HEADER HYDROLASE/TRANSPORT PROTEIN 16-SEP-11 3TUI
TITLE INWARD FACING CONFORMATIONS OF THE METNI METHIONINE ABC TRANSPORTER:
TITLE 2 CY5 NATIVE CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-METHIONINE TRANSPORT SYSTEM PERMEASE PROTEIN METI;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: METHIONINE IMPORT ATP-BINDING PROTEIN METN;
COMPND 7 CHAIN: C, D, G, H;
COMPND 8 EC: 3.6.3.-;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B0198, JW0194, METI, YAEE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21*;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 83333;
SOURCE 13 STRAIN: K12;
SOURCE 14 GENE: ABC, B0199, JW0195, METN;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21*;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PET
KEYWDS ABC-TRANSPORTER, TYPE I ABC TYPE IMPORTER, METHIONINE UPTAKE
KEYWDS 2 TRANSPORTER, MEMBRANE PROTEIN, AMINO-ACID TRANSPORT, ATP-BINDING,
KEYWDS 3 HYDROLASE, INNER MEMBRANE, HYDROLASE-TRANSPORT PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.JOHNSON,P.T.NGUYEN,D.C.REES
REVDAT 3 13-SEP-23 3TUI 1 REMARK SEQADV
REVDAT 2 28-DEC-11 3TUI 1 JRNL
REVDAT 1 30-NOV-11 3TUI 0
JRNL AUTH E.JOHNSON,P.T.NGUYEN,T.O.YEATES,D.C.REES
JRNL TITL INWARD FACING CONFORMATIONS OF THE METNI METHIONINE ABC
JRNL TITL 2 TRANSPORTER: IMPLICATIONS FOR THE MECHANISM OF
JRNL TITL 3 TRANSINHIBITION.
JRNL REF PROTEIN SCI. V. 21 84 2012
JRNL REFN ISSN 0961-8368
JRNL PMID 22095702
JRNL DOI 10.1002/PRO.765
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 74334
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 3692
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.6101 - 8.5251 0.98 2777 164 0.2181 0.2676
REMARK 3 2 8.5251 - 6.7935 1.00 2819 131 0.1922 0.2395
REMARK 3 3 6.7935 - 5.9426 1.00 2797 142 0.2350 0.3080
REMARK 3 4 5.9426 - 5.4029 1.00 2770 150 0.2467 0.2922
REMARK 3 5 5.4029 - 5.0176 1.00 2797 139 0.2239 0.3170
REMARK 3 6 5.0176 - 4.7231 1.00 2774 152 0.2081 0.3247
REMARK 3 7 4.7231 - 4.4874 1.00 2765 141 0.1838 0.2334
REMARK 3 8 4.4874 - 4.2926 1.00 2747 157 0.1760 0.2525
REMARK 3 9 4.2926 - 4.1278 1.00 2803 145 0.1877 0.2517
REMARK 3 10 4.1278 - 3.9857 1.00 2726 153 0.2064 0.2365
REMARK 3 11 3.9857 - 3.8614 1.00 2801 137 0.2072 0.2679
REMARK 3 12 3.8614 - 3.7512 1.00 2761 163 0.2123 0.3179
REMARK 3 13 3.7512 - 3.6527 1.00 2731 149 0.2197 0.3140
REMARK 3 14 3.6527 - 3.5637 1.00 2818 119 0.2301 0.3137
REMARK 3 15 3.5637 - 3.4828 1.00 2736 138 0.2399 0.3042
REMARK 3 16 3.4828 - 3.4088 1.00 2777 159 0.2458 0.3271
REMARK 3 17 3.4088 - 3.3407 1.00 2740 145 0.2669 0.3772
REMARK 3 18 3.3407 - 3.2777 1.00 2841 124 0.2891 0.3413
REMARK 3 19 3.2777 - 3.2193 1.00 2748 121 0.2998 0.3798
REMARK 3 20 3.2193 - 3.1648 1.00 2794 139 0.3084 0.3408
REMARK 3 21 3.1648 - 3.1138 1.00 2712 153 0.3278 0.3680
REMARK 3 22 3.1138 - 3.0659 1.00 2785 158 0.3486 0.3631
REMARK 3 23 3.0659 - 3.0209 0.97 2651 154 0.3720 0.4046
REMARK 3 24 3.0209 - 2.9784 0.91 2486 137 0.3856 0.4333
REMARK 3 25 2.9784 - 2.9382 0.84 2364 108 0.4068 0.4642
REMARK 3 26 2.9382 - 2.9000 0.78 2122 114 0.4420 0.4122
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.28
REMARK 3 B_SOL : 32.99
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.290
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) : -3.52730
REMARK 3 B22 (A**2) : 2.37420
REMARK 3 B33 (A**2) : 0.86020
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.20730
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 17537
REMARK 3 ANGLE : 1.469 23863
REMARK 3 CHIRALITY : 0.088 2910
REMARK 3 PLANARITY : 0.007 2999
REMARK 3 DIHEDRAL : 15.893 6421
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91606
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 29.608
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
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) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40400
REMARK 200 R SYM FOR SHELL (I) : 0.40400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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 3DHW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% V/V POLYETHYLENE GLYCOL 400, 0.1 M
REMARK 280 TRIS, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 70.04000
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 LYS A 217
