HEADER TRANSLATION FACTOR/ANTIBIOTIC 12-OCT-11 3U6B
TITLE EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LDI028
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TU 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: EF-TU 1, P-43;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: THIOCILLIN GE2270 ANALOGUE NVP-LDI028;
COMPND 8 CHAIN: C, D;
COMPND 9 SYNONYM: EF-TU 1, P-43 ,EF-TU;
COMPND 10 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 EXPRESSION_SYSTEM_STRAIN: BL21 (STAR);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS TRANSLATION FACTOR-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.PALESTRANT
REVDAT 2 18-APR-12 3U6B 1 COMPND
REVDAT 1 08-FEB-12 3U6B 0
JRNL AUTH M.J.LAMARCHE,J.A.LEEDS,K.AMARAL,J.T.BREWER,S.M.BUSHELL,
JRNL AUTH 2 J.M.DEWHURST,J.DZINK-FOX,E.GANGL,J.GOLDOVITZ,A.JAIN,
JRNL AUTH 3 S.MULLIN,G.NECKERMANN,C.OSBORNE,D.PALESTRANT,M.A.PATANE,
JRNL AUTH 4 E.M.RANN,M.SACHDEVA,J.SHAO,S.TIAMFOOK,L.WHITEHEAD,D.YU
JRNL TITL ANTIBACTERIAL OPTIMIZATION OF 4-AMINOTHIAZOLYL ANALOGUES OF
JRNL TITL 2 THE NATURAL PRODUCT GE2270 A: IDENTIFICATION OF THE
JRNL TITL 3 CYCLOALKYLCARBOXYLIC ACIDS.
JRNL REF J.MED.CHEM. V. 54 8099 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21999529
JRNL DOI 10.1021/JM200938F
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 37531
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1861
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 19
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.85
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2543
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2379
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2458
REMARK 3 BIN R VALUE (WORKING SET) : 0.2356
REMARK 3 BIN FREE R VALUE : 0.3036
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.34
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 85
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 : 5875
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.44850
REMARK 3 B22 (A**2) : -1.55720
REMARK 3 B33 (A**2) : 3.00570
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) : 0.29
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6056 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8231 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2046 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 137 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 915 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6056 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.25
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3U6B 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 RCSB068360.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
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 : NULL
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 : 39701
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
REMARK 200 R SYM FOR SHELL (I) : 0.25700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.030
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 (%): 42.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 22% PEG 3350,
