HEADER ACETYLCHOLINE-BINDING PROTEIN 03-MAY-14 4QAA
TITLE X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP) IN COMPLEX
TITLE 2 WITH 6-(4-METHOXYPHENYL)-N4-OCTYLPYRIMIDINE-2,4-DIAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINE-BINDING PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 SYNONYM: ACH-BINDING PROTEIN, ACHBP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LYMNAEA STAGNALIS;
SOURCE 3 ORGANISM_COMMON: GREAT POND SNAIL;
SOURCE 4 ORGANISM_TAXID: 6523;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S-GNT1;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFLAG-CMV3
KEYWDS ACETYLCHOLINE-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KACZANOWSKA,M.HAREL,Z.RADIC,J.-P.CHANGEUX,M.G.FINN,P.TAYLOR
REVDAT 5 29-JUL-20 4QAA 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 24-JAN-18 4QAA 1 AUTHOR
REVDAT 3 13-AUG-14 4QAA 1 JRNL
REVDAT 2 30-JUL-14 4QAA 1 JRNL
REVDAT 1 16-JUL-14 4QAA 0
JRNL AUTH K.KACZANOWSKA,M.HAREL,Z.RADIC,J.P.CHANGEUX,M.G.FINN,P.TAYLOR
JRNL TITL STRUCTURAL BASIS FOR COOPERATIVE INTERACTIONS OF SUBSTITUTED
JRNL TITL 2 2-AMINOPYRIMIDINES WITH THE ACETYLCHOLINE BINDING PROTEIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 10749 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 25006260
JRNL DOI 10.1073/PNAS.1410992111
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 68911
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3486
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 49.6604 - 7.8847 0.99 2688 126 0.1971 0.2001
REMARK 3 2 7.8847 - 6.2623 1.00 2658 142 0.1911 0.2434
REMARK 3 3 6.2623 - 5.4718 1.00 2633 139 0.1835 0.2267
REMARK 3 4 5.4718 - 4.9720 1.00 2623 136 0.1756 0.2344
REMARK 3 5 4.9720 - 4.6159 1.00 2607 157 0.1616 0.2067
REMARK 3 6 4.6159 - 4.3440 1.00 2627 139 0.1723 0.2521
REMARK 3 7 4.3440 - 4.1265 1.00 2614 157 0.1748 0.2421
REMARK 3 8 4.1265 - 3.9470 1.00 2609 146 0.1867 0.3010
REMARK 3 9 3.9470 - 3.7951 1.00 2608 131 0.1844 0.2442
REMARK 3 10 3.7951 - 3.6642 1.00 2631 151 0.1896 0.2688
REMARK 3 11 3.6642 - 3.5496 1.00 2635 134 0.1815 0.2277
REMARK 3 12 3.5496 - 3.4482 1.00 2607 129 0.1908 0.2654
REMARK 3 13 3.4482 - 3.3574 1.00 2606 136 0.1993 0.3173
REMARK 3 14 3.3574 - 3.2755 1.00 2630 135 0.2089 0.2734
REMARK 3 15 3.2755 - 3.2011 1.00 2569 162 0.2138 0.3200
REMARK 3 16 3.2011 - 3.1330 1.00 2635 132 0.2159 0.3282
REMARK 3 17 3.1330 - 3.0703 1.00 2602 132 0.2167 0.3041
REMARK 3 18 3.0703 - 3.0124 1.00 2629 135 0.2032 0.3112
REMARK 3 19 3.0124 - 2.9586 1.00 2594 138 0.2178 0.3242
REMARK 3 20 2.9586 - 2.9084 1.00 2620 129 0.2312 0.3262
REMARK 3 21 2.9084 - 2.8615 1.00 2588 132 0.2284 0.3326
REMARK 3 22 2.8615 - 2.8175 1.00 2624 134 0.2255 0.3034
REMARK 3 23 2.8175 - 2.7761 1.00 2560 148 0.2433 0.3244
REMARK 3 24 2.7761 - 2.7370 1.00 2649 147 0.2485 0.3398
REMARK 3 25 2.7370 - 2.7000 1.00 2579 139 0.2438 0.3426
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.008 17515
REMARK 3 ANGLE : 1.216 23827
REMARK 3 CHIRALITY : 0.080 2672
REMARK 3 PLANARITY : 0.005 3041
REMARK 3 DIHEDRAL : 17.822 6496
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 4QAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000085801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI-111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.15300
REMARK 200 R SYM (I) : 0.15300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: 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 (%): 52.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.26 M AMMONIUM PHOSPHATE MONOBASIC,
REMARK 280 35% V/V GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 290K, PH 5
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 64.96700
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, I, J
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 THR A 184
REMARK 465 TYR A 185
REMARK 465 SER A 186
REMARK 465 CYS A 187
REMARK 465 CYS A 188
REMARK 465 PRO A 189
REMARK 465 ARG A 206
REMARK 465 SER A 207
REMARK 465 GLU A 208
REMARK 465 ILE A 209
REMARK 465 ASP B -7
REMARK 465 TYR B -6
REMARK 465 TYR B 185
REMARK 465 SER B 186
REMARK 465 CYS B 187
REMARK 465 CYS B 188
REMARK 465 ARG B 206
REMARK 465 SER B 207
REMARK 465 GLU B 208
REMARK 465 ILE B 209
REMARK 465 TYR C 185
REMARK 465 SER C 186
REMARK 465 CYS C 187
REMARK 465 CYS C 188
REMARK 465 ARG C 206
REMARK 465 SER C 207
REMARK 465 GLU C 208
REMARK 465 ILE C 209
REMARK 465 ARG D 206
REMARK 465 SER D 207
REMARK 465 GLU D 208
REMARK 465 ILE D 209
REMARK 465 THR E 156
REMARK 465 GLU E 157
REMARK 465 ASN E 158
REMARK 465 TYR E 185
REMARK 465 SER E 186
REMARK 465 CYS E 187
REMARK 465 CYS E 188
REMARK 465 PRO E 189
REMARK 465 ARG E 206
REMARK 465 SER E 207
REMARK 465 GLU E 208
REMARK 465 ILE E 209
REMARK 465 THR F 156
REMARK 465 TYR F 185
REMARK 465 SER F 186
REMARK 465 CYS F 187
REMARK 465 ARG F 206
REMARK 465 SER F 207
REMARK 465 GLU F 208
REMARK 465 ILE F 209
REMARK 465 ASP G 160
REMARK 465 ASP G 161
REMARK 465 SER G 186
REMARK 465 CYS G 187
REMARK 465 CYS G 188
REMARK 465 ARG G 206
REMARK 465 SER G 207
REMARK 465 GLU G 208
REMARK 465 ILE G 209
REMARK 465 THR H 156
REMARK 465 GLU H 157
REMARK 465 ASN H 158
REMARK 465 SER H 159
REMARK 465 CYS H 187
REMARK 465 CYS H 188
REMARK 465 ARG H 206
REMARK 465 SER H 207
REMARK 465 GLU H 208
REMARK 465 ILE H 209
REMARK 465 THR I 156
REMARK 465 GLU I 157
REMARK 465 ASN I 158
REMARK 465 SER I 186
REMARK 465 CYS I 187
REMARK 465 CYS I 188
REMARK 465 ARG I 206
REMARK 465 SER I 207
REMARK 465 GLU I 208
REMARK 465 ILE I 209
REMARK 465 VAL J 183
REMARK 465 THR J 184
REMARK 465 TYR J 185
REMARK 465 SER J 186
REMARK 465 CYS J 187
REMARK 465 CYS J 188
REMARK 465 PRO J 189
REMARK 465 ARG J 206
REMARK 465 SER J 207
