HEADER BIOSYNTHETIC PROTEIN 05-JUL-04 1TXK
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI OPGG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCANS BIOSYNTHESIS PROTEIN G;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OPGG;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: OPGG;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET29A
KEYWDS BETA-SANDWICH, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HANOULLE,E.ROLLET,B.CLANTIN,I.LANDRIEU,C.ODBERG-FERRAGUT,G.LIPPENS,
AUTHOR 2 J.P.BOHIN,V.VILLERET
REVDAT 4 13-JUL-11 1TXK 1 VERSN
REVDAT 3 24-FEB-09 1TXK 1 VERSN
REVDAT 2 14-FEB-06 1TXK 1 REMARK
REVDAT 1 07-SEP-04 1TXK 0
JRNL AUTH X.HANOULLE,E.ROLLET,B.CLANTIN,I.LANDRIEU,C.ODBERG-FERRAGUT,
JRNL AUTH 2 G.LIPPENS,J.P.BOHIN,V.VILLERET
JRNL TITL STRUCTURAL ANALYSIS OF ESCHERICHIA COLI OPGG, A PROTEIN
JRNL TITL 2 REQUIRED FOR THE BIOSYNTHESIS OF OSMOREGULATED PERIPLASMIC
JRNL TITL 3 GLUCANS.
JRNL REF J.MOL.BIOL. V. 342 195 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15313617
JRNL DOI 10.1016/J.JMB.2004.07.004
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3445747.350
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 80513
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 7856
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11756
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1188
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7813
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 477
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.35000
REMARK 3 B22 (A**2) : 4.28000
REMARK 3 B33 (A**2) : -9.63000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.89
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 42.33
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUL-04.
REMARK 100 THE RCSB ID CODE IS RCSB023005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793, 0.9795, 0.9739
REMARK 200 MONOCHROMATOR : SI CRYSTALS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XNEMO
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 200, SODIUM ACETATE, MES, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 31.93000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 107.82500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.06000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 107.82500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.06000
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, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 22
REMARK 465 VAL A 50
REMARK 465 PHE A 51
REMARK 465 ARG A 52
REMARK 465 ASP A 53
REMARK 465 HIS A 517
REMARK 465 HIS A 518
REMARK 465 HIS A 519
REMARK 465 VAL B 50