REMARK 465 LYS B 217
REMARK 465 MET C -22
REMARK 465 GLY C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 HIS C -7
REMARK 465 ILE C -6
REMARK 465 ASP C -5
REMARK 465 ASP C -4
REMARK 465 ASP C -3
REMARK 465 ASP C -2
REMARK 465 LYS C -1
REMARK 465 MET D -22
REMARK 465 GLY D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 HIS D -7
REMARK 465 ILE D -6
REMARK 465 ASP D -5
REMARK 465 ASP D -4
REMARK 465 ASP D -3
REMARK 465 ASP D -2
REMARK 465 LYS D -1
REMARK 465 HIS D 0
REMARK 465 LYS E 217
REMARK 465 LYS F 217
REMARK 465 MET G -22
REMARK 465 GLY G -21
REMARK 465 HIS G -20
REMARK 465 HIS G -19
REMARK 465 HIS G -18
REMARK 465 HIS G -17
REMARK 465 HIS G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 HIS G -13
REMARK 465 HIS G -12
REMARK 465 HIS G -11
REMARK 465 SER G -10
REMARK 465 SER G -9
REMARK 465 GLY G -8
REMARK 465 HIS G -7
REMARK 465 ILE G -6
REMARK 465 ASP G -5
REMARK 465 ASP G -4
REMARK 465 ASP G -3
REMARK 465 ASP G -2
REMARK 465 LYS G -1
REMARK 465 HIS G 0
REMARK 465 MET H -22
REMARK 465 GLY H -21
REMARK 465 HIS H -20
REMARK 465 HIS H -19
REMARK 465 HIS H -18
REMARK 465 HIS H -17
REMARK 465 HIS H -16
REMARK 465 HIS H -15
REMARK 465 HIS H -14
REMARK 465 HIS H -13
REMARK 465 HIS H -12
REMARK 465 HIS H -11
REMARK 465 SER H -10
REMARK 465 SER H -9
REMARK 465 GLY H -8
REMARK 465 HIS H -7
REMARK 465 ILE H -6
REMARK 465 ASP H -5
REMARK 465 ASP H -4
REMARK 465 ASP H -3
REMARK 465 ASP H -2
REMARK 465 LYS H -1
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 OE2 GLU A 121 NH1 ARG C 49 1.91
REMARK 500 OH TYR H 253 OE2 GLU H 315 1.97
REMARK 500 O GLN B 45 O HOH B 247 2.00
REMARK 500 NH1 ARG G 148 O HOH G 358 2.05
REMARK 500 O LEU F 119 OG SER F 123 2.09
REMARK 500 N ASN D 22 O GLY D 217 2.10
REMARK 500 O ARG B 216 O HOH B 5032 2.13
REMARK 500 O ILE B 62 OG SER B 65 2.13
REMARK 500 O GLY B 118 OD1 ASN D 92 2.14
REMARK 500 N ASP C 279 O HOH C 347 2.16
REMARK 500 OD1 ASP G 185 NH1 ARG G 188 2.17
REMARK 500 O PHE C 240 OG SER C 243 2.17
REMARK 500 O ARG H 119 OG1 THR H 122 2.18
REMARK 500 O ILE E 120 OG SER E 123 2.19
REMARK 500 O GLU G 123 N SER G 126 2.19
REMARK 500 OH TYR E 53 OE2 GLU E 109 2.19
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 PRO C 138 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU D 196 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LEU G 47 CA - CB - CG ANGL. DEV. = 15.4 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 ILE A 30 -68.05 -94.98
REMARK 500 VAL A 137 -70.35 -115.46
REMARK 500 TYR A 181 -65.40 -126.62
REMARK 500 ILE B 46 -71.53 -50.72
REMARK 500 SER B 86 -59.13 -132.56
REMARK 500 VAL B 137 -64.98 -124.12
REMARK 500 ILE B 182 -68.27 -120.90
REMARK 500 LEU C 69 -53.37 -125.17
REMARK 500 ASP C 223 -170.86 -66.28
REMARK 500 HIS C 334 38.13 71.91
REMARK 500 ASN D 23 70.39 41.93
REMARK 500 ASN D 158 70.62 51.60
REMARK 500 GLN D 166 28.46 49.89
REMARK 500 PRO D 281 48.00 -81.00
REMARK 500 ILE E 30 -63.76 -98.80
REMARK 500 VAL E 137 -57.57 -127.53
REMARK 500 ILE F 82 -70.70 -87.43
REMARK 500 SER F 86 0.53 80.11
REMARK 500 VAL F 137 -59.40 -127.90
REMARK 500 ILE F 182 -66.38 -127.97
REMARK 500 LEU G 53 -0.38 78.99
REMARK 500 GLU G 123 -70.97 -54.55
REMARK 500 ASN G 158 70.09 56.37
REMARK 500 THR G 198 163.88 173.61
REMARK 500 ASP G 209 -61.91 -92.97
REMARK 500 ASP G 223 -168.85 -170.14
REMARK 500 LYS H 114 -125.95 43.70
REMARK 500 ASP H 132 -8.78 65.65
REMARK 500 PRO H 138 -16.08 -49.71
REMARK 500 ASN H 158 72.26 53.26
REMARK 500 HIS H 334 40.00 71.91
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 GLY B 118 LEU B 119 149.47
REMARK 500 HIS G 12 GLN G 13 145.19
REMARK 500 PRO H 113 LYS H 114 146.22
REMARK 500 ASP H 132 LYS H 133 134.41
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 ADP C 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 2501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 2503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP H 2502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DHW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF METHIONINE IMPORTER METNI
REMARK 900 RELATED ID: 3DHX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ISOLATED C2 DOMAIN OF THE METHIONINE UPTAKE
REMARK 900 TRANSPORTER
