HEADER CELL CYCLE 05-AUG-18 6H9N
TITLE COMPLEX OF THE PERIPLASMIC DOMAINS OF BACTERIAL CELL DIVISION PROTEINS
TITLE 2 FTSQ AND FTSB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN FTSQ;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CELL DIVISION PROTEIN FTSB;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: FTSQ, B0093, JW0091;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI 55989;
SOURCE 9 ORGANISM_TAXID: 585055;
SOURCE 10 GENE: FTSB, EC55989_3020;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BACTERIAL CELL DIVISION, DIVISOME, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KUREISAITE-CIZIENE,J.LOWE
REVDAT 3 17-JAN-24 6H9N 1 REMARK
REVDAT 2 26-SEP-18 6H9N 1 JRNL
REVDAT 1 05-SEP-18 6H9N 0
JRNL AUTH D.KUREISAITE-CIZIENE,A.VARADAJAN,S.H.MCLAUGHLIN,M.GLAS,
JRNL AUTH 2 A.MONTON SILVA,R.LUIRINK,C.MUELLER,T.DEN BLAAUWEN,
JRNL AUTH 3 T.N.GROSSMANN,J.LUIRINK,J.LOWE
JRNL TITL STRUCTURAL ANALYSIS OF THE INTERACTION BETWEEN THE BACTERIAL
JRNL TITL 2 CELL DIVISION PROTEINS FTSQ AND FTSB.
JRNL REF MBIO V. 9 2018
JRNL REFN ESSN 2150-7511
JRNL PMID 30206170
JRNL DOI 10.1128/MBIO.01346-18
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 15024
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840
REMARK 3 FREE R VALUE TEST SET COUNT : 1340
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 29.9955 - 5.5907 0.99 2595 159 0.1832 0.1601
REMARK 3 2 5.5907 - 4.4421 1.00 2657 121 0.1879 0.2090
REMARK 3 3 4.4421 - 3.8820 0.99 2633 136 0.1971 0.2916
REMARK 3 4 3.8820 - 3.5276 1.00 2661 137 0.2424 0.2705
REMARK 3 5 3.5276 - 3.2751 1.00 2611 145 0.2483 0.3577
REMARK 3 6 3.2751 - 3.0822 0.99 2666 111 0.2766 0.3142
REMARK 3 7 3.0822 - 2.9280 0.98 2618 134 0.2895 0.3322
REMARK 3 8 2.9280 - 2.8006 1.00 2621 143 0.3037 0.3433
REMARK 3 9 2.8006 - 2.6929 0.99 2655 118 0.3420 0.3339
REMARK 3 10 2.6929 - 2.6000 0.99 2627 136 0.3760 0.3891
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.930
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 : 0.009 1878
REMARK 3 ANGLE : 1.162 2540
REMARK 3 CHIRALITY : 0.058 275
REMARK 3 PLANARITY : 0.007 333
REMARK 3 DIHEDRAL : 22.200 1151
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 6H9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1200011160.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-16
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 : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92819
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15037
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 12.80
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 13.40
REMARK 200 R MERGE FOR SHELL (I) : 1.70200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 2VH1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M POTASSIUM THIOCYANATE, 20 % PEG
REMARK 280 550 MME, 0.1 M SODIUM CACODYLATE PH 6.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 53.19600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 46.89250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.89250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.59800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.89250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.89250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.79400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.89250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.89250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.59800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.89250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.89250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 79.79400