REMARK 465 PHE B 51
REMARK 465 ARG B 52
REMARK 465 ASP B 53
REMARK 465 GLU B 513
REMARK 465 HIS B 514
REMARK 465 HIS B 515
REMARK 465 HIS B 516
REMARK 465 HIS B 517
REMARK 465 HIS B 518
REMARK 465 HIS B 519
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 492 O - C - N ANGL. DEV. = 10.7 DEGREES
REMARK 500 VAL A 493 C - N - CA ANGL. DEV. = -15.2 DEGREES
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 PRO A 48 -134.40 -73.90
REMARK 500 TRP A 71 10.37 83.36
REMARK 500 MSE A 87 -122.03 59.73
REMARK 500 GLN A 119 -81.87 -36.66
REMARK 500 ALA A 154 -129.01 41.74
REMARK 500 LEU A 255 -60.63 -91.66
REMARK 500 GLN A 260 81.75 -154.65
REMARK 500 ASN A 306 60.92 61.76
REMARK 500 GLU A 323 -0.40 71.41
REMARK 500 ASP A 390 74.57 -109.32
REMARK 500 LYS A 469 30.19 71.34
REMARK 500 ASN A 494 -160.84 -103.61
REMARK 500 PRO B 48 -139.21 -75.17
REMARK 500 TRP B 71 14.65 84.00
REMARK 500 THR B 76 135.60 -172.29
REMARK 500 MSE B 87 -128.90 53.05
REMARK 500 ASP B 117 52.41 -97.33
REMARK 500 GLN B 119 -85.04 -39.47
REMARK 500 ALA B 154 -126.47 34.85
REMARK 500 LEU B 255 -60.42 -97.58
REMARK 500 GLN B 260 80.43 -163.92
REMARK 500 ASN B 293 77.97 -111.69
REMARK 500 ASP B 390 72.38 -110.05
REMARK 500 THR B 409 -87.63 -54.33
REMARK 500 PRO B 444 63.68 -68.96
REMARK 500 ALA B 495 -111.65 63.29
REMARK 500 ASN B 510 2.74 82.66
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 771 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH A 802 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH B 674 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH B 690 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 732 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH B 737 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH B 740 DISTANCE = 5.16 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 600 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 320 OG
REMARK 620 2 SER B 320 OG 157.7
REMARK 620 3 HOH A 840 O 99.6 102.6
REMARK 620 4 HOH A 839 O 77.8 80.1 177.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 600
DBREF 1TXK A 23 511 UNP P33136 OPGG_ECOLI 23 511
DBREF 1TXK B 23 511 UNP P33136 OPGG_ECOLI 23 511
SEQADV 1TXK MET A 22 UNP P33136 INITIATING METHIONINE
SEQADV 1TXK MSE A 54 UNP P33136 MET 54 MODIFIED RESIDUE
SEQADV 1TXK MSE A 87 UNP P33136 MET 87 MODIFIED RESIDUE
SEQADV 1TXK MSE A 151 UNP P33136 MET 151 MODIFIED RESIDUE
SEQADV 1TXK MSE A 223 UNP P33136 MET 223 MODIFIED RESIDUE
SEQADV 1TXK MSE A 253 UNP P33136 MET 253 MODIFIED RESIDUE
SEQADV 1TXK MSE A 304 UNP P33136 MET 304 MODIFIED RESIDUE
SEQADV 1TXK MSE A 379 UNP P33136 MET 379 MODIFIED RESIDUE
SEQADV 1TXK MSE A 436 UNP P33136 MET 436 MODIFIED RESIDUE
