HEADER ISOMERASE 28-OCT-05 2EUA
TITLE STRUCTURE AND MECHANISM OF MENF, THE MENAQUINONE-SPECIFIC
TITLE 2 ISOCHORISMATE SYNTHASE FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MENAQUINONE-SPECIFIC ISOCHORISMATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ISOCHORISMATE MUTASE;
COMPND 5 EC: 5.4.4.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MENF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA FOLD, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KOLAPPAN,C.KISKER,J.ZWAHLEN,R.ZHOU,P.J.TONGE
REVDAT 5 14-FEB-24 2EUA 1 REMARK
REVDAT 4 18-OCT-17 2EUA 1 REMARK
REVDAT 3 19-JAN-10 2EUA 1 JRNL
REVDAT 2 24-FEB-09 2EUA 1 VERSN
REVDAT 1 05-DEC-06 2EUA 0
JRNL AUTH S.KOLAPPAN,J.ZWAHLEN,R.ZHOU,J.J.TRUGLIO,P.J.TONGE,C.KISKER
JRNL TITL LYSINE 190 IS THE CATALYTIC BASE IN MENF, THE
JRNL TITL 2 MENAQUINONE-SPECIFIC ISOCHORISMATE SYNTHASE FROM ESCHERICHIA
JRNL TITL 3 COLI: IMPLICATIONS FOR AN ENZYME FAMILY.
JRNL REF BIOCHEMISTRY V. 46 946 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17240978
JRNL DOI 10.1021/BI0608515
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 44680
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2393
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2903
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.4080
REMARK 3 BIN FREE R VALUE SET COUNT : 153
REMARK 3 BIN FREE R VALUE : 0.4520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6687
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : -0.05000
REMARK 3 B33 (A**2) : 0.10000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.370
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.276
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.027
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6859 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9335 ; 1.592 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 854 ; 8.959 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 324 ;37.302 ;23.519
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1115 ;20.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 62 ;16.579 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1050 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5276 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3049 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4626 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 327 ; 0.148 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 39 ; 0.221 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.260 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4364 ; 0.541 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6834 ; 0.930 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2814 ; 1.401 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2501 ; 2.206 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 429 4
REMARK 3 1 B 2 B 429 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3240 ; NULL ; NULL