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 53.19600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 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 57
REMARK 465 PRO A 261
REMARK 465 GLU A 262
REMARK 465 GLU A 263
REMARK 465 SER A 264
REMARK 465 THR A 265
REMARK 465 GLN A 266
REMARK 465 GLN A 267
REMARK 465 GLN A 268
REMARK 465 ASN A 269
REMARK 465 GLN A 270
REMARK 465 ALA A 271
REMARK 465 GLN A 272
REMARK 465 ALA A 273
REMARK 465 GLU A 274
REMARK 465 GLN A 275
REMARK 465 GLN A 276
REMARK 465 GLY A 277
REMARK 465 SER A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 GLY B 18
REMARK 465 SER B 19
REMARK 465 HIS B 20
REMARK 465 MET B 21
REMARK 465 GLY B 22
REMARK 465 LYS B 23
REMARK 465 ASN B 24
REMARK 465 GLY B 25
REMARK 465 ILE B 26
REMARK 465 HIS B 27
REMARK 465 ASP B 28
REMARK 465 TYR B 29
REMARK 465 THR B 30
REMARK 465 ARG B 31
REMARK 465 VAL B 32
REMARK 465 ASN B 33
REMARK 465 ASP B 34
REMARK 465 ASP B 35
REMARK 465 VAL B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 GLN B 39
REMARK 465 GLN B 40
REMARK 465 ALA B 41
REMARK 465 THR B 42
REMARK 465 ASN B 43
REMARK 465 ALA B 44
REMARK 465 LYS B 45
REMARK 465 LEU B 46
REMARK 465 LYS B 47
REMARK 465 ALA B 48
REMARK 465 ARG B 49
REMARK 465 ASN B 50
REMARK 465 ASP B 51
REMARK 465 GLN B 52
REMARK 465 LEU B 53
REMARK 465 PHE B 54
REMARK 465 ALA B 55
REMARK 465 GLU B 56
REMARK 465 ILE B 57
REMARK 465 ASP B 58
REMARK 465 ASP B 59
REMARK 465 LEU B 60
REMARK 465 ASN B 61
REMARK 465 GLY B 62
REMARK 465 GLY B 63
REMARK 465 VAL B 88
REMARK 465 PRO B 89
REMARK 465 ASP B 90
REMARK 465 ALA B 91
REMARK 465 SER B 92
REMARK 465 LYS B 93
REMARK 465 ARG B 94
REMARK 465 ALA B 95
REMARK 465 GLN B 96
REMARK 465 SER B 97
REMARK 465 ALA B 98
REMARK 465 GLY B 99
REMARK 465 GLN B 100
REMARK 465 ASN B 101
REMARK 465 ASN B 102
REMARK 465 ARG B 103
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 ALA A 80 16.39 -67.73
REMARK 500 LEU A 81 -40.68 -138.75
REMARK 500 MET A 88 -83.77 -58.36
REMARK 500 PRO A 116 -74.24 -57.18
REMARK 500 ALA A 130 149.30 -171.34
REMARK 500 ASN A 133 -122.16 42.26
REMARK 500 HIS A 136 -169.36 -113.38
REMARK 500 ARG A 197 41.68 71.58
REMARK 500 ASP A 206 -1.28 75.46
REMARK 500 ASP A 215 92.44 -61.26
REMARK 500 SER A 250 43.83 -158.05
REMARK 500 THR B 78 -152.97 -124.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 86 PHE A 87 -133.78
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6H9N A 58 276 UNP P06136 FTSQ_ECOLI 58 276
DBREF 6H9N B 22 103 UNP B7LEG6 FTSB_ECO55 22 103
SEQADV 6H9N MET A 57 UNP P06136 INITIATING METHIONINE
SEQADV 6H9N GLY A 277 UNP P06136 EXPRESSION TAG
SEQADV 6H9N SER A 278 UNP P06136 EXPRESSION TAG
SEQADV 6H9N HIS A 279 UNP P06136 EXPRESSION TAG
SEQADV 6H9N HIS A 280 UNP P06136 EXPRESSION TAG
SEQADV 6H9N HIS A 281 UNP P06136 EXPRESSION TAG
SEQADV 6H9N HIS A 282 UNP P06136 EXPRESSION TAG
SEQADV 6H9N HIS A 283 UNP P06136 EXPRESSION TAG
SEQADV 6H9N HIS A 284 UNP P06136 EXPRESSION TAG
SEQADV 6H9N MET B 1 UNP B7LEG6 INITIATING METHIONINE
SEQADV 6H9N GLY B 2 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N SER B 3 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N SER B 4 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N HIS B 5 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N HIS B 6 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N HIS B 7 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N HIS B 8 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N HIS B 9 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N HIS B 10 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N