SEQADV 1TXK MSE A 475 UNP P33136 MET 475 MODIFIED RESIDUE
SEQADV 1TXK MSE A 488 UNP P33136 MET 488 MODIFIED RESIDUE
SEQADV 1TXK VAL A 512 UNP P33136 EXPRESSION TAG
SEQADV 1TXK GLU A 513 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS A 514 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS A 515 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS A 516 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS A 517 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS A 518 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS A 519 UNP P33136 EXPRESSION TAG
SEQADV 1TXK MET B 22 UNP P33136 INITIATING METHIONINE
SEQADV 1TXK MSE B 54 UNP P33136 MET 54 MODIFIED RESIDUE
SEQADV 1TXK MSE B 87 UNP P33136 MET 87 MODIFIED RESIDUE
SEQADV 1TXK MSE B 151 UNP P33136 MET 151 MODIFIED RESIDUE
SEQADV 1TXK MSE B 223 UNP P33136 MET 223 MODIFIED RESIDUE
SEQADV 1TXK MSE B 253 UNP P33136 MET 253 MODIFIED RESIDUE
SEQADV 1TXK MSE B 304 UNP P33136 MET 304 MODIFIED RESIDUE
SEQADV 1TXK MSE B 379 UNP P33136 MET 379 MODIFIED RESIDUE
SEQADV 1TXK MSE B 436 UNP P33136 MET 436 MODIFIED RESIDUE
SEQADV 1TXK MSE B 475 UNP P33136 MET 475 MODIFIED RESIDUE
SEQADV 1TXK MSE B 488 UNP P33136 MET 488 MODIFIED RESIDUE
SEQADV 1TXK VAL B 512 UNP P33136 EXPRESSION TAG
SEQADV 1TXK GLU B 513 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS B 514 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS B 515 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS B 516 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS B 517 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS B 518 UNP P33136 EXPRESSION TAG
SEQADV 1TXK HIS B 519 UNP P33136 EXPRESSION TAG
SEQRES 1 A 498 MET PHE SER ILE ASP ASP VAL ALA LYS GLN ALA GLN SER
SEQRES 2 A 498 LEU ALA GLY LYS GLY TYR GLU THR PRO LYS SER ASN LEU
SEQRES 3 A 498 PRO SER VAL PHE ARG ASP MSE LYS TYR ALA ASP TYR GLN
SEQRES 4 A 498 GLN ILE GLN PHE ASN HIS ASP LYS ALA TYR TRP ASN ASN
SEQRES 5 A 498 LEU LYS THR PRO PHE LYS LEU GLU PHE TYR HIS GLN GLY
SEQRES 6 A 498 MSE TYR PHE ASP THR PRO VAL LYS ILE ASN GLU VAL THR
SEQRES 7 A 498 ALA THR ALA VAL LYS ARG ILE LYS TYR SER PRO ASP TYR
SEQRES 8 A 498 PHE THR PHE GLY ASP VAL GLN HIS ASP LYS ASP THR VAL
SEQRES 9 A 498 LYS ASP LEU GLY PHE ALA GLY PHE LYS VAL LEU TYR PRO
SEQRES 10 A 498 ILE ASN SER LYS ASP LYS ASN ASP GLU ILE VAL SER MSE
SEQRES 11 A 498 LEU GLY ALA SER TYR PHE ARG VAL ILE GLY ALA GLY GLN
SEQRES 12 A 498 VAL TYR GLY LEU SER ALA ARG GLY LEU ALA ILE ASP THR
SEQRES 13 A 498 ALA LEU PRO SER GLY GLU GLU PHE PRO ARG PHE LYS GLU
SEQRES 14 A 498 PHE TRP ILE GLU ARG PRO LYS PRO THR ASP LYS ARG LEU