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3240 ; NULL ; NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EUA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035100.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-04; 31-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X26C; X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.25360; 0.9745, 0.97971
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47401
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09900
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) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE 2.03, RESOLVE 2.03
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M POTASSIUM SODIUM TARTRATE, 0.1 M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 62.80000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 73.20400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 73.20400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 94.20000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 73.20400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 73.20400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.40000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 73.20400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 73.20400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 94.20000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 73.20400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 73.20400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.40000
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 62.80000
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: 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 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 1
REMARK 465 MET A 430
REMARK 465 GLU A 431
REMARK 465 MET B 1
REMARK 465 MET B 430
REMARK 465 GLU B 431
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 2 CG CD OE1 NE2
REMARK 470 ASP A 36 CG OD1 OD2
REMARK 470 GLN A 48 CG CD OE1 NE2
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 HIS A 157 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 ARG A 283 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 294 CG CD OE1 NE2
REMARK 470 LEU A 348 CG CD1 CD2
REMARK 470 ARG A 350 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 351 CG OD1 OD2
REMARK 470 ARG A 406 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 415 CG CD OE1 NE2
REMARK 470 GLU A 416 CG CD OE1 OE2
REMARK 470 THR B 5 OG1 CG2
REMARK 470 LYS B 35 CG CD CE NZ
REMARK 470 ASP B 36 CG OD1 OD2
REMARK 470 GLN B 48 CG CD OE1 NE2
REMARK 470 HIS B 135 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 158 CG CD1 CD2
REMARK 470 GLU B 187 CG CD OE1 OE2
REMARK 470 ARG B 283 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 348 CG CD1 CD2
REMARK 470 ARG B 350 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 351 CG OD1 OD2
REMARK 470 GLN B 355 CG CD OE1 NE2
REMARK 470 ARG B 359 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 406 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 412 CG CD OE1 NE2
REMARK 470 GLN B 415 CG CD OE1 NE2