DBREF 3TUI A 1 217 UNP P31547 METI_ECOLI 1 217
DBREF 3TUI B 1 217 UNP P31547 METI_ECOLI 1 217
DBREF 3TUI C 1 343 UNP P30750 METN_ECOLI 1 343
DBREF 3TUI D 1 343 UNP P30750 METN_ECOLI 1 343
DBREF 3TUI E 1 217 UNP P31547 METI_ECOLI 1 217
DBREF 3TUI F 1 217 UNP P31547 METI_ECOLI 1 217
DBREF 3TUI G 1 343 UNP P30750 METN_ECOLI 1 343
DBREF 3TUI H 1 343 UNP P30750 METN_ECOLI 1 343
SEQADV 3TUI MET C -22 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY C -21 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -20 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -19 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -18 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -17 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -16 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -15 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -14 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -13 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -12 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -11 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER C -10 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER C -9 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY C -8 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C -7 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ILE C -6 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP C -5 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP C -4 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP C -3 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP C -2 UNP P30750 EXPRESSION TAG
SEQADV 3TUI LYS C -1 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS C 0 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLN C 166 UNP P30750 GLU 166 ENGINEERED MUTATION
SEQADV 3TUI MET D -22 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY D -21 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -20 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -19 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -18 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -17 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -16 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -15 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -14 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -13 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -12 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -11 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER D -10 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER D -9 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY D -8 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D -7 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ILE D -6 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP D -5 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP D -4 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP D -3 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP D -2 UNP P30750 EXPRESSION TAG
SEQADV 3TUI LYS D -1 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS D 0 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLN D 166 UNP P30750 GLU 166 ENGINEERED MUTATION
SEQADV 3TUI MET G -22 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY G -21 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -20 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -19 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -18 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -17 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -16 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -15 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -14 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -13 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -12 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -11 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER G -10 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER G -9 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY G -8 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G -7 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ILE G -6 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP G -5 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP G -4 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP G -3 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP G -2 UNP P30750 EXPRESSION TAG