SER B 11 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N SER B 12 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N GLY B 13 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N LEU B 14 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N VAL B 15 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N PRO B 16 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N ARG B 17 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N GLY B 18 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N SER B 19 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N HIS B 20 UNP B7LEG6 EXPRESSION TAG
SEQADV 6H9N MET B 21 UNP B7LEG6 EXPRESSION TAG
SEQRES 1 A 228 MET SER LYS LEU VAL LEU THR GLY GLU ARG HIS TYR THR
SEQRES 2 A 228 ARG ASN ASP ASP ILE ARG GLN SER ILE LEU ALA LEU GLY
SEQRES 3 A 228 GLU PRO GLY THR PHE MET THR GLN ASP VAL ASN ILE ILE
SEQRES 4 A 228 GLN THR GLN ILE GLU GLN ARG LEU PRO TRP ILE LYS GLN
SEQRES 5 A 228 VAL SER VAL ARG LYS GLN TRP PRO ASP GLU LEU LYS ILE
SEQRES 6 A 228 HIS LEU VAL GLU TYR VAL PRO ILE ALA ARG TRP ASN ASP
SEQRES 7 A 228 GLN HIS MET VAL ASP ALA GLU GLY ASN THR PHE SER VAL
SEQRES 8 A 228 PRO PRO GLU ARG THR SER LYS GLN VAL LEU PRO MET LEU
SEQRES 9 A 228 TYR GLY PRO GLU GLY SER ALA ASN GLU VAL LEU GLN GLY
SEQRES 10 A 228 TYR ARG GLU MET GLY GLN MET LEU ALA LYS ASP ARG PHE
SEQRES 11 A 228 THR LEU LYS GLU ALA ALA MET THR ALA ARG ARG SER TRP
SEQRES 12 A 228 GLN LEU THR LEU ASN ASN ASP ILE LYS LEU ASN LEU GLY
SEQRES 13 A 228 ARG GLY ASP THR MET LYS ARG LEU ALA ARG PHE VAL GLU
SEQRES 14 A 228 LEU TYR PRO VAL LEU GLN GLN GLN ALA GLN THR ASP GLY
SEQRES 15 A 228 LYS ARG ILE SER TYR VAL ASP LEU ARG TYR ASP SER GLY
SEQRES 16 A 228 ALA ALA VAL GLY TRP ALA PRO LEU PRO PRO GLU GLU SER
SEQRES 17 A 228 THR GLN GLN GLN ASN GLN ALA GLN ALA GLU GLN GLN GLY
SEQRES 18 A 228 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 103 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 103 LEU VAL PRO ARG GLY SER HIS MET GLY LYS ASN GLY ILE
SEQRES 3 B 103 HIS ASP TYR THR ARG VAL ASN ASP ASP VAL ALA ALA GLN
SEQRES 4 B 103 GLN ALA THR ASN ALA LYS LEU LYS ALA ARG ASN ASP GLN
SEQRES 5 B 103 LEU PHE ALA GLU ILE ASP ASP LEU ASN GLY GLY GLN GLU
SEQRES 6 B 103 ALA LEU GLU GLU ARG ALA ARG ASN GLU LEU SER MET THR
SEQRES 7 B 103 ARG PRO GLY GLU THR PHE TYR ARG LEU VAL PRO ASP ALA
SEQRES 8 B 103 SER LYS ARG ALA GLN SER ALA GLY GLN ASN ASN ARG
FORMUL 3 HOH *7(H2 O)
HELIX 1 AA1 ARG A 70 ALA A 80 1 11
HELIX 2 AA2 ASP A 91 LEU A 103 1 13
HELIX 3 AA3 PRO A 148 THR A 152 5 5
HELIX 4 AA4 SER A 166 LYS A 183 1 18
HELIX 5 AA5 ASP A 215 ASP A 237 1 23
HELIX 6 AA6 GLU B 65 GLU B 74 1 10
SHEET 1 AA1 3 LYS A 59 GLU A 65 0
SHEET 2 AA1 3 GLU A 118 GLU A 125 1 O ILE A 121 N THR A 63
SHEET 3 AA1 3 ILE A 106 GLN A 114 -1 N GLN A 108 O VAL A 124
SHEET 1 AA210 THR A 144 PHE A 145 0
SHEET 2 AA210 HIS A 136 VAL A 138 -1 N MET A 137 O PHE A 145
SHEET 3 AA210 ALA A 130 TRP A 132 -1 N ALA A 130 O VAL A 138
SHEET 4 AA210 MET A 159 TYR A 161 1 O LEU A 160 N ARG A 131
SHEET 5 AA210 LEU A 188 MET A 193 1 O ALA A 191 N MET A 159
SHEET 6 AA210 TRP A 199 LEU A 203 -1 O THR A 202 N LYS A 189
SHEET 7 AA210 LYS A 208 GLY A 212 -1 O LEU A 209 N LEU A 201
SHEET 8 AA210 LYS A 239 ASP A 245 1 O VAL A 244 N ASN A 210
SHEET 9 AA210 GLY A 251 PRO A 258 -1 O ALA A 253 N ASP A 245
SHEET 10 AA210 THR B 83 ARG B 86 -1 O THR B 83 N VAL A 254
CISPEP 1 TRP A 115 PRO A 116 0 20.62
CRYST1 93.785 93.785 106.392 90.00 90.00 90.00 P 41 21 2 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 0.010663 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