SEQRES 15 A 498 THR ILE TYR ALA LEU LEU ASP SER PRO ARG ALA THR GLY
SEQRES 16 A 498 ALA TYR LYS PHE VAL VAL MSE PRO GLY ARG ASP THR VAL
SEQRES 17 A 498 VAL ASP VAL GLN SER LYS ILE TYR LEU ARG ASP LYS VAL
SEQRES 18 A 498 GLY LYS LEU GLY VAL ALA PRO LEU THR SER MSE PHE LEU
SEQRES 19 A 498 PHE GLY PRO ASN GLN PRO SER PRO ALA ASN ASN TYR ARG
SEQRES 20 A 498 PRO GLU LEU HIS ASP SER ASN GLY LEU SER ILE HIS ALA
SEQRES 21 A 498 GLY ASN GLY GLU TRP ILE TRP ARG PRO LEU ASN ASN PRO
SEQRES 22 A 498 LYS HIS LEU ALA VAL SER SER PHE SER MSE GLU ASN PRO
SEQRES 23 A 498 GLN GLY PHE GLY LEU LEU GLN ARG GLY ARG ASP PHE SER
SEQRES 24 A 498 ARG PHE GLU ASP LEU ASP ASP ARG TYR ASP LEU ARG PRO
SEQRES 25 A 498 SER ALA TRP VAL THR PRO LYS GLY GLU TRP GLY LYS GLY
SEQRES 26 A 498 SER VAL GLU LEU VAL GLU ILE PRO THR ASN ASP GLU THR
SEQRES 27 A 498 ASN ASP ASN ILE VAL ALA TYR TRP THR PRO ASP GLN LEU
SEQRES 28 A 498 PRO GLU PRO GLY LYS GLU MSE ASN PHE LYS TYR THR ILE
SEQRES 29 A 498 THR PHE SER ARG ASP GLU ASP LYS LEU HIS ALA PRO ASP
SEQRES 30 A 498 ASN ALA TRP VAL GLN GLN THR ARG ARG SER THR GLY ASP
SEQRES 31 A 498 VAL LYS GLN SER ASN LEU ILE ARG GLN PRO ASP GLY THR
SEQRES 32 A 498 ILE ALA PHE VAL VAL ASP PHE THR GLY ALA GLU MSE LYS
SEQRES 33 A 498 LYS LEU PRO GLU ASP THR PRO VAL THR ALA GLN THR SER
SEQRES 34 A 498 ILE GLY ASP ASN GLY GLU ILE VAL GLU SER THR VAL ARG
SEQRES 35 A 498 TYR ASN PRO VAL THR LYS GLY TRP ARG LEU VAL MSE ARG
SEQRES 36 A 498 VAL LYS VAL LYS ASP ALA LYS LYS THR THR GLU MSE ARG
SEQRES 37 A 498 ALA ALA LEU VAL ASN ALA ASP GLN THR LEU SER GLU THR
SEQRES 38 A 498 TRP SER TYR GLN LEU PRO ALA ASN GLU VAL GLU HIS HIS
SEQRES 39 A 498 HIS HIS HIS HIS
SEQRES 1 B 498 MET PHE SER ILE ASP ASP VAL ALA LYS GLN ALA GLN SER
SEQRES 2 B 498 LEU ALA GLY LYS GLY TYR GLU THR PRO LYS SER ASN LEU
SEQRES 3 B 498 PRO SER VAL PHE ARG ASP MSE LYS TYR ALA ASP TYR GLN
SEQRES 4 B 498 GLN ILE GLN PHE ASN HIS ASP LYS ALA TYR TRP ASN ASN
SEQRES 5 B 498 LEU LYS THR PRO PHE LYS LEU GLU PHE TYR HIS GLN GLY
SEQRES 6 B 498 MSE TYR PHE ASP THR PRO VAL LYS ILE ASN GLU VAL THR
SEQRES 7 B 498 ALA THR ALA VAL LYS ARG ILE LYS TYR SER PRO ASP TYR
SEQRES 8 B 498 PHE THR PHE GLY ASP VAL GLN HIS ASP LYS ASP THR VAL
SEQRES 9 B 498 LYS ASP LEU GLY PHE ALA GLY PHE LYS VAL LEU TYR PRO
SEQRES 10 B 498 ILE ASN SER LYS ASP LYS ASN ASP GLU ILE VAL SER MSE
SEQRES 11 B 498 LEU GLY ALA SER TYR PHE ARG VAL ILE GLY ALA GLY GLN
SEQRES 12 B 498 VAL TYR GLY LEU SER ALA ARG GLY LEU ALA ILE ASP THR
SEQRES 13 B 498 ALA LEU PRO SER GLY GLU GLU PHE PRO ARG PHE LYS GLU
SEQRES 14 B 498 PHE TRP ILE GLU ARG PRO LYS PRO THR ASP LYS ARG LEU
SEQRES 15 B 498 THR ILE TYR ALA LEU LEU ASP SER PRO ARG ALA THR GLY