SEQADV 3TUI LYS G -1 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS G 0 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLN G 166 UNP P30750 GLU 166 ENGINEERED MUTATION
SEQADV 3TUI MET H -22 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY H -21 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -20 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -19 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -18 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -17 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -16 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -15 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -14 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -13 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -12 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -11 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER H -10 UNP P30750 EXPRESSION TAG
SEQADV 3TUI SER H -9 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLY H -8 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H -7 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ILE H -6 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP H -5 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP H -4 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP H -3 UNP P30750 EXPRESSION TAG
SEQADV 3TUI ASP H -2 UNP P30750 EXPRESSION TAG
SEQADV 3TUI LYS H -1 UNP P30750 EXPRESSION TAG
SEQADV 3TUI HIS H 0 UNP P30750 EXPRESSION TAG
SEQADV 3TUI GLN H 166 UNP P30750 GLU 166 ENGINEERED MUTATION
SEQRES 1 A 217 MET SER GLU PRO MET MET TRP LEU LEU VAL ARG GLY VAL
SEQRES 2 A 217 TRP GLU THR LEU ALA MET THR PHE VAL SER GLY PHE PHE
SEQRES 3 A 217 GLY PHE VAL ILE GLY LEU PRO VAL GLY VAL LEU LEU TYR
SEQRES 4 A 217 VAL THR ARG PRO GLY GLN ILE ILE ALA ASN ALA LYS LEU
SEQRES 5 A 217 TYR ARG THR VAL SER ALA ILE VAL ASN ILE PHE ARG SER
SEQRES 6 A 217 ILE PRO PHE ILE ILE LEU LEU VAL TRP MET ILE PRO PHE
SEQRES 7 A 217 THR ARG VAL ILE VAL GLY THR SER ILE GLY LEU GLN ALA
SEQRES 8 A 217 ALA ILE VAL PRO LEU THR VAL GLY ALA ALA PRO PHE ILE
SEQRES 9 A 217 ALA ARG MET VAL GLU ASN ALA LEU LEU GLU ILE PRO THR
SEQRES 10 A 217 GLY LEU ILE GLU ALA SER ARG ALA MET GLY ALA THR PRO
SEQRES 11 A 217 MET GLN ILE VAL ARG LYS VAL LEU LEU PRO GLU ALA LEU
SEQRES 12 A 217 PRO GLY LEU VAL ASN ALA ALA THR ILE THR LEU ILE THR
SEQRES 13 A 217 LEU VAL GLY TYR SER ALA MET GLY GLY ALA VAL GLY ALA
SEQRES 14 A 217 GLY GLY LEU GLY GLN ILE GLY TYR GLN TYR GLY TYR ILE
SEQRES 15 A 217 GLY TYR ASN ALA THR VAL MET ASN THR VAL LEU VAL LEU
SEQRES 16 A 217 LEU VAL ILE LEU VAL TYR LEU ILE GLN PHE ALA GLY ASP
SEQRES 17 A 217 ARG ILE VAL ARG ALA VAL THR ARG LYS
SEQRES 1 B 217 MET SER GLU PRO MET MET TRP LEU LEU VAL ARG GLY VAL
SEQRES 2 B 217 TRP GLU THR LEU ALA MET THR PHE VAL SER GLY PHE PHE
SEQRES 3 B 217 GLY PHE VAL ILE GLY LEU PRO VAL GLY VAL LEU LEU TYR
SEQRES 4 B 217 VAL THR ARG PRO GLY GLN ILE ILE ALA ASN ALA LYS LEU
SEQRES 5 B 217 TYR ARG THR VAL SER ALA ILE VAL ASN ILE PHE ARG SER
SEQRES 6 B 217 ILE PRO PHE ILE ILE LEU LEU VAL TRP MET ILE PRO PHE
SEQRES 7 B 217 THR ARG VAL ILE VAL GLY THR SER ILE GLY LEU GLN ALA
SEQRES 8 B 217 ALA ILE VAL PRO LEU THR VAL GLY ALA ALA PRO PHE ILE
SEQRES 9 B 217 ALA ARG MET VAL GLU ASN ALA LEU LEU GLU ILE PRO THR
SEQRES 10 B 217 GLY LEU ILE GLU ALA SER ARG ALA MET GLY ALA THR PRO
SEQRES 11 B 217 MET GLN ILE VAL ARG LYS VAL LEU LEU PRO GLU ALA LEU
SEQRES 12 B 217 PRO GLY LEU VAL ASN ALA ALA THR ILE THR LEU ILE THR
SEQRES 13 B 217 LEU VAL GLY TYR SER ALA MET GLY GLY ALA VAL GLY ALA
SEQRES 14 B 217 GLY GLY LEU GLY GLN ILE GLY TYR GLN TYR GLY TYR ILE
SEQRES 15 B 217 GLY TYR ASN ALA THR VAL MET ASN THR VAL LEU VAL LEU
SEQRES 16 B 217 LEU VAL ILE LEU VAL TYR LEU ILE GLN PHE ALA GLY ASP
SEQRES 17 B 217 ARG ILE VAL ARG ALA VAL THR ARG LYS
SEQRES 1 C 366 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 C 366 SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET ILE LYS
SEQRES 3 C 366 LEU SER ASN ILE THR LYS VAL PHE HIS GLN GLY THR ARG
SEQRES 4 C 366 THR ILE GLN ALA LEU ASN ASN VAL SER LEU HIS VAL PRO
