HEADER TRANSLATION FACTOR/ANTIBIOTIC 04-OCT-11 3U2Q
TITLE EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LFF571
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TU 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EF-TU 1, P-43;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NVP-LFF571;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: TUFA, B3339, JW3301;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES
KEYWDS TRANSLATION FACTOR-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.PALESTRANT
REVDAT 1 02-MAY-12 3U2Q 0
JRNL AUTH M.J.LAMARCHE,J.A.LEEDS,A.AMARAL,J.T.BREWER,S.M.BUSHELL,
JRNL AUTH 2 G.DENG,J.M.DEWHURST,J.DING,J.DZINK-FOX,G.GAMBER,A.JAIN,
JRNL AUTH 3 K.LEE,L.LEE,T.LISTER,D.MCKENNEY,S.MULLIN,C.OSBORNE,
JRNL AUTH 4 D.PALESTRANT,M.A.PATANE,E.M.RANN,M.SACHDEVA,J.SHAO,
JRNL AUTH 5 S.TIAMFOOK,A.TRZASKO,L.WHITEHEAD,A.YIFRU,D.YU,W.YAN,Q.ZHU
JRNL TITL DISCOVERY OF LFF571: AN INVESTIGATIONAL AGENT FOR
JRNL TITL 2 CLOSTRIDIUM DIFFICILE INFECTION.
JRNL REF J.MED.CHEM. V. 55 2376 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22315981
JRNL DOI 10.1021/JM201685H
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 11365
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.315
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 582
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 11365
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3058
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 89
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
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) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3U2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB068231.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.23
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11365
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.790
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: PDB ENTRY 1D8T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS PH8, 50MM NACL , PH 8.23,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 41.65150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.23650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.65150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.23650
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 443 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 ALA A 1
REMARK 465 LYS A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 PHE A 5
REMARK 465 ARG A 58
REMARK 465 GLY A 59
REMARK 465 ILE A 60
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 ARG A 7 -78.77 115.10
REMARK 500 PRO A 10 128.08 -36.88
REMARK 500 ASP A 21 39.67 35.36
REMARK 500 THR A 33 -81.43 -62.45
REMARK 500 LYS A 37 -79.03 -59.15
REMARK 500 PHE A 46 -74.47 -36.37
REMARK 500 ALA A 52 74.13 -117.30
REMARK 500 PRO A 53 -135.67 -72.14
REMARK 500 GLU A 54 -161.23 -20.21
REMARK 500 GLU A 55 -171.49 164.03
REMARK 500 LYS A 56 -103.24 177.77
REMARK 500 PRO A 111 109.96 -52.02
REMARK 500 VAL A 127 109.15 -46.93
REMARK 500 LEU A 134 99.13 -62.91
REMARK 500 CYS A 137 2.45 -68.50
REMARK 500 LEU A 146 3.73 -63.31
REMARK 500 PRO A 163 68.69 -59.03
REMARK 500 SER A 173 99.12 -160.58
REMARK 500 ALA A 174 1.22 -58.10
REMARK 500 LEU A 175 -62.22 -103.14
REMARK 500 ASP A 181 76.57 -63.16
REMARK 500 ALA A 182 -37.81 -35.62
REMARK 500 ALA A 205 -48.01 -21.44
REMARK 500 GLU A 215 -68.01 -106.64
REMARK 500 SER A 221 -62.95 -16.47
REMARK 500 ILE A 247 -58.03 58.78
REMARK 500 SER A 253 150.30 175.14
REMARK 500 ARG A 262 -7.42 86.64
REMARK 500 ALA A 270 130.86 -35.77
REMARK 500 PRO A 328 -166.88 -100.81
REMARK 500 ARG A 333 -71.33 51.53
REMARK 500 LYS A 390 116.53 -168.14
REMARK 500 MEN B 3 -167.62 -118.89
REMARK 500 VAL B 5 -50.94 -145.51
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 433 O
REMARK 620 2 THR A 25 OG1 144.9
REMARK 620 3 GDP A 501 O2B 111.9 85.9
REMARK 620 4 HOH A 405 O 86.8 58.7 124.7
REMARK 620 5 GDP A 501 O2A 114.9 95.8 85.6 134.3
REMARK 620 6 GDP A 501 O1B 58.9 142.6 57.5 135.0 89.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF NVP-LFF571
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U6K RELATED DB: PDB
REMARK 900 EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LDK733
REMARK 900 RELATED ID: 3U6B RELATED DB: PDB
REMARK 900 EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LDI028
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE GE2270A-LIKE ANTIBIOTIC COMPOUND IS REPRESENTED AS POLYMER. THE
REMARK 999 FIRST 11 RESIDUES OF THE ANTIBIOTIC ARE IDENTICAL TO THE
REMARK 999 CORRESPONDING RESIDUES IN GE2270A, WITH ONLY THE LAST RESIDUE
REMARK 999 MODIFIED.