REMARK 470 GLU B 416 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CD PRO B 51 O HOH B 1071 1.96
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 264 C ASP A 264 O 0.221
REMARK 500 LYS A 266 CG LYS A 266 CD 0.369
REMARK 500 LYS A 266 CD LYS A 266 CE 0.243
REMARK 500 LYS A 266 CE LYS A 266 NZ 0.319
REMARK 500 GLN A 267 CD GLN A 267 OE1 0.148
REMARK 500 GLN A 267 CD GLN A 267 NE2 0.196
REMARK 500 ALA A 268 C ALA A 268 O 0.121
REMARK 500 LYS B 266 C GLN B 267 N 0.174
REMARK 500 GLN B 270 CG GLN B 270 CD 0.168
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 50 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 PRO A 167 C - N - CA ANGL. DEV. = 32.0 DEGREES
REMARK 500 PRO A 167 C - N - CD ANGL. DEV. = -32.8 DEGREES
REMARK 500 ARG A 244 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 264 CB - CG - OD2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 LYS A 266 CB - CG - CD ANGL. DEV. = -19.3 DEGREES
REMARK 500 PRO A 341 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 PRO B 167 C - N - CA ANGL. DEV. = 12.8 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 GLN A 17 -160.20 -78.13
REMARK 500 GLU A 18 -88.46 -46.44
REMARK 500 ILE A 19 107.72 62.91
REMARK 500 LYS A 35 -9.45 -47.57
REMARK 500 ASP A 36 169.07 59.81
REMARK 500 ALA A 37 -1.92 131.55
REMARK 500 SER A 131 -40.37 -133.96
REMARK 500 HIS A 157 -93.78 -75.20
REMARK 500 LEU A 158 107.23 65.62
REMARK 500 PRO A 167 121.18 26.91
REMARK 500 GLU A 187 -85.69 60.83
REMARK 500 ASP A 247 -105.94 53.34
REMARK 500 ASP A 264 96.32 -55.28
REMARK 500 LYS A 266 -36.44 -163.75
REMARK 500 GLN A 301 -140.16 -74.31
REMARK 500 LEU A 313 -160.37 -114.41
REMARK 500 PRO A 341 114.42 12.68
REMARK 500 LEU A 348 -121.49 -28.78
REMARK 500 PRO A 362 26.17 -67.72
REMARK 500 GLU A 366 -116.09 61.23
REMARK 500 GLN B 17 -147.55 -76.37
REMARK 500 ALA B 21 42.61 -93.92
REMARK 500 ALA B 37 24.59 -143.81
REMARK 500 ARG B 58 -52.11 -27.14
REMARK 500 ILE B 150 104.14 -56.96
REMARK 500 HIS B 157 -90.24 -103.50
REMARK 500 LEU B 158 147.43 73.61
REMARK 500 PRO B 167 122.66 21.07
REMARK 500 ASP B 168 -169.31 -78.31
REMARK 500 ALA B 184 34.57 -82.53
REMARK 500 GLU B 185 -43.01 -136.35
REMARK 500 ASP B 247 -110.46 51.37
REMARK 500 GLN B 297 -64.61 -24.86
REMARK 500 GLN B 301 -143.00 -83.96
REMARK 500 LEU B 313 -166.75 -105.93
REMARK 500 PRO B 341 104.76 12.08
REMARK 500 ALA B 346 -59.69 -120.94
REMARK 500 LEU B 348 -144.51 18.06
REMARK 500 PRO B 362 26.98 -79.86
REMARK 500 TRP B 367 -40.89 78.02
REMARK 500 ARG B 387 56.46 39.62
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 49 TYR A 50 -148.51
REMARK 500 TYR A 50 PRO A 51 138.96
REMARK 500 TRP A 166 PRO A 167 -110.57
REMARK 500 GLN A 340 PRO A 341 -100.01
REMARK 500 THR B 49 TYR B 50 -149.72
REMARK 500 TYR B 50 PRO B 51 128.02
REMARK 500 TRP B 166 PRO B 167 -111.13
REMARK 500 GLN B 340 PRO B 341 -103.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR B 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EUJ RELATED DB: PDB
DBREF 2EUA A 1 431 UNP P38051 MENF_ECOLI 1 431