SEQRES 5 C 366 ALA GLY GLN ILE TYR GLY VAL ILE GLY ALA SER GLY ALA
SEQRES 6 C 366 GLY LYS SER THR LEU ILE ARG CYS VAL ASN LEU LEU GLU
SEQRES 7 C 366 ARG PRO THR GLU GLY SER VAL LEU VAL ASP GLY GLN GLU
SEQRES 8 C 366 LEU THR THR LEU SER GLU SER GLU LEU THR LYS ALA ARG
SEQRES 9 C 366 ARG GLN ILE GLY MET ILE PHE GLN HIS PHE ASN LEU LEU
SEQRES 10 C 366 SER SER ARG THR VAL PHE GLY ASN VAL ALA LEU PRO LEU
SEQRES 11 C 366 GLU LEU ASP ASN THR PRO LYS ASP GLU VAL LYS ARG ARG
SEQRES 12 C 366 VAL THR GLU LEU LEU SER LEU VAL GLY LEU GLY ASP LYS
SEQRES 13 C 366 HIS ASP SER TYR PRO SER ASN LEU SER GLY GLY GLN LYS
SEQRES 14 C 366 GLN ARG VAL ALA ILE ALA ARG ALA LEU ALA SER ASN PRO
SEQRES 15 C 366 LYS VAL LEU LEU CYS ASP GLN ALA THR SER ALA LEU ASP
SEQRES 16 C 366 PRO ALA THR THR ARG SER ILE LEU GLU LEU LEU LYS ASP
SEQRES 17 C 366 ILE ASN ARG ARG LEU GLY LEU THR ILE LEU LEU ILE THR
SEQRES 18 C 366 HIS GLU MET ASP VAL VAL LYS ARG ILE CYS ASP CYS VAL
SEQRES 19 C 366 ALA VAL ILE SER ASN GLY GLU LEU ILE GLU GLN ASP THR
SEQRES 20 C 366 VAL SER GLU VAL PHE SER HIS PRO LYS THR PRO LEU ALA
SEQRES 21 C 366 GLN LYS PHE ILE GLN SER THR LEU HIS LEU ASP ILE PRO
SEQRES 22 C 366 GLU ASP TYR GLN GLU ARG LEU GLN ALA GLU PRO PHE THR
SEQRES 23 C 366 ASP CYS VAL PRO MET LEU ARG LEU GLU PHE THR GLY GLN
SEQRES 24 C 366 SER VAL ASP ALA PRO LEU LEU SER GLU THR ALA ARG ARG
SEQRES 25 C 366 PHE ASN VAL ASN ASN ASN ILE ILE SER ALA GLN MET ASP
SEQRES 26 C 366 TYR ALA GLY GLY VAL LYS PHE GLY ILE MET LEU THR GLU
SEQRES 27 C 366 MET HIS GLY THR GLN GLN ASP THR GLN ALA ALA ILE ALA
SEQRES 28 C 366 TRP LEU GLN GLU HIS HIS VAL LYS VAL GLU VAL LEU GLY
SEQRES 29 C 366 TYR VAL
SEQRES 1 D 366 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 D 366 SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET ILE LYS
SEQRES 3 D 366 LEU SER ASN ILE THR LYS VAL PHE HIS GLN GLY THR ARG
SEQRES 4 D 366 THR ILE GLN ALA LEU ASN ASN VAL SER LEU HIS VAL PRO
SEQRES 5 D 366 ALA GLY GLN ILE TYR GLY VAL ILE GLY ALA SER GLY ALA
SEQRES 6 D 366 GLY LYS SER THR LEU ILE ARG CYS VAL ASN LEU LEU GLU
SEQRES 7 D 366 ARG PRO THR GLU GLY SER VAL LEU VAL ASP GLY GLN GLU
SEQRES 8 D 366 LEU THR THR LEU SER GLU SER GLU LEU THR LYS ALA ARG
SEQRES 9 D 366 ARG GLN ILE GLY MET ILE PHE GLN HIS PHE ASN LEU LEU
SEQRES 10 D 366 SER SER ARG THR VAL PHE GLY ASN VAL ALA LEU PRO LEU
SEQRES 11 D 366 GLU LEU ASP ASN THR PRO LYS ASP GLU VAL LYS ARG ARG
SEQRES 12 D 366 VAL THR GLU LEU LEU SER LEU VAL GLY LEU GLY ASP LYS
SEQRES 13 D 366 HIS ASP SER TYR PRO SER ASN LEU SER GLY GLY GLN LYS
SEQRES 14 D 366 GLN ARG VAL ALA ILE ALA ARG ALA LEU ALA SER ASN PRO
SEQRES 15 D 366 LYS VAL LEU LEU CYS ASP GLN ALA THR SER ALA LEU ASP
SEQRES 16 D 366 PRO ALA THR THR ARG SER ILE LEU GLU LEU LEU LYS ASP
SEQRES 17 D 366 ILE ASN ARG ARG LEU GLY LEU THR ILE LEU LEU ILE THR
SEQRES 18 D 366 HIS GLU MET ASP VAL VAL LYS ARG ILE CYS ASP CYS VAL
SEQRES 19 D 366 ALA VAL ILE SER ASN GLY GLU LEU ILE GLU GLN ASP THR
SEQRES 20 D 366 VAL SER GLU VAL PHE SER HIS PRO LYS THR PRO LEU ALA
SEQRES 21 D 366 GLN LYS PHE ILE GLN SER THR LEU HIS LEU ASP ILE PRO
SEQRES 22 D 366 GLU ASP TYR GLN GLU ARG LEU GLN ALA GLU PRO PHE THR
SEQRES 23 D 366 ASP CYS VAL PRO MET LEU ARG LEU GLU PHE THR GLY GLN
SEQRES 24 D 366 SER VAL ASP ALA PRO LEU LEU SER GLU THR ALA ARG ARG
SEQRES 25 D 366 PHE ASN VAL ASN ASN ASN ILE ILE SER ALA GLN MET ASP
SEQRES 26 D 366 TYR ALA GLY GLY VAL LYS PHE GLY ILE MET LEU THR GLU
SEQRES 27 D 366 MET HIS GLY THR GLN GLN ASP THR GLN ALA ALA ILE ALA
SEQRES 28 D 366 TRP LEU GLN GLU HIS HIS VAL LYS VAL GLU VAL LEU GLY
SEQRES 29 D 366 TYR VAL
SEQRES 1 E 217 MET SER GLU PRO MET MET TRP LEU LEU VAL ARG GLY VAL
SEQRES 2 E 217 TRP GLU THR LEU ALA MET THR PHE VAL SER GLY PHE PHE
SEQRES 3 E 217 GLY PHE VAL ILE GLY LEU PRO VAL GLY VAL LEU LEU TYR
SEQRES 4 E 217 VAL THR ARG PRO GLY GLN ILE ILE ALA ASN ALA LYS LEU
SEQRES 5 E 217 TYR ARG THR VAL SER ALA ILE VAL ASN ILE PHE ARG SER
SEQRES 6 E 217 ILE PRO PHE ILE ILE LEU LEU VAL TRP MET ILE PRO PHE
SEQRES 7 E 217 THR ARG VAL ILE VAL GLY THR SER ILE GLY LEU GLN ALA
SEQRES 8 E 217 ALA ILE VAL PRO LEU THR VAL GLY ALA ALA PRO PHE ILE
SEQRES 9 E 217 ALA ARG MET VAL GLU ASN ALA LEU LEU GLU ILE PRO THR
SEQRES 10 E 217 GLY LEU ILE GLU ALA SER ARG ALA MET GLY ALA THR PRO