DBREF 3U2Q A 2 393 UNP P0CE47 EFTU1_ECOLI 3 394
DBREF 3U2Q B 1 12 UNP Q7M0J8 THCL_PLARO 1 12
SEQADV 3U2Q MET A 0 UNP P0CE47 EXPRESSION TAG
SEQADV 3U2Q ALA A 1 UNP P0CE47 EXPRESSION TAG
SEQADV 3U2Q 7BB B 12 UNP Q7M0J8 CYS 12 SEE REMARK 999
SEQRES 1 A 394 MET ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL
SEQRES 2 A 394 ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR
SEQRES 3 A 394 THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR
SEQRES 4 A 394 TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN
SEQRES 5 A 394 ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR
SEQRES 6 A 394 SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA
SEQRES 7 A 394 HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN
SEQRES 8 A 394 MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU
SEQRES 9 A 394 VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG
SEQRES 10 A 394 GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR
SEQRES 11 A 394 ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP
SEQRES 12 A 394 GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU
SEQRES 13 A 394 LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO
SEQRES 14 A 394 ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP
SEQRES 15 A 394 ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE
SEQRES 16 A 394 LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP
SEQRES 17 A 394 LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE
SEQRES 18 A 394 SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG
SEQRES 19 A 394 GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY
SEQRES 20 A 394 ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU
SEQRES 21 A 394 MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU
SEQRES 22 A 394 ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU
SEQRES 23 A 394 ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE
SEQRES 24 A 394 LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU
SEQRES 25 A 394 SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS
SEQRES 26 A 394 GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL
SEQRES 27 A 394 THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL
SEQRES 28 A 394 MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE
SEQRES 29 A 394 HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE
SEQRES 30 A 394 ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA
SEQRES 31 A 394 LYS VAL LEU GLY
SEQRES 1 B 12 SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 7BB
MODRES 3U2Q BB9 B 2 CYS
MODRES 3U2Q MEN B 3 ASN N-METHYL ASPARAGINE