REMARK 280 0.1M BIS-TRIS PH6.5 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 78.24150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.24150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 48.62300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.18800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 48.62300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.18800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.24150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 48.62300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.18800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.24150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 48.62300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.18800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 B 524 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 ALA A 42
REMARK 465 ALA A 43
REMARK 465 ARG A 44
REMARK 465 ALA A 45
REMARK 465 PHE A 46
REMARK 465 ASP A 47
REMARK 465 GLN A 48
REMARK 465 ILE A 49
REMARK 465 ASP A 50
REMARK 465 ASN A 51
REMARK 465 ALA A 52
REMARK 465 PRO A 53
REMARK 465 GLU A 54
REMARK 465 GLU A 55
REMARK 465 LYS A 56
REMARK 465 ALA A 57
REMARK 465 SER A 221
REMARK 465 GLY A 222
REMARK 465 ARG A 223
REMARK 465 GLY A 224
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 ARG B 44
REMARK 465 ALA B 45
REMARK 465 PHE B 46
REMARK 465 ASP B 47
REMARK 465 GLN B 48
REMARK 465 ILE B 49
REMARK 465 ASP B 50
REMARK 465 ASN B 51
REMARK 465 ALA B 52
REMARK 465 PRO B 53
REMARK 465 GLU B 54
REMARK 465 GLU B 55
REMARK 465 SER B 221
REMARK 465 GLY B 222
REMARK 465 ARG B 223
REMARK 465 GLY B 224
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER C 1 CA SER C 1 CB -0.118
REMARK 500 SER D 1 CA SER D 1 CB -0.134
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 ALA A 96 74.83 -100.39
REMARK 500 ASP A 141 38.03 -96.04
REMARK 500 ILE A 247 -67.95 55.44
REMARK 500 ARG A 262 -11.67 73.79
REMARK 500 ARG A 283 -39.11 -38.41
REMARK 500 ARG A 327 73.48 -116.67
REMARK 500 ARG A 333 -70.81 58.71
REMARK 500 ARG B 7 77.05 -64.56
REMARK 500 THR B 8 13.97 -156.76
REMARK 500 ASP B 21 -0.21 71.06
REMARK 500 ARG B 58 -33.53 84.66
REMARK 500 ASP B 141 69.36 -114.41
REMARK 500 ASP B 161 -1.92 78.16
REMARK 500 GLU B 215 -68.89 -96.13
REMARK 500 ILE B 247 -65.19 57.86
REMARK 500 ARG B 262 -5.49 82.95
REMARK 500 ALA B 270 130.55 -38.54
REMARK 500 PHE B 323 -165.09 -114.42
REMARK 500 ARG B 333 -65.34 63.66
REMARK 500 MEN D 3 -167.14 -100.31
REMARK 500 VAL D 5 -24.11 -171.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 377 24.2 L L OUTSIDE RANGE
REMARK 500 ARG B 58 23.0 L L OUTSIDE RANGE
REMARK 500 MET B 358 24.6 L L OUTSIDE RANGE
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 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP A 402 O2B
REMARK 620 2 HOH A 514 O 91.2
REMARK 620 3 HOH A 503 O 102.8 165.7
REMARK 620 4 THR A 25 OG1 95.4 80.8 94.5
REMARK 620 5 HOH A 517 O 95.3 89.4 92.5 165.6
REMARK 620 6 HOH A 531 O 167.7 78.0 87.8 77.3 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 25 OG1
REMARK 620 2 HOH B 512 O 87.8
REMARK 620 3 HOH B 505 O 91.8 172.4
REMARK 620 4 GDP B 401 O2B 93.1 93.9 93.6
REMARK 620 5 HOH B 516 O 90.0 77.5 95.0 170.8
REMARK 620 6 HOH B 514 O 177.0 91.7 88.4 89.9 87.0
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 MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF NVP-LDI028
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF NVP-LDI028
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: 3U2Q RELATED DB: PDB
REMARK 900 EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH NVP-LFF571
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 3U6B A 2 393 UNP P0CE47 EFTU1_ECOLI 3 394
DBREF 3U6B B 2 393 UNP P0CE47 EFTU1_ECOLI 3 394
DBREF 3U6B C 1 12 UNP Q7M0J8 THCL_PLARO 1 12
DBREF 3U6B D 1 12 UNP Q7M0J8 THCL_PLARO 1 12
SEQADV 3U6B MET A 0 UNP P0CE47 EXPRESSION TAG