SEQRES 16 B 498 ALA TYR LYS PHE VAL VAL MSE PRO GLY ARG ASP THR VAL
SEQRES 17 B 498 VAL ASP VAL GLN SER LYS ILE TYR LEU ARG ASP LYS VAL
SEQRES 18 B 498 GLY LYS LEU GLY VAL ALA PRO LEU THR SER MSE PHE LEU
SEQRES 19 B 498 PHE GLY PRO ASN GLN PRO SER PRO ALA ASN ASN TYR ARG
SEQRES 20 B 498 PRO GLU LEU HIS ASP SER ASN GLY LEU SER ILE HIS ALA
SEQRES 21 B 498 GLY ASN GLY GLU TRP ILE TRP ARG PRO LEU ASN ASN PRO
SEQRES 22 B 498 LYS HIS LEU ALA VAL SER SER PHE SER MSE GLU ASN PRO
SEQRES 23 B 498 GLN GLY PHE GLY LEU LEU GLN ARG GLY ARG ASP PHE SER
SEQRES 24 B 498 ARG PHE GLU ASP LEU ASP ASP ARG TYR ASP LEU ARG PRO
SEQRES 25 B 498 SER ALA TRP VAL THR PRO LYS GLY GLU TRP GLY LYS GLY
SEQRES 26 B 498 SER VAL GLU LEU VAL GLU ILE PRO THR ASN ASP GLU THR
SEQRES 27 B 498 ASN ASP ASN ILE VAL ALA TYR TRP THR PRO ASP GLN LEU
SEQRES 28 B 498 PRO GLU PRO GLY LYS GLU MSE ASN PHE LYS TYR THR ILE
SEQRES 29 B 498 THR PHE SER ARG ASP GLU ASP LYS LEU HIS ALA PRO ASP
SEQRES 30 B 498 ASN ALA TRP VAL GLN GLN THR ARG ARG SER THR GLY ASP
SEQRES 31 B 498 VAL LYS GLN SER ASN LEU ILE ARG GLN PRO ASP GLY THR
SEQRES 32 B 498 ILE ALA PHE VAL VAL ASP PHE THR GLY ALA GLU MSE LYS
SEQRES 33 B 498 LYS LEU PRO GLU ASP THR PRO VAL THR ALA GLN THR SER
SEQRES 34 B 498 ILE GLY ASP ASN GLY GLU ILE VAL GLU SER THR VAL ARG
SEQRES 35 B 498 TYR ASN PRO VAL THR LYS GLY TRP ARG LEU VAL MSE ARG
SEQRES 36 B 498 VAL LYS VAL LYS ASP ALA LYS LYS THR THR GLU MSE ARG
SEQRES 37 B 498 ALA ALA LEU VAL ASN ALA ASP GLN THR LEU SER GLU THR
SEQRES 38 B 498 TRP SER TYR GLN LEU PRO ALA ASN GLU VAL GLU HIS HIS
SEQRES 39 B 498 HIS HIS HIS HIS
MODRES 1TXK MSE A 54 MET SELENOMETHIONINE
MODRES 1TXK MSE A 87 MET SELENOMETHIONINE
MODRES 1TXK MSE A 151 MET SELENOMETHIONINE
MODRES 1TXK MSE A 223 MET SELENOMETHIONINE
MODRES 1TXK MSE A 253 MET SELENOMETHIONINE
MODRES 1TXK MSE A 304 MET SELENOMETHIONINE
MODRES 1TXK MSE A 379 MET SELENOMETHIONINE
MODRES 1TXK MSE A 436 MET SELENOMETHIONINE
MODRES 1TXK MSE A 475 MET SELENOMETHIONINE
MODRES 1TXK MSE A 488 MET SELENOMETHIONINE
MODRES 1TXK MSE B 54 MET SELENOMETHIONINE
MODRES 1TXK MSE B 87 MET SELENOMETHIONINE
MODRES 1TXK MSE B 151 MET SELENOMETHIONINE
MODRES 1TXK MSE B 223 MET SELENOMETHIONINE
MODRES 1TXK MSE B 253 MET SELENOMETHIONINE
MODRES 1TXK MSE B 304 MET SELENOMETHIONINE
MODRES 1TXK MSE B 379 MET SELENOMETHIONINE
MODRES 1TXK MSE B 436 MET SELENOMETHIONINE
MODRES 1TXK MSE B 475 MET SELENOMETHIONINE
MODRES 1TXK MSE B 488 MET SELENOMETHIONINE
HET MSE A 54 8
HET MSE A 87 8
HET MSE A 151 8
HET MSE A 223 8
HET MSE A 253 8
HET MSE A 304 8
HET MSE A 379 8
HET MSE A 436 8
HET MSE A 475 8
HET MSE A 488 8
HET MSE B 54 8