MODRES 3U2Q BB6 B 4 CYS (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID
MODRES 3U2Q BB7 B 6 CYS
MODRES 3U2Q BB8 B 8 PHE (2S,3S)-BETA-HYDROXY-PHENYLALANINE
MODRES 3U2Q BB9 B 9 CYS
MODRES 3U2Q BB9 B 10 CYS
MODRES 3U2Q MH6 B 11 SER 3-HYDROXY-2-IMINOPROPANOIC ACID
HET BB9 B 2 6
HET MEN B 3 8
HET BB6 B 4 7
HET BB7 B 6 9
HET BB8 B 8 11
HET BB9 B 9 5
HET BB9 B 10 5
HET MH6 B 11 4
HET 7BB B 12 24
HET GDP A 501 28
HET MG A 503 1
HETNAM BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID
HETNAM MEN N-METHYL ASPARAGINE
HETNAM BB6 (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID
HETNAM BB7 (2Z)-2-AMINO-4-METHOXY-3-SULFANYLBUT-2-ENOIC ACID
HETNAM BB8 (2S,3S)-BETA-HYDROXY-PHENYLALANINE
HETNAM MH6 3-HYDROXY-2-IMINOPROPANOIC ACID
HETNAM 7BB TRANS-4-({[(E)-1-AMINO-2-SULFANYLETHENYL](4-
HETNAM 2 7BB CARBOXYBUTYL)CARBAMOYL}OXY)CYCLOHEXANECARBOXYLIC ACID
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN BB8 BETA-HYDROXY-PHENYLALANINE, THREO-BETA-HYDROXY-L-
HETSYN 2 BB8 PHENYLALANINE, (BETAS)-BETA-HYDROXY-L-PHENYLALANINE,
HETSYN 3 BB8 L-THREO-3-PHENYLSERINE, L-THREO-BETA-PHENYLSERINE, 3-
HETSYN 4 BB8 HYDROXY-L-PHENYLALANINE
FORMUL 2 BB9 3(C3 H5 N O2 S)
FORMUL 2 MEN C5 H10 N2 O3
FORMUL 2 BB6 C4 H7 N O2 S
FORMUL 2 BB7 C5 H9 N O3 S
FORMUL 2 BB8 C9 H11 N O3
FORMUL 2 MH6 C3 H5 N O3
FORMUL 2 7BB C15 H24 N2 O6 S
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 MG MG 2+
FORMUL 5 HOH *89(H2 O)
HELIX 1 1 GLY A 23 GLY A 40 1 18
HELIX 2 2 ALA A 45 ILE A 49 5 5
HELIX 3 3 GLY A 83 GLY A 94 1 12
HELIX 4 4 MET A 112 GLY A 126 1 15
HELIX 5 5 GLU A 147 TYR A 160 1 14
HELIX 6 6 LEU A 175 GLY A 180 1 6
HELIX 7 7 ASP A 181 ILE A 199 1 19
HELIX 8 8 ARG A 204 LYS A 208 5 5
HELIX 9 9 LYS A 282 ILE A 286 5 5
HELIX 10 10 SER A 312 GLY A 316 5 5
SHEET 1 A 6 SER A 65 THR A 71 0
SHEET 2 A 6 ARG A 74 ASP A 80 -1 O TYR A 76 N TYR A 69
SHEET 3 A 6 HIS A 11 ILE A 17 1 N VAL A 14 O ALA A 77
SHEET 4 A 6 ALA A 101 ALA A 106 1 O VAL A 104 N ILE A 17
SHEET 5 A 6 ILE A 130 ASN A 135 1 O ILE A 131 N ALA A 101
SHEET 6 A 6 ILE A 169 ARG A 171 1 O VAL A 170 N VAL A 132
SHEET 1 B 7 LEU A 211 PRO A 213 0
SHEET 2 B 7 VAL A 291 ALA A 293 -1 O LEU A 292 N LEU A 212
SHEET 3 B 7 GLU A 241 VAL A 245 -1 N GLU A 243 O ALA A 293
SHEET 4 B 7 GLN A 251 MET A 260 -1 O SER A 253 N VAL A 242
SHEET 5 B 7 ASN A 273 ARG A 279 -1 O LEU A 277 N THR A 256
SHEET 6 B 7 GLY A 224 ARG A 230 -1 N THR A 225 O LEU A 278
SHEET 7 B 7 VAL A 217 ILE A 220 -1 N ILE A 220 O GLY A 224
SHEET 1 C 5 LEU A 211 PRO A 213 0
SHEET 2 C 5 VAL A 291 ALA A 293 -1 O LEU A 292 N LEU A 212
SHEET 3 C 5 GLU A 241 VAL A 245 -1 N GLU A 243 O ALA A 293