SEQADV 3U6B ALA A 1 UNP P0CE47 EXPRESSION TAG
SEQADV 3U6B MET B 0 UNP P0CE47 EXPRESSION TAG
SEQADV 3U6B ALA B 1 UNP P0CE47 EXPRESSION TAG
SEQADV 3U6B 8BB C 12 UNP Q7M0J8 CYS 12 SEE REMARK 999
SEQADV 3U6B 8BB D 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 394 MET ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL
SEQRES 2 B 394 ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR
SEQRES 3 B 394 THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR
SEQRES 4 B 394 TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN
SEQRES 5 B 394 ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR
SEQRES 6 B 394 SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA
SEQRES 7 B 394 HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN
SEQRES 8 B 394 MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU
SEQRES 9 B 394 VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG
SEQRES 10 B 394 GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR
SEQRES 11 B 394 ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP
SEQRES 12 B 394 GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU
SEQRES 13 B 394 LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO
SEQRES 14 B 394 ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP
SEQRES 15 B 394 ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE
SEQRES 16 B 394 LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP
SEQRES 17 B 394 LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE
SEQRES 18 B 394 SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG
SEQRES 19 B 394 GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY
SEQRES 20 B 394 ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU
SEQRES 21 B 394 MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU
SEQRES 22 B 394 ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU
SEQRES 23 B 394 ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE
SEQRES 24 B 394 LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU
SEQRES 25 B 394 SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS
SEQRES 26 B 394 GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL
SEQRES 27 B 394 THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL
SEQRES 28 B 394 MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE
SEQRES 29 B 394 HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE
SEQRES 30 B 394 ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA
SEQRES 31 B 394 LYS VAL LEU GLY
SEQRES 1 C 12 SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 8BB
SEQRES 1 D 12 SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 8BB
MODRES 3U6B BB9 C 2 CYS
MODRES 3U6B MEN C 3 ASN N-METHYL ASPARAGINE
MODRES 3U6B BB6 C 4 CYS (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID
MODRES 3U6B BB7 C 6 CYS
MODRES 3U6B BB8 C 8 PHE (2S,3S)-BETA-HYDROXY-PHENYLALANINE
MODRES 3U6B BB9 C 9 CYS
MODRES 3U6B BB9 C 10 CYS
MODRES 3U6B MH6 C 11 SER 3-HYDROXY-2-IMINOPROPANOIC ACID
MODRES 3U6B BB9 D 2 CYS
MODRES 3U6B MEN D 3 ASN N-METHYL ASPARAGINE
MODRES 3U6B BB6 D 4 CYS (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID
MODRES 3U6B BB7 D 6 CYS
MODRES 3U6B BB8 D 8 PHE (2S,3S)-BETA-HYDROXY-PHENYLALANINE
MODRES 3U6B BB9 D 9 CYS
MODRES 3U6B BB9 D 10 CYS
MODRES 3U6B MH6 D 11 SER 3-HYDROXY-2-IMINOPROPANOIC ACID
HET BB9 C 2 6
HET MEN C 3 8
HET BB6 C 4 7
HET BB7 C 6 9
HET BB8 C 8 11
HET BB9 C 9 5
HET BB9 C 10 5
HET MH6 C 11 4
HET 8BB C 12 16
HET BB9 D 2 6
HET MEN D 3 8
HET BB6 D 4 7
HET BB7 D 6 9
HET BB8 D 8 11
HET BB9 D 9 5
HET BB9 D 10 5