DBREF 2EUA B 1 431 UNP P38051 MENF_ECOLI 1 431
SEQRES 1 A 431 MET GLN SER LEU THR THR ALA LEU GLU ASN LEU LEU ARG
SEQRES 2 A 431 HIS LEU SER GLN GLU ILE PRO ALA THR PRO GLY ILE ARG
SEQRES 3 A 431 VAL ILE ASP ILE PRO PHE PRO LEU LYS ASP ALA PHE ASP
SEQRES 4 A 431 ALA LEU SER TRP LEU ALA SER GLN GLN THR TYR PRO GLN
SEQRES 5 A 431 PHE TYR TRP GLN GLN ARG ASN GLY ASP GLU GLU ALA VAL
SEQRES 6 A 431 VAL LEU GLY ALA ILE THR ARG PHE THR SER LEU ASP GLN
SEQRES 7 A 431 ALA GLN ARG PHE LEU ARG GLN HIS PRO GLU HIS ALA ASP
SEQRES 8 A 431 LEU ARG ILE TRP GLY LEU ASN ALA PHE ASP PRO SER GLN
SEQRES 9 A 431 GLY ASN LEU LEU LEU PRO ARG LEU GLU TRP ARG ARG CYS
SEQRES 10 A 431 GLY GLY LYS ALA THR LEU ARG LEU THR LEU PHE SER GLU
SEQRES 11 A 431 SER SER LEU GLN HIS ASP ALA ILE GLN ALA LYS GLU PHE
SEQRES 12 A 431 ILE ALA THR LEU VAL SER ILE LYS PRO LEU PRO GLY LEU
SEQRES 13 A 431 HIS LEU THR THR THR ARG GLU GLN HIS TRP PRO ASP LYS
SEQRES 14 A 431 THR GLY TRP THR GLN LEU ILE GLU LEU ALA THR LYS THR
SEQRES 15 A 431 ILE ALA GLU GLY GLU LEU ASP LYS VAL VAL LEU ALA ARG
SEQRES 16 A 431 ALA THR ASP LEU HIS PHE ALA SER PRO VAL ASN ALA ALA
SEQRES 17 A 431 ALA MET MET ALA ALA SER ARG ARG LEU ASN LEU ASN CYS
SEQRES 18 A 431 TYR HIS PHE TYR MET ALA PHE ASP GLY GLU ASN ALA PHE
SEQRES 19 A 431 LEU GLY SER SER PRO GLU ARG LEU TRP ARG ARG ARG ASP
SEQRES 20 A 431 LYS ALA LEU ARG THR GLU ALA LEU ALA GLY THR VAL ALA
SEQRES 21 A 431 ASN ASN PRO ASP ASP LYS GLN ALA GLN GLN LEU GLY GLU
SEQRES 22 A 431 TRP LEU MET ALA ASP ASP LYS ASN GLN ARG GLU ASN MET
SEQRES 23 A 431 LEU VAL VAL GLU ASP ILE CYS GLN ARG LEU GLN ALA ASP
SEQRES 24 A 431 THR GLN THR LEU ASP VAL LEU PRO PRO GLN VAL LEU ARG
SEQRES 25 A 431 LEU ARG LYS VAL GLN HIS LEU ARG ARG CYS ILE TRP THR
SEQRES 26 A 431 SER LEU ASN LYS ALA ASP ASP VAL ILE CYS LEU HIS GLN
SEQRES 27 A 431 LEU GLN PRO THR ALA ALA VAL ALA GLY LEU PRO ARG ASP
SEQRES 28 A 431 LEU ALA ARG GLN PHE ILE ALA ARG HIS GLU PRO PHE THR
SEQRES 29 A 431 ARG GLU TRP TYR ALA GLY SER ALA GLY TYR LEU SER LEU
SEQRES 30 A 431 GLN GLN SER GLU PHE CYS VAL SER LEU ARG SER ALA LYS
SEQRES 31 A 431 ILE SER GLY ASN VAL VAL ARG LEU TYR ALA GLY ALA GLY
SEQRES 32 A 431 ILE VAL ARG GLY SER ASP PRO GLU GLN GLU TRP GLN GLU
SEQRES 33 A 431 ILE ASP ASN LYS ALA ALA GLY LEU ARG THR LEU LEU GLN
SEQRES 34 A 431 MET GLU
SEQRES 1 B 431 MET GLN SER LEU THR THR ALA LEU GLU ASN LEU LEU ARG
SEQRES 2 B 431 HIS LEU SER GLN GLU ILE PRO ALA THR PRO GLY ILE ARG
SEQRES 3 B 431 VAL ILE ASP ILE PRO PHE PRO LEU LYS ASP ALA PHE ASP
SEQRES 4 B 431 ALA LEU SER TRP LEU ALA SER GLN GLN THR TYR PRO GLN
SEQRES 5 B 431 PHE TYR TRP GLN GLN ARG ASN GLY ASP GLU GLU ALA VAL
SEQRES 6 B 431 VAL LEU GLY ALA ILE THR ARG PHE THR SER LEU ASP GLN
SEQRES 7 B 431 ALA GLN ARG PHE LEU ARG GLN HIS PRO GLU HIS ALA ASP
SEQRES 8 B 431 LEU ARG ILE TRP GLY LEU ASN ALA PHE ASP PRO SER GLN
SEQRES 9 B 431 GLY ASN LEU LEU LEU PRO ARG LEU GLU TRP ARG ARG CYS
SEQRES 10 B 431 GLY GLY LYS ALA THR LEU ARG LEU THR LEU PHE SER GLU
SEQRES 11 B 431 SER SER LEU GLN HIS ASP ALA ILE GLN ALA LYS GLU PHE
