TYR LEU GLN
SEQRES 8 B 255 THR ILE HIS CYS ILE ILE GLN LEU LEU SER ASN THR ASN
SEQRES 9 B 255 GLN GLU ASP THR TYR LEU LEU GLY SER SER LYS GLY GLY
SEQRES 10 B 255 VAL GLY ALA LEU LEU LEU GLY LEU THR TYR ASN TYR PRO
SEQRES 11 B 255 ASN ILE ILE ILE ASN ALA PRO GLN ALA LYS LEU ALA ASP
SEQRES 12 B 255 TYR ILE LYS THR ARG SER LYS THR ILE LEU SER TYR MET
SEQRES 13 B 255 LEU GLY THR SER LYS ARG PHE GLN ASP ILE ASN TYR ASP
SEQRES 14 B 255 TYR ILE ASN ASP PHE LEU LEU SER LYS ILE LYS THR CYS
SEQRES 15 B 255 ASP SER SER LEU LYS TRP ASN ILE HIS ILE THR CYS GLY
SEQRES 16 B 255 LYS ASP ASP SER TYR HIS LEU ASN GLU LEU GLU ILE LEU
SEQRES 17 B 255 LYS ASN GLU PHE ASN ILE LYS ALA ILE THR ILE LYS THR
SEQRES 18 B 255 LYS LEU ILE SER GLY GLY HIS ASP ASN GLU ALA ILE ALA
SEQRES 19 B 255 HIS TYR ARG GLU TYR PHE LYS THR ILE ILE GLN ASN ILE
SEQRES 20 B 255 LEU GLU HIS HIS HIS HIS HIS HIS
HET EDO A 401 4
HET PEG A 402 7
HET CL A 403 1
HET BMX A 404 19
HET BMX A 405 18
HET BMX A 406 18
HET BM3 A 407 14
HET PGE B 301 10
HET CL B 302 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
HETNAM BMX 2-ACETAMIDO-2-DEOXY-6-O-PHOSPHONO-ALPHA-D-MANNOPYRANOSE
HETNAM BM3 2-ACETAMIDO-2-DEOXY-ALPHA-D-MANNOPYRANOSE
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN BMX 2-(ACETYLAMINO)-2-DEOXY-6-O-PHOSPHONO-ALPHA-D-
HETSYN 2 BMX MANNOPYRANOSE; N-ACETYL-6-O-PHOSPHONO-ALPHA-D-
HETSYN 3 BMX MANNOSAMINE; 2-ACETAMIDO-2-DEOXY-6-O-PHOSPHONO-ALPHA-
HETSYN 4 BMX D-MANNOSE; 2-ACETAMIDO-2-DEOXY-6-O-PHOSPHONO-D-
HETSYN 5 BMX MANNOSE; 2-ACETAMIDO-2-DEOXY-6-O-PHOSPHONO-MANNOSE
HETSYN BM3 N-ACETYL-ALPHA-D-MANNOSAMINE; 2-ACETAMIDO-2-DEOXY-
HETSYN 2 BM3 ALPHA-D-MANNOSE; 2-ACETAMIDO-2-DEOXY-D-MANNOSE; 2-
HETSYN 3 BM3 ACETAMIDO-2-DEOXY-MANNOSE; 2-(ACETYLAMINO)-2-DEOXY-
HETSYN 4 BM3 ALPHA-D-MANNOPYRANOSE
FORMUL 3 EDO C2 H6 O2
FORMUL 4 PEG C4 H10 O3
FORMUL 5 CL 2(CL 1-)
FORMUL 6 BMX 3(C8 H16 N O9 P)
FORMUL 9 BM3 C8 H15 N O6
FORMUL 10 PGE C6 H14 O4
FORMUL 12 HOH *47(H2 O)
HELIX 1 AA1 MET A 1 ASN A 4 5 4
HELIX 2 AA2 TYR A 51 LEU A 56 1 6
HELIX 3 AA3 ASN A 87 SER A 101 1 15
HELIX 4 AA4 ASN A 104 GLU A 106 5 3
HELIX 5 AA5 SER A 114 ASN A 128 1 15
HELIX 6 AA6 LYS A 140 THR A 147 1 8
HELIX 7 AA7 SER A 149 GLY A 158 1 10