HET MH6 D 11 4
HET 8BB D 12 16
HET MG A 401 1
HET GDP A 402 28
HET GDP B 401 28
HET MG B 402 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 8BB TRANS-4-{[(E)-1-AMINO-2-
HETNAM 2 8BB SULFANYLETHENYL]CARBAMOYL}CYCLOHEXANECARBOXYLIC ACID
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
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 3 BB9 6(C3 H5 N O2 S)
FORMUL 3 MEN 2(C5 H10 N2 O3)
FORMUL 3 BB6 2(C4 H7 N O2 S)
FORMUL 3 BB7 2(C5 H9 N O3 S)
FORMUL 3 BB8 2(C9 H11 N O3)
FORMUL 3 MH6 2(C3 H5 N O3)
FORMUL 3 8BB 2(C10 H16 N2 O3 S)
FORMUL 5 MG 2(MG 2+)
FORMUL 6 GDP 2(C10 H15 N5 O11 P2)
FORMUL 9 HOH *111(H2 O)
HELIX 1 1 GLY A 23 TYR A 39 1 17
HELIX 2 2 GLY A 83 GLY A 94 1 12
HELIX 3 3 MET A 112 GLY A 126 1 15
HELIX 4 4 ASP A 142 TYR A 160 1 19
HELIX 5 5 PRO A 163 THR A 167 5 5
HELIX 6 6 SER A 173 GLU A 179 1 7
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
HELIX 11 11 GLU B 3 ARG B 7 1 5
HELIX 12 12 GLY B 23 GLY B 40 1 18
HELIX 13 13 GLY B 83 GLY B 94 1 12
HELIX 14 14 MET B 112 VAL B 125 1 14
HELIX 15 15 ASP B 142 TYR B 160 1 19
HELIX 16 16 PRO B 163 THR B 167 5 5
HELIX 17 17 SER B 173 GLU B 179 1 7
HELIX 18 18 ASP B 181 ILE B 199 1 19
HELIX 19 19 ARG B 204 LYS B 208 5 5
HELIX 20 20 LYS B 282 ILE B 286 5 5
HELIX 21 21 SER B 312 GLY B 316 5 5
SHEET 1 A 6 SER A 65 ASP A 70 0
SHEET 2 A 6 HIS A 75 ASP A 80 -1 O HIS A 78 N VAL A 67
SHEET 3 A 6 HIS A 11 ILE A 17 1 N VAL A 14 O ALA A 77
SHEET 4 A 6 GLY A 100 ALA A 106 1 O ILE A 102 N GLY A 15
SHEET 5 A 6 ILE A 130 ASN A 135 1 O ASN A 135 N VAL A 105
SHEET 6 A 6 ILE A 169 ARG A 171 1 O VAL A 170 N LEU A 134
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 LEU A 278 -1 O LEU A 277 N THR A 256
SHEET 6 B 7 VAL A 226 ARG A 230 -1 N VAL A 227 O VAL A 276
SHEET 7 B 7 VAL A 217 PHE A 218 -1 N PHE A 218 O VAL A 226
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 LEU A 362 N THR A 302
SHEET 3 E 7 THR A 335 GLU A 342 -1 N THR A 340 O THR A 361
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 ARG A 377 N GLN A 329
SHEET 6 E 7 ARG A 381 GLY A 393 -1 O GLY A 384 N ILE A 376
SHEET 7 E 7 LYS A 299 ILE A 310 -1 N GLU A 305 O LYS A 390
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
SHEET 1 G 6 SER B 65 ASP B 70 0
SHEET 2 G 6 HIS B 75 ASP B 80 -1 O HIS B 78 N VAL B 67
SHEET 3 G 6 HIS B 11 ILE B 17 1 N VAL B 14 O ALA B 77
SHEET 4 G 6 GLY B 100 ALA B 106 1 O VAL B 104 N ILE B 17
SHEET 5 G 6 ILE B 130 ASN B 135 1 O ILE B 131 N LEU B 103
SHEET 6 G 6 ILE B 169 ARG B 171 1 O VAL B 170 N LEU B 134
SHEET 1 H 7 LEU B 211 PRO B 213 0
SHEET 2 H 7 VAL B 291 ALA B 293 -1 O LEU B 292 N LEU B 212
SHEET 3 H 7 GLU B 241 VAL B 245 -1 N GLU B 243 O ALA B 293
SHEET 4 H 7 GLN B 251 MET B 260 -1 O SER B 253 N VAL B 242
SHEET 5 H 7 ASN B 273 ARG B 279 -1 O LEU B 277 N THR B 256
SHEET 6 H 7 VAL B 226 ARG B 230 -1 N GLY B 229 O VAL B 274
SHEET 7 H 7 VAL B 217 PHE B 218 -1 N PHE B 218 O VAL B 226
SHEET 1 I 5 LEU B 211 PRO B 213 0
SHEET 2 I 5 VAL B 291 ALA B 293 -1 O LEU B 292 N LEU B 212
SHEET 3 I 5 GLU B 241 VAL B 245 -1 N GLU B 243 O ALA B 293
SHEET 4 I 5 GLN B 251 MET B 260 -1 O SER B 253 N VAL B 242
SHEET 5 I 5 LYS B 263 LEU B 265 -1 O LEU B 265 N VAL B 258
SHEET 1 J 2 ILE B 235 LYS B 237 0
SHEET 2 J 2 GLU B 267 ARG B 269 -1 O GLY B 268 N ILE B 236
SHEET 1 K 7 LYS B 299 ILE B 310 0
SHEET 2 K 7 ASN B 355 MET B 368 -1 O ILE B 356 N VAL B 308
SHEET 3 K 7 THR B 335 GLU B 342 -1 N THR B 340 O THR B 361
SHEET 4 K 7 GLN B 329 PHE B 332 -1 N PHE B 330 O VAL B 337