SEQRES 12 B 431 ILE ALA THR LEU VAL SER ILE LYS PRO LEU PRO GLY LEU
SEQRES 13 B 431 HIS LEU THR THR THR ARG GLU GLN HIS TRP PRO ASP LYS
SEQRES 14 B 431 THR GLY TRP THR GLN LEU ILE GLU LEU ALA THR LYS THR
SEQRES 15 B 431 ILE ALA GLU GLY GLU LEU ASP LYS VAL VAL LEU ALA ARG
SEQRES 16 B 431 ALA THR ASP LEU HIS PHE ALA SER PRO VAL ASN ALA ALA
SEQRES 17 B 431 ALA MET MET ALA ALA SER ARG ARG LEU ASN LEU ASN CYS
SEQRES 18 B 431 TYR HIS PHE TYR MET ALA PHE ASP GLY GLU ASN ALA PHE
SEQRES 19 B 431 LEU GLY SER SER PRO GLU ARG LEU TRP ARG ARG ARG ASP
SEQRES 20 B 431 LYS ALA LEU ARG THR GLU ALA LEU ALA GLY THR VAL ALA
SEQRES 21 B 431 ASN ASN PRO ASP ASP LYS GLN ALA GLN GLN LEU GLY GLU
SEQRES 22 B 431 TRP LEU MET ALA ASP ASP LYS ASN GLN ARG GLU ASN MET
SEQRES 23 B 431 LEU VAL VAL GLU ASP ILE CYS GLN ARG LEU GLN ALA ASP
SEQRES 24 B 431 THR GLN THR LEU ASP VAL LEU PRO PRO GLN VAL LEU ARG
SEQRES 25 B 431 LEU ARG LYS VAL GLN HIS LEU ARG ARG CYS ILE TRP THR
SEQRES 26 B 431 SER LEU ASN LYS ALA ASP ASP VAL ILE CYS LEU HIS GLN
SEQRES 27 B 431 LEU GLN PRO THR ALA ALA VAL ALA GLY LEU PRO ARG ASP
SEQRES 28 B 431 LEU ALA ARG GLN PHE ILE ALA ARG HIS GLU PRO PHE THR
SEQRES 29 B 431 ARG GLU TRP TYR ALA GLY SER ALA GLY TYR LEU SER LEU
SEQRES 30 B 431 GLN GLN SER GLU PHE CYS VAL SER LEU ARG SER ALA LYS
SEQRES 31 B 431 ILE SER GLY ASN VAL VAL ARG LEU TYR ALA GLY ALA GLY
SEQRES 32 B 431 ILE VAL ARG GLY SER ASP PRO GLU GLN GLU TRP GLN GLU
SEQRES 33 B 431 ILE ASP ASN LYS ALA ALA GLY LEU ARG THR LEU LEU GLN
SEQRES 34 B 431 MET GLU
HET TAR A1000 10
HET TAR B1001 10
HETNAM TAR D(-)-TARTARIC ACID
FORMUL 3 TAR 2(C4 H6 O6)
FORMUL 5 HOH *150(H2 O)
HELIX 1 1 GLN A 2 LEU A 15 1 14
HELIX 2 2 ASP A 39 SER A 46 1 8
HELIX 3 3 SER A 75 ARG A 84 1 10
HELIX 4 4 GLN A 85 ALA A 90 5 6
HELIX 5 5 SER A 132 THR A 146 1 15
HELIX 6 6 ASP A 168 GLU A 185 1 18
HELIX 7 7 ASN A 206 ASN A 218 1 13
HELIX 8 8 LYS A 266 MET A 276 1 11
HELIX 9 9 ASP A 278 GLN A 297 1 20
HELIX 10 10 ASP A 331 GLN A 340 1 10
HELIX 11 11 PRO A 349 GLU A 361 1 13
HELIX 12 12 ASP A 409 LEU A 427 1 19
HELIX 13 13 GLN B 2 LEU B 15 1 14
HELIX 14 14 ASP B 39 GLN B 47 1 9
HELIX 15 15 SER B 75 ARG B 84 1 10
HELIX 16 16 SER B 132 THR B 146 1 15
HELIX 17 17 ASP B 168 ALA B 184 1 17
HELIX 18 18 ASN B 206 ASN B 218 1 13
HELIX 19 19 ASP B 264 ALA B 277 1 14
HELIX 20 20 ASP B 278 GLN B 297 1 20
HELIX 21 21 ALA B 298 THR B 300 5 3
HELIX 22 22 ASP B 331 GLN B 340 1 10
HELIX 23 23 THR B 342 GLY B 347 1 6
HELIX 24 24 PRO B 349 GLU B 361 1 13
HELIX 25 25 ASP B 409 THR B 426 1 18
HELIX 26 26 LEU B 427 GLN B 429 5 3
SHEET 1 A10 GLY A 24 PHE A 32 0
SHEET 2 A10 LYS A 120 SER A 129 -1 O LEU A 127 N ARG A 26
SHEET 3 A10 GLY A 105 CYS A 117 -1 N GLU A 113 O ARG A 124
SHEET 4 A10 ILE A 94 ASN A 98 -1 N TRP A 95 O LEU A 108
SHEET 5 A10 SER A 371 LEU A 375 -1 O SER A 371 N ASN A 98
SHEET 6 A10 GLN A 379 VAL A 384 -1 O CYS A 383 N ALA A 372
SHEET 7 A10 ARG A 241 ARG A 246 -1 N ARG A 245 O SER A 380
SHEET 8 A10 ALA A 249 ALA A 260 -1 O ALA A 249 N ARG A 246