HELIX 8 AA8 SER A 160 ARG A 162 5 3
HELIX 9 AA9 PHE A 163 ASP A 173 1 11
HELIX 10 AB1 ASP A 173 THR A 181 1 9
HELIX 11 AB2 ASP A 198 LYS A 215 1 18
HELIX 12 AB3 ASP A 229 GLN A 245 1 17
HELIX 13 AB4 MET B 1 ASN B 4 5 4
HELIX 14 AB5 TYR B 51 SER B 57 1 7
HELIX 15 AB6 PRO B 71 ALA B 75 5 5
HELIX 16 AB7 ASN B 87 SER B 101 1 15
HELIX 17 AB8 ASN B 104 GLU B 106 5 3
HELIX 18 AB9 SER B 114 ASN B 128 1 15
HELIX 19 AC1 LYS B 140 SER B 149 1 10
HELIX 20 AC2 SER B 149 GLY B 158 1 10
HELIX 21 AC3 SER B 160 ASP B 173 1 14
HELIX 22 AC4 ASP B 173 THR B 181 1 9
HELIX 23 AC5 ASP B 198 LYS B 215 1 18
HELIX 24 AC6 ASP B 229 GLN B 245 1 17
SHEET 1 AA1 9 LYS A 6 ILE A 11 0
SHEET 2 AA1 9 LEU A 14 LEU A 19 -1 O GLU A 16 N THR A 7
SHEET 3 AA1 9 CYS A 22 LYS A 27 -1 O PHE A 24 N PHE A 17
SHEET 4 AA1 9 TYR A 60 PHE A 65 -1 O PHE A 62 N LYS A 27
SHEET 5 AA1 9 ILE A 30 PHE A 37 1 N ILE A 34 O THR A 61
SHEET 6 AA1 9 THR A 108 SER A 113 1 O LEU A 111 N ILE A 35
SHEET 7 AA1 9 ASN A 131 ASN A 135 1 O ASN A 131 N LEU A 110
SHEET 8 AA1 9 ASN A 189 GLY A 195 1 O HIS A 191 N ILE A 132
SHEET 9 AA1 9 LYS A 220 ILE A 224 1 O LYS A 220 N ILE A 190
SHEET 1 AA2 9 LYS B 6 ILE B 11 0
SHEET 2 AA2 9 LEU B 14 LEU B 19 -1 O LEU B 14 N ILE B 11
SHEET 3 AA2 9 CYS B 22 LYS B 27 -1 O PHE B 24 N PHE B 17
SHEET 4 AA2 9 THR B 61 PHE B 65 -1 O PHE B 62 N LYS B 27
SHEET 5 AA2 9 THR B 33 PHE B 37 1 N ILE B 34 O THR B 61
SHEET 6 AA2 9 THR B 108 SER B 113 1 O TYR B 109 N ILE B 35
SHEET 7 AA2 9 ASN B 131 ASN B 135 1 O ASN B 131 N LEU B 110
SHEET 8 AA2 9 ASN B 189 GLY B 195 1 O HIS B 191 N ILE B 132
SHEET 9 AA2 9 LYS B 220 ILE B 224 1 O LYS B 220 N ILE B 190
LINK O18 BMX A 404 C1 BMX A 405 1555 1555 1.36
LINK O18 BMX A 405 C1 BMX A 406 1555 1555 1.38
LINK O18 BMX A 406 C1 BM3 A 407 1555 1555 1.37
CISPEP 1 TYR A 70 PRO A 71 0 -11.74
CISPEP 2 TYR B 70 PRO B 71 0 -1.34
CRYST1 137.483 137.483 70.253 90.00 90.00 90.00 P 41 21 2 16
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 0.007274 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007274 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014234 0.00000
TER 1944 GLN A 245
TER 3900 GLN B 245
MASTER 337 0 9 24 18 0 0 6 4037 2 90 40
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