SHEET 5 K 7 ARG B 373 GLU B 378 -1 O ALA B 375 N TYR B 331
SHEET 6 K 7 ARG B 381 VAL B 391 -1 O GLY B 384 N ILE B 376
SHEET 7 K 7 LYS B 299 ILE B 310 -1 N GLU B 305 O LYS B 390
LINK C SER C 1 N BB9 C 2 1555 1555 1.36
LINK C BB9 C 2 N MEN C 3 1555 1555 1.35
LINK C BB6 C 4 N VAL C 5 1555 1555 1.35
LINK C BB7 C 6 N GLY C 7 1555 1555 1.35
LINK C BB8 C 8 N BB9 C 9 1555 1555 1.31
LINK C BB9 C 9 N BB9 C 10 1555 1555 1.33
LINK C BB9 C 10 N MH6 C 11 1555 1555 1.35
LINK C MH6 C 11 N 8BB C 12 1555 1555 1.34
LINK C MH6 C 11 SG 8BB C 12 1555 1555 1.76
LINK C SER D 1 N BB9 D 2 1555 1555 1.34
LINK C BB9 D 2 N MEN D 3 1555 1555 1.33
LINK C BB6 D 4 N VAL D 5 1555 1555 1.35
LINK C BB7 D 6 N GLY D 7 1555 1555 1.35
LINK C BB8 D 8 N BB9 D 9 1555 1555 1.31
LINK C BB9 D 9 N BB9 D 10 1555 1555 1.34
LINK C BB9 D 10 N MH6 D 11 1555 1555 1.35
LINK C MH6 D 11 N 8BB D 12 1555 1555 1.34
LINK C MH6 D 11 SG 8BB D 12 1555 1555 1.77
LINK MG MG A 401 O2B GDP A 402 1555 1555 1.97
LINK MG MG A 401 O HOH A 514 1555 1555 1.97
LINK OG1 THR B 25 MG MG B 402 1555 1555 1.97
LINK MG MG B 402 O HOH B 512 1555 1555 2.00
LINK MG MG A 401 O HOH A 503 1555 1555 2.01
LINK MG MG B 402 O HOH B 505 1555 1555 2.03
LINK OG1 THR A 25 MG MG A 401 1555 1555 2.09
LINK O2B GDP B 401 MG MG B 402 1555 1555 2.10
LINK MG MG B 402 O HOH B 516 1555 1555 2.14
LINK MG MG A 401 O HOH A 517 1555 1555 2.16
LINK MG MG B 402 O HOH B 514 1555 1555 2.20
LINK MG MG A 401 O HOH A 531 1555 1555 2.24
LINK CB SER D 1 CB MH6 D 11 1555 1555 1.39
LINK CB SER C 1 CB MH6 C 11 1555 1555 1.40
LINK CA SER C 1 C BB9 C 10 1555 1555 1.42
LINK CA SER D 1 C BB9 D 10 1555 1555 1.42
LINK C MEN D 3 SG BB6 D 4 1555 1555 1.74
LINK C MEN C 3 SG BB6 C 4 1555 1555 1.75
LINK C VAL C 5 SG BB7 C 6 1555 1555 1.75
LINK C BB9 D 9 SG BB9 D 10 1555 1555 1.75
LINK C VAL D 5 SG BB7 D 6 1555 1555 1.76
LINK C SER D 1 SG BB9 D 2 1555 1555 1.76
LINK C BB8 C 8 SG BB9 C 9 1555 1555 1.76
LINK C BB8 D 8 SG BB9 D 9 1555 1555 1.77
LINK C SER C 1 SG BB9 C 2 1555 1555 1.77
LINK C BB9 C 9 SG BB9 C 10 1555 1555 1.77
CISPEP 1 ALA B 95 ALA B 96 0 3.72
SITE 1 AC1 6 THR A 25 GDP A 402 HOH A 503 HOH A 514
SITE 2 AC1 6 HOH A 517 HOH A 531
SITE 1 AC2 18 ASP A 21 HIS A 22 GLY A 23 LYS A 24
SITE 2 AC2 18 THR A 25 THR A 26 ASN A 135 LYS A 136
SITE 3 AC2 18 ASP A 138 MET A 139 SER A 173 ALA A 174
SITE 4 AC2 18 LEU A 175 MG A 401 HOH A 514 HOH A 517
SITE 5 AC2 18 HOH A 554 HOH A 562
SITE 1 AC3 20 HIS B 19 ASP B 21 HIS B 22 GLY B 23
SITE 2 AC3 20 LYS B 24 THR B 25 THR B 26 ASN B 135
SITE 3 AC3 20 LYS B 136 ASP B 138 MET B 139 SER B 173
SITE 4 AC3 20 ALA B 174 LEU B 175 MG B 402 HOH B 505
SITE 5 AC3 20 HOH B 509 HOH B 512 HOH B 514 HOH B 515
SITE 1 AC4 6 THR B 25 GDP B 401 HOH B 505 HOH B 512
SITE 2 AC4 6 HOH B 514 HOH B 516
SITE 1 AC5 17 GLU B 143 GLU B 215 ASP B 216 PHE B 218
SITE 2 AC5 17 VAL B 226 THR B 228 THR B 256 GLY B 257
SITE 3 AC5 17 GLU B 259 PHE B 261 ARG B 262 ARG B 269
SITE 4 AC5 17 ASN B 273 VAL B 274 GLY B 275 LEU B 277
SITE 5 AC5 17 HOH C 101
SITE 1 AC6 17 GLU A 143 ILE A 206 GLU A 215 ASP A 216
SITE 2 AC6 17 PHE A 218 THR A 228 THR A 256 GLY A 257
SITE 3 AC6 17 GLU A 259 MET A 260 PHE A 261 ARG A 262
SITE 4 AC6 17 ARG A 269 ASN A 273 VAL A 274 GLY A 275
SITE 5 AC6 17 LEU A 277
CRYST1 97.246 100.376 156.483 90.00 90.00 90.00 C 2 2 21 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 0.010283 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009963 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006390 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