HET MSE B 87 8
HET MSE B 151 8
HET MSE B 223 8
HET MSE B 253 8
HET MSE B 304 8
HET MSE B 379 8
HET MSE B 436 8
HET MSE B 475 8
HET MSE B 488 8
HET NA A 600 1
HETNAM MSE SELENOMETHIONINE
HETNAM NA SODIUM ION
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 NA NA 1+
FORMUL 4 HOH *477(H2 O)
HELIX 1 1 SER A 24 GLY A 37 1 14
HELIX 2 2 LYS A 55 GLN A 60 1 6
HELIX 3 3 HIS A 66 ALA A 69 5 4
HELIX 4 4 SER A 109 ASP A 111 5 3
HELIX 5 5 ASP A 318 PHE A 322 5 5
HELIX 6 6 ARG A 328 ARG A 332 5 5
HELIX 7 7 ASP A 390 HIS A 395 5 6
HELIX 8 8 GLU A 435 LEU A 439 5 5
HELIX 9 9 SER B 24 GLY B 37 1 14
HELIX 10 10 LYS B 55 GLN B 60 1 6
HELIX 11 11 HIS B 66 ALA B 69 5 4
HELIX 12 12 SER B 109 ASP B 111 5 3
HELIX 13 13 ASP B 318 PHE B 322 5 5
HELIX 14 14 ARG B 328 ARG B 332 5 5
HELIX 15 15 ASP B 390 HIS B 395 5 6
HELIX 16 16 GLU B 435 LEU B 439 5 5
SHEET 1 A 2 GLN A 63 PHE A 64 0
SHEET 2 A 2 PHE A 113 THR A 114 -1 O THR A 114 N GLN A 63
SHEET 1 B 7 LYS A 79 HIS A 84 0
SHEET 2 B 7 PHE A 130 TYR A 137 -1 O LEU A 136 N LYS A 79
SHEET 3 B 7 ASP A 146 LEU A 152 -1 O MSE A 151 N PHE A 133
SHEET 4 B 7 TYR A 156 VAL A 159 -1 O ARG A 158 N SER A 150
SHEET 5 B 7 SER A 169 ARG A 171 -1 O ALA A 170 N PHE A 157
SHEET 6 B 7 LEU A 245 SER A 252 -1 O THR A 251 N SER A 169
SHEET 7 B 7 ALA A 174 ILE A 175 -1 N ALA A 174 O GLY A 246
SHEET 1 C 9 LYS A 79 HIS A 84 0
SHEET 2 C 9 PHE A 130 TYR A 137 -1 O LEU A 136 N LYS A 79
SHEET 3 C 9 ASP A 146 LEU A 152 -1 O MSE A 151 N PHE A 133
SHEET 4 C 9 TYR A 156 VAL A 159 -1 O ARG A 158 N SER A 150
SHEET 5 C 9 SER A 169 ARG A 171 -1 O ALA A 170 N PHE A 157
SHEET 6 C 9 LEU A 245 SER A 252 -1 O THR A 251 N SER A 169
SHEET 7 C 9 ILE A 363 PRO A 369 -1 O TRP A 367 N VAL A 247
SHEET 8 C 9 LYS A 345 GLU A 352 -1 N GLU A 349 O TYR A 366
SHEET 9 C 9 ALA A 298 GLU A 305 -1 N ALA A 298 O GLU A 352
SHEET 1 D14 VAL A 103 ARG A 105 0
SHEET 2 D14 LYS A 94 VAL A 98 -1 N GLU A 97 O LYS A 104
SHEET 3 D14 ARG A 187 GLU A 194 1 O ILE A 193 N ASN A 96
SHEET 4 D14 LEU A 203 SER A 211 -1 O TYR A 206 N TRP A 192
SHEET 5 D14 ALA A 214 MSE A 223 -1 O PHE A 220 N ILE A 205
SHEET 6 D14 THR A 228 LEU A 238 -1 O VAL A 229 N MSE A 223
SHEET 7 D14 GLU A 378 SER A 388 -1 O TYR A 383 N VAL A 232
SHEET 8 D14 SER A 334 PRO A 339 -1 N SER A 334 O SER A 388
SHEET 9 D14 GLY A 309 LEU A 313 -1 N PHE A 310 O VAL A 337
SHEET 10 D14 GLY A 276 HIS A 280 -1 N HIS A 280 O GLY A 309
SHEET 11 D14 TRP A 286 PRO A 290 -1 O ILE A 287 N ILE A 279
SHEET 12 D14 THR A 498 LEU A 507 1 O THR A 502 N TRP A 286
SHEET 13 D14 THR A 486 VAL A 493 -1 N THR A 486 O LEU A 507
SHEET 14 D14 THR A 446 ILE A 451 -1 N THR A 446 O VAL A 493
SHEET 1 E 2 PHE A 254 PHE A 256 0