SHEET 9 A10 VAL A 316 SER A 326 -1 O ILE A 323 N THR A 252
SHEET 10 A10 ASP A 304 VAL A 305 -1 N ASP A 304 O TRP A 324
SHEET 1 B16 THR A 160 TRP A 166 0
SHEET 2 B16 VAL A 191 PHE A 201 -1 O ALA A 196 N TRP A 166
SHEET 3 B16 VAL A 395 ILE A 404 -1 O VAL A 396 N LEU A 199
SHEET 4 B16 SER A 388 SER A 392 -1 N LYS A 390 O ARG A 397
SHEET 5 B16 ASN A 232 SER A 238 -1 N ALA A 233 O ILE A 391
SHEET 6 B16 TYR A 222 ASP A 229 -1 N TYR A 222 O SER A 238
SHEET 7 B16 GLN A 52 GLN A 56 -1 N GLN A 52 O ALA A 227
SHEET 8 B16 GLU A 62 PHE A 73 -1 O ALA A 64 N TRP A 55
SHEET 9 B16 GLY A 105 CYS A 117 -1 O LEU A 109 N ILE A 70
SHEET 10 B16 ILE A 94 ASN A 98 -1 N TRP A 95 O LEU A 108
SHEET 11 B16 SER A 371 LEU A 375 -1 O SER A 371 N ASN A 98
SHEET 12 B16 GLN A 379 VAL A 384 -1 O CYS A 383 N ALA A 372
SHEET 13 B16 ARG A 241 ARG A 246 -1 N ARG A 245 O SER A 380
SHEET 14 B16 ALA A 249 ALA A 260 -1 O ALA A 249 N ARG A 246
SHEET 15 B16 VAL A 316 SER A 326 -1 O ILE A 323 N THR A 252
SHEET 16 B16 GLN A 309 ARG A 312 -1 N GLN A 309 O ARG A 320
SHEET 1 C10 GLY B 24 PRO B 31 0
SHEET 2 C10 LYS B 120 SER B 129 -1 O LEU B 123 N ILE B 30
SHEET 3 C10 GLY B 105 CYS B 117 -1 N GLU B 113 O ARG B 124
SHEET 4 C10 ILE B 94 ASN B 98 -1 N TRP B 95 O LEU B 108
SHEET 5 C10 SER B 371 LEU B 375 -1 O SER B 371 N ASN B 98
SHEET 6 C10 GLN B 379 VAL B 384 -1 O CYS B 383 N ALA B 372
SHEET 7 C10 ARG B 241 ARG B 246 -1 N ARG B 245 O SER B 380
SHEET 8 C10 ALA B 249 ALA B 260 -1 O ALA B 249 N ARG B 246
SHEET 9 C10 VAL B 316 SER B 326 -1 O THR B 325 N LEU B 250
SHEET 10 C10 ASP B 304 VAL B 305 -1 N ASP B 304 O TRP B 324
SHEET 1 D16 THR B 160 TRP B 166 0
SHEET 2 D16 ARG B 195 PHE B 201 -1 O HIS B 200 N THR B 161
SHEET 3 D16 VAL B 395 ALA B 400 -1 O VAL B 396 N LEU B 199
SHEET 4 D16 SER B 388 SER B 392 -1 N LYS B 390 O ARG B 397
SHEET 5 D16 ASN B 232 SER B 238 -1 N ALA B 233 O ILE B 391
SHEET 6 D16 TYR B 222 ASP B 229 -1 N MET B 226 O PHE B 234
SHEET 7 D16 GLN B 52 GLN B 56 -1 N GLN B 52 O ALA B 227
SHEET 8 D16 GLU B 62 PHE B 73 -1 O ALA B 64 N TRP B 55
SHEET 9 D16 GLY B 105 CYS B 117 -1 O LEU B 109 N ILE B 70
SHEET 10 D16 ILE B 94 ASN B 98 -1 N TRP B 95 O LEU B 108
SHEET 11 D16 SER B 371 LEU B 375 -1 O SER B 371 N ASN B 98
SHEET 12 D16 GLN B 379 VAL B 384 -1 O CYS B 383 N ALA B 372
SHEET 13 D16 ARG B 241 ARG B 246 -1 N ARG B 245 O SER B 380
SHEET 14 D16 ALA B 249 ALA B 260 -1 O ALA B 249 N ARG B 246
SHEET 15 D16 VAL B 316 SER B 326 -1 O THR B 325 N LEU B 250
SHEET 16 D16 GLN B 309 ARG B 312 -1 N GLN B 309 O ARG B 320
SHEET 1 E 2 LYS B 190 VAL B 192 0
SHEET 2 E 2 GLY B 403 VAL B 405 -1 O ILE B 404 N VAL B 191
SITE 1 AC1 8 ARG A 58 ASN A 59 ARG A 241 ARG A 244
SITE 2 AC1 8 ARG A 251 HOH A1035 HOH A1049 HOH A1066
SITE 1 AC2 7 ARG B 58 ASN B 59 ARG B 241 ARG B 244
SITE 2 AC2 7 ARG B 251 HOH B1003 HOH B1056
CRYST1 146.408 146.408 125.600 90.00 90.00 90.00 P 43 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006830 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007960 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