SEQRES 11 E 217 MET GLN ILE VAL ARG LYS VAL LEU LEU PRO GLU ALA LEU
SEQRES 12 E 217 PRO GLY LEU VAL ASN ALA ALA THR ILE THR LEU ILE THR
SEQRES 13 E 217 LEU VAL GLY TYR SER ALA MET GLY GLY ALA VAL GLY ALA
SEQRES 14 E 217 GLY GLY LEU GLY GLN ILE GLY TYR GLN TYR GLY TYR ILE
SEQRES 15 E 217 GLY TYR ASN ALA THR VAL MET ASN THR VAL LEU VAL LEU
SEQRES 16 E 217 LEU VAL ILE LEU VAL TYR LEU ILE GLN PHE ALA GLY ASP
SEQRES 17 E 217 ARG ILE VAL ARG ALA VAL THR ARG LYS
SEQRES 1 F 217 MET SER GLU PRO MET MET TRP LEU LEU VAL ARG GLY VAL
SEQRES 2 F 217 TRP GLU THR LEU ALA MET THR PHE VAL SER GLY PHE PHE
SEQRES 3 F 217 GLY PHE VAL ILE GLY LEU PRO VAL GLY VAL LEU LEU TYR
SEQRES 4 F 217 VAL THR ARG PRO GLY GLN ILE ILE ALA ASN ALA LYS LEU
SEQRES 5 F 217 TYR ARG THR VAL SER ALA ILE VAL ASN ILE PHE ARG SER
SEQRES 6 F 217 ILE PRO PHE ILE ILE LEU LEU VAL TRP MET ILE PRO PHE
SEQRES 7 F 217 THR ARG VAL ILE VAL GLY THR SER ILE GLY LEU GLN ALA
SEQRES 8 F 217 ALA ILE VAL PRO LEU THR VAL GLY ALA ALA PRO PHE ILE
SEQRES 9 F 217 ALA ARG MET VAL GLU ASN ALA LEU LEU GLU ILE PRO THR
SEQRES 10 F 217 GLY LEU ILE GLU ALA SER ARG ALA MET GLY ALA THR PRO
SEQRES 11 F 217 MET GLN ILE VAL ARG LYS VAL LEU LEU PRO GLU ALA LEU
SEQRES 12 F 217 PRO GLY LEU VAL ASN ALA ALA THR ILE THR LEU ILE THR
SEQRES 13 F 217 LEU VAL GLY TYR SER ALA MET GLY GLY ALA VAL GLY ALA
SEQRES 14 F 217 GLY GLY LEU GLY GLN ILE GLY TYR GLN TYR GLY TYR ILE
SEQRES 15 F 217 GLY TYR ASN ALA THR VAL MET ASN THR VAL LEU VAL LEU
SEQRES 16 F 217 LEU VAL ILE LEU VAL TYR LEU ILE GLN PHE ALA GLY ASP
SEQRES 17 F 217 ARG ILE VAL ARG ALA VAL THR ARG LYS
SEQRES 1 G 366 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 G 366 SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET ILE LYS
SEQRES 3 G 366 LEU SER ASN ILE THR LYS VAL PHE HIS GLN GLY THR ARG
SEQRES 4 G 366 THR ILE GLN ALA LEU ASN ASN VAL SER LEU HIS VAL PRO
SEQRES 5 G 366 ALA GLY GLN ILE TYR GLY VAL ILE GLY ALA SER GLY ALA
SEQRES 6 G 366 GLY LYS SER THR LEU ILE ARG CYS VAL ASN LEU LEU GLU
SEQRES 7 G 366 ARG PRO THR GLU GLY SER VAL LEU VAL ASP GLY GLN GLU
SEQRES 8 G 366 LEU THR THR LEU SER GLU SER GLU LEU THR LYS ALA ARG
SEQRES 9 G 366 ARG GLN ILE GLY MET ILE PHE GLN HIS PHE ASN LEU LEU
SEQRES 10 G 366 SER SER ARG THR VAL PHE GLY ASN VAL ALA LEU PRO LEU
SEQRES 11 G 366 GLU LEU ASP ASN THR PRO LYS ASP GLU VAL LYS ARG ARG
SEQRES 12 G 366 VAL THR GLU LEU LEU SER LEU VAL GLY LEU GLY ASP LYS
SEQRES 13 G 366 HIS ASP SER TYR PRO SER ASN LEU SER GLY GLY GLN LYS
SEQRES 14 G 366 GLN ARG VAL ALA ILE ALA ARG ALA LEU ALA SER ASN PRO
SEQRES 15 G 366 LYS VAL LEU LEU CYS ASP GLN ALA THR SER ALA LEU ASP
SEQRES 16 G 366 PRO ALA THR THR ARG SER ILE LEU GLU LEU LEU LYS ASP
SEQRES 17 G 366 ILE ASN ARG ARG LEU GLY LEU THR ILE LEU LEU ILE THR
SEQRES 18 G 366 HIS GLU MET ASP VAL VAL LYS ARG ILE CYS ASP CYS VAL
SEQRES 19 G 366 ALA VAL ILE SER ASN GLY GLU LEU ILE GLU GLN ASP THR
SEQRES 20 G 366 VAL SER GLU VAL PHE SER HIS PRO LYS THR PRO LEU ALA
SEQRES 21 G 366 GLN LYS PHE ILE GLN SER THR LEU HIS LEU ASP ILE PRO
SEQRES 22 G 366 GLU ASP TYR GLN GLU ARG LEU GLN ALA GLU PRO PHE THR
SEQRES 23 G 366 ASP CYS VAL PRO MET LEU ARG LEU GLU PHE THR GLY GLN
SEQRES 24 G 366 SER VAL ASP ALA PRO LEU LEU SER GLU THR ALA ARG ARG
SEQRES 25 G 366 PHE ASN VAL ASN ASN ASN ILE ILE SER ALA GLN MET ASP
SEQRES 26 G 366 TYR ALA GLY GLY VAL LYS PHE GLY ILE MET LEU THR GLU
SEQRES 27 G 366 MET HIS GLY THR GLN GLN ASP THR GLN ALA ALA ILE ALA
SEQRES 28 G 366 TRP LEU GLN GLU HIS HIS VAL LYS VAL GLU VAL LEU GLY
SEQRES 29 G 366 TYR VAL
SEQRES 1 H 366 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 H 366 SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET ILE LYS
SEQRES 3 H 366 LEU SER ASN ILE THR LYS VAL PHE HIS GLN GLY THR ARG
SEQRES 4 H 366 THR ILE GLN ALA LEU ASN ASN VAL SER LEU HIS VAL PRO
SEQRES 5 H 366 ALA GLY GLN ILE TYR GLY VAL ILE GLY ALA SER GLY ALA
SEQRES 6 H 366 GLY LYS SER THR LEU ILE ARG CYS VAL ASN LEU LEU GLU
SEQRES 7 H 366 ARG PRO THR GLU GLY SER VAL LEU VAL ASP GLY GLN GLU
SEQRES 8 H 366 LEU THR THR LEU SER GLU SER GLU LEU THR LYS ALA ARG
SEQRES 9 H 366 ARG GLN ILE GLY MET ILE PHE GLN HIS PHE ASN LEU LEU
SEQRES 10 H 366 SER SER ARG THR VAL PHE GLY ASN VAL ALA LEU PRO LEU