SHEET 2 E 2 LEU A 271 HIS A 272 -1 O LEU A 271 N LEU A 255
SHEET 1 F 4 TRP A 401 THR A 409 0
SHEET 2 F 4 THR A 424 THR A 432 -1 O ASP A 430 N GLN A 403
SHEET 3 F 4 GLY A 470 VAL A 479 -1 O VAL A 477 N ILE A 425
SHEET 4 F 4 GLY A 455 ASN A 465 -1 N ARG A 463 O ARG A 472
SHEET 1 G 2 GLN B 63 PHE B 64 0
SHEET 2 G 2 PHE B 113 THR B 114 -1 O THR B 114 N GLN B 63
SHEET 1 H 7 LYS B 79 HIS B 84 0
SHEET 2 H 7 PHE B 130 SER B 141 -1 O LEU B 136 N LYS B 79
SHEET 3 H 7 LYS B 144 LEU B 152 -1 O MSE B 151 N PHE B 133
SHEET 4 H 7 TYR B 156 VAL B 159 -1 O ARG B 158 N SER B 150
SHEET 5 H 7 SER B 169 ARG B 171 -1 O ALA B 170 N PHE B 157
SHEET 6 H 7 LEU B 245 SER B 252 -1 O THR B 251 N SER B 169
SHEET 7 H 7 ALA B 174 ILE B 175 -1 N ALA B 174 O GLY B 246
SHEET 1 I 9 LYS B 79 HIS B 84 0
SHEET 2 I 9 PHE B 130 SER B 141 -1 O LEU B 136 N LYS B 79
SHEET 3 I 9 LYS B 144 LEU B 152 -1 O MSE B 151 N PHE B 133
SHEET 4 I 9 TYR B 156 VAL B 159 -1 O ARG B 158 N SER B 150
SHEET 5 I 9 SER B 169 ARG B 171 -1 O ALA B 170 N PHE B 157
SHEET 6 I 9 LEU B 245 SER B 252 -1 O THR B 251 N SER B 169
SHEET 7 I 9 ILE B 363 PRO B 369 -1 O TRP B 367 N VAL B 247
SHEET 8 I 9 LYS B 345 GLU B 352 -1 N VAL B 351 O VAL B 364
SHEET 9 I 9 ALA B 298 GLU B 305 -1 N MSE B 304 O GLY B 346
SHEET 1 J14 VAL B 103 ARG B 105 0
SHEET 2 J14 LYS B 94 VAL B 98 -1 N GLU B 97 O LYS B 104
SHEET 3 J14 ARG B 187 GLU B 194 1 O PHE B 191 N LYS B 94
SHEET 4 J14 LEU B 203 SER B 211 -1 O TYR B 206 N TRP B 192
SHEET 5 J14 ALA B 214 MSE B 223 -1 O PHE B 220 N ILE B 205
SHEET 6 J14 THR B 228 LEU B 238 -1 O VAL B 229 N MSE B 223
SHEET 7 J14 GLU B 378 SER B 388 -1 O TYR B 383 N VAL B 232
SHEET 8 J14 SER B 334 PRO B 339 -1 N SER B 334 O SER B 388
SHEET 9 J14 GLY B 309 LEU B 313 -1 N PHE B 310 O VAL B 337
SHEET 10 J14 GLY B 276 HIS B 280 -1 N HIS B 280 O GLY B 309
SHEET 11 J14 TRP B 286 PRO B 290 -1 O ILE B 287 N ILE B 279
SHEET 12 J14 THR B 502 LEU B 507 1 O THR B 502 N TRP B 286
SHEET 13 J14 THR B 486 ASN B 494 -1 N ALA B 490 O TRP B 503
SHEET 14 J14 THR B 446 ILE B 451 -1 N THR B 446 O VAL B 493
SHEET 1 K14 VAL B 103 ARG B 105 0
SHEET 2 K14 LYS B 94 VAL B 98 -1 N GLU B 97 O LYS B 104
SHEET 3 K14 ARG B 187 GLU B 194 1 O PHE B 191 N LYS B 94
SHEET 4 K14 LEU B 203 SER B 211 -1 O TYR B 206 N TRP B 192
SHEET 5 K14 ALA B 214 MSE B 223 -1 O PHE B 220 N ILE B 205
SHEET 6 K14 THR B 228 LEU B 238 -1 O VAL B 229 N MSE B 223
SHEET 7 K14 GLU B 378 SER B 388 -1 O TYR B 383 N VAL B 232
SHEET 8 K14 SER B 334 PRO B 339 -1 N SER B 334 O SER B 388
SHEET 9 K14 GLY B 309 LEU B 313 -1 N PHE B 310 O VAL B 337
SHEET 10 K14 GLY B 276 HIS B 280 -1 N HIS B 280 O GLY B 309