SHEET 4 C 5 GLN A 251 MET A 260 -1 O SER A 253 N VAL A 242
SHEET 5 C 5 LYS A 263 LEU A 265 -1 O LEU A 265 N VAL A 258
SHEET 1 D 2 ILE A 235 LYS A 237 0
SHEET 2 D 2 GLU A 267 ARG A 269 -1 O GLY A 268 N ILE A 236
SHEET 1 E 7 LYS A 299 ILE A 310 0
SHEET 2 E 7 ASN A 355 MET A 368 -1 O MET A 358 N SER A 306
SHEET 3 E 7 THR A 335 GLU A 342 -1 N THR A 338 O ILE A 363
SHEET 4 E 7 GLN A 329 PHE A 332 -1 N PHE A 330 O VAL A 337
SHEET 5 E 7 ARG A 373 GLU A 378 -1 O ALA A 375 N TYR A 331
SHEET 6 E 7 ARG A 381 VAL A 391 -1 O GLY A 384 N ILE A 376
SHEET 7 E 7 LYS A 299 ILE A 310 -1 N TYR A 309 O ALA A 385
SHEET 1 F 2 PHE A 322 PHE A 323 0
SHEET 2 F 2 MET A 349 VAL A 350 -1 O VAL A 350 N PHE A 322
LINK C SER B 1 N BB9 B 2 1555 1555 1.33
LINK C BB9 B 2 N MEN B 3 1555 1555 1.32
LINK C BB6 B 4 N VAL B 5 1555 1555 1.38
LINK C BB7 B 6 N GLY B 7 1555 1555 1.34
LINK C BB8 B 8 N BB9 B 9 1555 1555 1.31
LINK C BB9 B 9 N BB9 B 10 1555 1555 1.32
LINK C BB9 B 10 N MH6 B 11 1555 1555 1.33
LINK MG MG A 503 O HOH A 433 1555 1555 2.43
LINK OG1 THR A 25 MG MG A 503 1555 1555 2.49
LINK O2B GDP A 501 MG MG A 503 1555 1555 2.51
LINK MG MG A 503 O HOH A 405 1555 1555 2.57
LINK O2A GDP A 501 MG MG A 503 1555 1555 2.71
LINK O1B GDP A 501 MG MG A 503 1555 1555 2.72
LINK CB SER B 1 CB MH6 B 11 1555 1555 1.43
LINK CA SER B 1 C BB9 B 10 1555 1555 1.44
LINK C SER B 1 SG BB9 B 2 1555 1555 1.72
LINK C BB9 B 9 SG BB9 B 10 1555 1555 1.74
LINK C MEN B 3 SG BB6 B 4 1555 1555 1.74
LINK C MH6 B 11 SG 7BB B 12 1555 1555 1.76
LINK C BB8 B 8 SG BB9 B 9 1555 1555 1.78
LINK C VAL B 5 SG BB7 B 6 1555 1555 1.79
LINK C MH6 B 11 N 7BB B 12 1555 1555 1.31
SITE 1 AC1 18 HIS A 19 VAL A 20 ASP A 21 HIS A 22
SITE 2 AC1 18 GLY A 23 LYS A 24 THR A 25 THR A 26
SITE 3 AC1 18 PHE A 46 ASP A 50 ASN A 135 LYS A 136
SITE 4 AC1 18 ASP A 138 MET A 139 SER A 173 LEU A 175
SITE 5 AC1 18 HOH A 433 MG A 503
SITE 1 AC2 5 THR A 25 ASP A 50 HOH A 405 HOH A 433
SITE 2 AC2 5 GDP A 501
SITE 1 AC3 25 THR A 38 TYR A 39 PRO A 72 GLU A 215
SITE 2 AC3 25 ASP A 216 PHE A 218 THR A 228 THR A 256
SITE 3 AC3 25 GLY A 257 GLU A 259 PHE A 261 ARG A 262
SITE 4 AC3 25 ASN A 273 VAL A 274 GLY A 275 LEU A 277
SITE 5 AC3 25 LYS A 303 HIS A 319 THR A 320 PRO A 321
SITE 6 AC3 25 PHE A 323 HOH A 407 HOH B 13 HOH B 18
SITE 7 AC3 25 HOH B 87
CRYST1 83.303 132.473 37.433 90.00 90.00 90.00 P 21 21 2 4
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 0.012004 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007549 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026714 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