SEQRES 11 H 366 GLU LEU ASP ASN THR PRO LYS ASP GLU VAL LYS ARG ARG
SEQRES 12 H 366 VAL THR GLU LEU LEU SER LEU VAL GLY LEU GLY ASP LYS
SEQRES 13 H 366 HIS ASP SER TYR PRO SER ASN LEU SER GLY GLY GLN LYS
SEQRES 14 H 366 GLN ARG VAL ALA ILE ALA ARG ALA LEU ALA SER ASN PRO
SEQRES 15 H 366 LYS VAL LEU LEU CYS ASP GLN ALA THR SER ALA LEU ASP
SEQRES 16 H 366 PRO ALA THR THR ARG SER ILE LEU GLU LEU LEU LYS ASP
SEQRES 17 H 366 ILE ASN ARG ARG LEU GLY LEU THR ILE LEU LEU ILE THR
SEQRES 18 H 366 HIS GLU MET ASP VAL VAL LYS ARG ILE CYS ASP CYS VAL
SEQRES 19 H 366 ALA VAL ILE SER ASN GLY GLU LEU ILE GLU GLN ASP THR
SEQRES 20 H 366 VAL SER GLU VAL PHE SER HIS PRO LYS THR PRO LEU ALA
SEQRES 21 H 366 GLN LYS PHE ILE GLN SER THR LEU HIS LEU ASP ILE PRO
SEQRES 22 H 366 GLU ASP TYR GLN GLU ARG LEU GLN ALA GLU PRO PHE THR
SEQRES 23 H 366 ASP CYS VAL PRO MET LEU ARG LEU GLU PHE THR GLY GLN
SEQRES 24 H 366 SER VAL ASP ALA PRO LEU LEU SER GLU THR ALA ARG ARG
SEQRES 25 H 366 PHE ASN VAL ASN ASN ASN ILE ILE SER ALA GLN MET ASP
SEQRES 26 H 366 TYR ALA GLY GLY VAL LYS PHE GLY ILE MET LEU THR GLU
SEQRES 27 H 366 MET HIS GLY THR GLN GLN ASP THR GLN ALA ALA ILE ALA
SEQRES 28 H 366 TRP LEU GLN GLU HIS HIS VAL LYS VAL GLU VAL LEU GLY
SEQRES 29 H 366 TYR VAL
HET ADP C2500 27
HET ADP D2501 27
HET ADP G2503 27
HET ADP H2502 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 9 ADP 4(C10 H15 N5 O10 P2)
FORMUL 13 HOH *146(H2 O)
HELIX 1 1 SER A 2 THR A 41 1 40
HELIX 2 2 ASN A 49 SER A 65 1 17
HELIX 3 3 PRO A 67 MET A 75 1 9
HELIX 4 4 MET A 75 GLY A 84 1 10
HELIX 5 5 GLY A 88 LEU A 113 1 26
HELIX 6 6 THR A 117 MET A 126 1 10
HELIX 7 7 THR A 129 VAL A 137 1 9
HELIX 8 8 VAL A 137 GLY A 164 1 28
HELIX 9 9 GLY A 170 TYR A 181 1 12
HELIX 10 10 ASN A 185 ARG A 212 1 28
HELIX 11 11 SER B 2 ARG B 42 1 41
HELIX 12 12 ASN B 49 ILE B 66 1 18
HELIX 13 13 PRO B 67 GLY B 84 1 18
HELIX 14 14 GLY B 88 LEU B 113 1 26
HELIX 15 15 GLY B 118 ALA B 125 1 8
HELIX 16 16 THR B 129 VAL B 137 1 9
HELIX 17 17 VAL B 137 GLY B 164 1 28
HELIX 18 18 GLY B 171 ILE B 182 1 12
HELIX 19 19 ASN B 185 THR B 215 1 31
HELIX 20 20 GLY C 43 ASN C 52 1 10
HELIX 21 21 SER C 73 ARG C 82 1 10
HELIX 22 22 THR C 98 ASP C 110 1 13
HELIX 23 23 PRO C 113 VAL C 128 1 16
HELIX 24 24 LEU C 130 HIS C 134 5 5
HELIX 25 25 SER C 142 LEU C 155 1 14
HELIX 26 26 ASP C 172 LEU C 190 1 19
HELIX 27 27 GLU C 200 CYS C 208 1 9
HELIX 28 28 THR C 224 SER C 230 1 7
HELIX 29 29 THR C 234 LEU C 245 1 12
HELIX 30 30 PRO C 250 LEU C 257 1 8
HELIX 31 31 GLY C 275 ASP C 279 1 5
HELIX 32 32 PRO C 281 ASN C 291 1 11
HELIX 33 33 THR C 319 HIS C 333 1 15
HELIX 34 34 HIS D 12 ARG D 16 5 5
HELIX 35 35 GLY D 43 ASN D 52 1 10
HELIX 36 36 SER D 73 ARG D 81 1 9
HELIX 37 37 THR D 98 ASP D 110 1 13
HELIX 38 38 PRO D 113 VAL D 128 1 16
HELIX 39 39 TYR D 137 LEU D 141 5 5
HELIX 40 40 SER D 142 ALA D 156 1 15
HELIX 41 41 ASP D 172 GLY D 191 1 20
HELIX 42 42 GLU D 200 CYS D 208 1 9
HELIX 43 43 VAL D 225 HIS D 231 1 7
HELIX 44 44 THR D 234 LEU D 245 1 12
HELIX 45 45 PRO D 250 LEU D 257 1 8
HELIX 46 46 GLY D 275 ALA D 280 1 6
HELIX 47 47 PRO D 281 PHE D 290 1 10
HELIX 48 48 THR D 319 HIS D 333 1 15
HELIX 49 49 SER E 2 THR E 41 1 40
HELIX 50 50 ASN E 49 ILE E 66 1 18
HELIX 51 51 PRO E 67 MET E 75 1 9
HELIX 52 52 MET E 75 GLY E 84 1 10
HELIX 53 53 GLY E 88 LEU E 113 1 26
HELIX 54 54 THR E 117 MET E 126 1 10
HELIX 55 55 THR E 129 VAL E 137 1 9
HELIX 56 56 VAL E 137 GLY E 165 1 29
HELIX 57 57 ALA E 166 GLY E 168 5 3
HELIX 58 58 GLY E 170 TYR E 179 1 10
HELIX 59 59 ASN E 185 THR E 215 1 31
HELIX 60 60 SER F 2 THR F 41 1 40
HELIX 61 61 ASN F 49 SER F 65 1 17
HELIX 62 62 PRO F 67 VAL F 83 1 17
HELIX 63 63 GLY F 88 LEU F 113 1 26
HELIX 64 64 THR F 117 MET F 126 1 10
HELIX 65 65 THR F 129 VAL F 137 1 9
HELIX 66 66 VAL F 137 VAL F 167 1 31
HELIX 67 67 GLY F 170 ILE F 182 1 13
HELIX 68 68 ASN F 185 THR F 215 1 31
HELIX 69 69 GLY G 43 LEU G 53 1 11
HELIX 70 70 SER G 75 ARG G 82 1 8
HELIX 71 71 THR G 98 ASP G 110 1 13
HELIX 72 72 PRO G 113 VAL G 128 1 16
HELIX 73 73 SER G 142 SER G 157 1 16
HELIX 74 74 ASP G 172 GLY G 191 1 20
HELIX 75 75 GLU G 200 CYS G 208 1 9
HELIX 76 76 VAL G 225 HIS G 231 1 7
HELIX 77 77 THR G 234 LEU G 245 1 12
HELIX 78 78 PRO G 250 LEU G 257 1 8
HELIX 79 79 GLY G 275 ALA G 280 1 6