SHEET 11 K14 TRP B 286 PRO B 290 -1 O ILE B 287 N ILE B 279
SHEET 12 K14 THR B 502 LEU B 507 1 O THR B 502 N TRP B 286
SHEET 13 K14 THR B 486 ASN B 494 -1 N ALA B 490 O TRP B 503
SHEET 14 K14 GLN B 497 THR B 498 -1 O GLN B 497 N ASN B 494
SHEET 1 L 2 PHE B 254 PHE B 256 0
SHEET 2 L 2 LEU B 271 HIS B 272 -1 O LEU B 271 N PHE B 256
SHEET 1 M 4 TRP B 401 SER B 408 0
SHEET 2 M 4 THR B 424 THR B 432 -1 O VAL B 428 N ARG B 406
SHEET 3 M 4 GLY B 470 VAL B 479 -1 O LEU B 473 N VAL B 429
SHEET 4 M 4 GLY B 455 ASN B 465 -1 N ARG B 463 O ARG B 472
LINK C MSE A 54 N LYS A 55 1555 1555 1.33
LINK C GLY A 86 N MSE A 87 1555 1555 1.33
LINK C MSE A 87 N TYR A 88 1555 1555 1.33
LINK C SER A 150 N MSE A 151 1555 1555 1.32
LINK C MSE A 151 N LEU A 152 1555 1555 1.33
LINK C VAL A 222 N MSE A 223 1555 1555 1.33
LINK C MSE A 223 N PRO A 224 1555 1555 1.34
LINK C SER A 252 N MSE A 253 1555 1555 1.33
LINK C MSE A 253 N PHE A 254 1555 1555 1.33
LINK C SER A 303 N MSE A 304 1555 1555 1.32
LINK C MSE A 304 N GLU A 305 1555 1555 1.32
LINK C GLU A 378 N MSE A 379 1555 1555 1.33
LINK C MSE A 379 N ASN A 380 1555 1555 1.33
LINK C GLU A 435 N MSE A 436 1555 1555 1.33
LINK C MSE A 436 N LYS A 437 1555 1555 1.33
LINK C VAL A 474 N MSE A 475 1555 1555 1.32
LINK C MSE A 475 N ARG A 476 1555 1555 1.32
LINK C GLU A 487 N MSE A 488 1555 1555 1.33
LINK C MSE A 488 N ARG A 489 1555 1555 1.33
LINK NA NA A 600 OG SER A 320 1555 1555 2.47
LINK NA NA A 600 OG SER B 320 1555 1555 2.43
LINK C MSE B 54 N LYS B 55 1555 1555 1.33
LINK C GLY B 86 N MSE B 87 1555 1555 1.33
LINK C MSE B 87 N TYR B 88 1555 1555 1.33
LINK C SER B 150 N MSE B 151 1555 1555 1.33
LINK C MSE B 151 N LEU B 152 1555 1555 1.33
LINK C VAL B 222 N MSE B 223 1555 1555 1.33
LINK C MSE B 223 N PRO B 224 1555 1555 1.34
LINK C SER B 252 N MSE B 253 1555 1555 1.33
LINK C MSE B 253 N PHE B 254 1555 1555 1.33
LINK C SER B 303 N MSE B 304 1555 1555 1.32
LINK C MSE B 304 N GLU B 305 1555 1555 1.33
LINK C GLU B 378 N MSE B 379 1555 1555 1.33
LINK C MSE B 379 N ASN B 380 1555 1555 1.33
LINK C GLU B 435 N MSE B 436 1555 1555 1.33
LINK C MSE B 436 N LYS B 437 1555 1555 1.33
LINK C VAL B 474 N MSE B 475 1555 1555 1.32
LINK C MSE B 475 N ARG B 476 1555 1555 1.33
LINK C GLU B 487 N MSE B 488 1555 1555 1.33
LINK C MSE B 488 N ARG B 489 1555 1555 1.33
LINK NA NA A 600 O HOH A 840 1555 1555 2.85
LINK NA NA A 600 O HOH A 839 1555 1555 2.99
SITE 1 AC1 5 SER A 320 HOH A 839 HOH A 840 HOH A 843
SITE 2 AC1 5 SER B 320
CRYST1 63.860 88.120 215.650 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 0.015659 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004637 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