HELIX 80 80 PRO G 281 ASN G 291 1 11
HELIX 81 81 THR G 319 HIS G 333 1 15
HELIX 82 82 GLY H 43 ASN H 52 1 10
HELIX 83 83 SER H 73 ARG H 82 1 10
HELIX 84 84 PHE H 100 LEU H 109 1 10
HELIX 85 85 PRO H 113 VAL H 128 1 16
HELIX 86 86 SER H 142 LEU H 155 1 14
HELIX 87 87 ALA H 156 ASN H 158 5 3
HELIX 88 88 ASP H 172 LEU H 190 1 19
HELIX 89 89 GLU H 200 CYS H 208 1 9
HELIX 90 90 VAL H 225 HIS H 231 1 7
HELIX 91 91 THR H 234 SER H 243 1 10
HELIX 92 92 PRO H 250 GLU H 255 1 6
HELIX 93 93 GLY H 275 VAL H 278 5 4
HELIX 94 94 PRO H 281 PHE H 290 1 10
HELIX 95 95 THR H 319 HIS H 333 1 15
SHEET 1 A 4 THR C 17 VAL C 28 0
SHEET 2 A 4 ILE C 2 HIS C 12 -1 N ILE C 7 O VAL C 24
SHEET 3 A 4 GLU C 59 VAL C 64 -1 O GLU C 59 N THR C 8
SHEET 4 A 4 GLN C 67 GLU C 68 -1 O GLN C 67 N VAL C 64
SHEET 1 B 6 ILE C 84 ILE C 87 0
SHEET 2 B 6 VAL C 161 ASP C 165 1 O LEU C 163 N GLY C 85
SHEET 3 B 6 THR C 193 THR C 198 1 O THR C 193 N LEU C 162
SHEET 4 B 6 ILE C 33 ILE C 37 1 N VAL C 36 O LEU C 196
SHEET 5 B 6 CYS C 210 SER C 215 1 O ILE C 214 N ILE C 37
SHEET 6 B 6 GLU C 218 GLU C 221 -1 O GLU C 218 N SER C 215
SHEET 1 C 8 VAL C 335 TYR C 342 0
SHEET 2 C 8 PRO C 267 THR C 274 -1 N ARG C 270 O GLU C 338
SHEET 3 C 8 LYS C 308 HIS C 317 -1 O MET C 312 N LEU C 271
SHEET 4 C 8 ASN C 293 TYR C 303 -1 N ASN C 293 O HIS C 317
SHEET 5 C 8 ASN D 293 ALA D 304 -1 O ALA D 299 N ALA C 299
SHEET 6 C 8 VAL D 307 HIS D 317 -1 O LEU D 313 N SER D 298
SHEET 7 C 8 VAL D 266 THR D 274 -1 N LEU D 271 O MET D 312
SHEET 8 C 8 LYS D 336 VAL D 343 -1 O GLY D 341 N MET D 268
SHEET 1 D 4 ILE D 18 VAL D 28 0
SHEET 2 D 4 ILE D 2 PHE D 11 -1 N ILE D 7 O VAL D 24
SHEET 3 D 4 GLU D 59 VAL D 64 -1 O GLU D 59 N THR D 8
SHEET 4 D 4 GLN D 67 GLU D 68 -1 O GLN D 67 N VAL D 64
SHEET 1 E 6 ILE D 84 ILE D 87 0
SHEET 2 E 6 VAL D 161 ASP D 165 1 O LEU D 163 N GLY D 85
SHEET 3 E 6 THR D 193 THR D 198 1 O LEU D 195 N CYS D 164
SHEET 4 E 6 ILE D 33 GLY D 38 1 N TYR D 34 O ILE D 194
SHEET 5 E 6 CYS D 210 SER D 215 1 O CYS D 210 N GLY D 35
SHEET 6 E 6 GLU D 218 THR D 224 -1 O GLU D 218 N SER D 215
SHEET 1 F 4 ARG G 16 HIS G 27 0
SHEET 2 F 4 LYS G 3 GLN G 13 -1 N PHE G 11 O ILE G 18
SHEET 3 F 4 GLU G 59 VAL G 64 -1 O GLU G 59 N THR G 8
SHEET 4 F 4 GLN G 67 GLU G 68 -1 O GLN G 67 N VAL G 64
SHEET 1 G 6 ILE G 84 PHE G 88 0
SHEET 2 G 6 VAL G 161 ASP G 165 1 O VAL G 161 N GLY G 85
SHEET 3 G 6 THR G 193 THR G 198 1 O ILE G 197 N CYS G 164
SHEET 4 G 6 ILE G 33 ILE G 37 1 N TYR G 34 O LEU G 196
SHEET 5 G 6 CYS G 210 SER G 215 1 O ILE G 214 N ILE G 37
SHEET 6 G 6 GLU G 218 THR G 224 -1 O GLU G 218 N SER G 215
SHEET 1 H 8 VAL G 335 TYR G 342 0
SHEET 2 H 8 PRO G 267 THR G 274 -1 N MET G 268 O GLY G 341
SHEET 3 H 8 VAL G 307 HIS G 317 -1 O THR G 314 N LEU G 269
SHEET 4 H 8 ASN G 293 ALA G 304 -1 N SER G 298 O LEU G 313
SHEET 5 H 8 ASN H 293 ALA H 304 -1 O ALA H 299 N ALA G 299
SHEET 6 H 8 VAL H 307 HIS H 317 -1 O LEU H 313 N ILE H 297
SHEET 7 H 8 PRO H 267 PHE H 273 -1 N PHE H 273 O GLY H 310
SHEET 8 H 8 VAL H 335 TYR H 342 -1 O LEU H 340 N MET H 268
SHEET 1 I 4 ARG H 16 VAL H 28 0
SHEET 2 I 4 ILE H 2 GLN H 13 -1 N LEU H 4 O LEU H 26
SHEET 3 I 4 GLU H 59 VAL H 64 -1 O SER H 61 N SER H 5
SHEET 4 I 4 GLN H 67 GLU H 68 -1 O GLN H 67 N VAL H 64
SHEET 1 J 6 ILE H 84 ILE H 87 0
SHEET 2 J 6 VAL H 161 ASP H 165 1 O LEU H 163 N GLY H 85
SHEET 3 J 6 THR H 193 THR H 198 1 O LEU H 195 N CYS H 164
SHEET 4 J 6 ILE H 33 ILE H 37 1 N TYR H 34 O ILE H 194
SHEET 5 J 6 CYS H 210 SER H 215 1 O ALA H 212 N GLY H 35
SHEET 6 J 6 GLU H 218 THR H 224 -1 O GLU H 221 N VAL H 213
SITE 1 AC1 9 PHE C 11 ALA C 39 SER C 40 GLY C 41
SITE 2 AC1 9 ALA C 42 GLY C 43 LYS C 44 SER C 45
SITE 3 AC1 9 THR C 46
SITE 1 AC2 10 PHE D 11 ALA D 20 ALA D 39 SER D 40
SITE 2 AC2 10 GLY D 41 ALA D 42 GLY D 43 LYS D 44
SITE 3 AC2 10 SER D 45 THR D 46
SITE 1 AC3 8 ALA G 20 SER G 40 GLY G 41 ALA G 42
SITE 2 AC3 8 GLY G 43 LYS G 44 SER G 45 THR G 46
SITE 1 AC4 9 PHE H 11 GLN H 13 ALA H 39 GLY H 41
SITE 2 AC4 9 ALA H 42 GLY H 43 LYS H 44 SER H 45
SITE 3 AC4 9 THR H 46
CRYST1 83.430 140.080 150.070 90.00 96.39 90.00 P 1 21 1 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 0.011986 0.000000 0.001342 0.00000
SCALE2 0.000000 0.007139 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