REMARK 465 GLU J 208
REMARK 465 ILE J 209
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 HIS A 69 21.56 -141.16
REMARK 500 HIS D 69 30.21 -160.43
REMARK 500 HIS H 69 28.74 -145.17
REMARK 500 HIS J 69 20.35 -143.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 KK1 G 301
REMARK 610 KK1 H 301
REMARK 610 KK1 J 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UX2 RELATED DB: PDB
REMARK 900 RELATED ID: 1UW6 RELATED DB: PDB
REMARK 900 RELATED ID: 1UV6 RELATED DB: PDB
REMARK 900 RELATED ID: 4QAB RELATED DB: PDB
REMARK 900 RELATED ID: 4QAC RELATED DB: PDB
DBREF 4QAA A 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA B 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA C 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA D 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA E 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA F 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA G 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA H 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA I 1 209 UNP P58154 ACHP_LYMST 20 228
DBREF 4QAA J 1 209 UNP P58154 ACHP_LYMST 20 228
SEQADV 4QAA ASP A -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR A -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS A -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP A -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP A -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP A -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP A -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS A 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP B -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR B -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS B -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP B -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP B -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP B -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP B -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS B 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP C -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR C -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS C -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP C -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP C -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP C -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP C -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS C 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP D -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR D -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS D -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP D -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP D -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP D -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP D -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS D 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP E -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR E -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS E -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP E -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP E -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP E -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP E -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS E 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP F -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR F -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS F -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP F -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP F -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP F -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP F -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS F 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP G -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR G -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS G -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP G -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP G -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP G -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP G -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS G 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP H -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR H -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS H -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP H -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP H -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP H -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP H -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS H 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP I -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR I -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS I -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP I -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP I -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP I -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP I -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS I 0 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP J -7 UNP P58154 EXPRESSION TAG
SEQADV 4QAA TYR J -6 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS J -5 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP J -4 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP J -3 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP J -2 UNP P58154 EXPRESSION TAG
SEQADV 4QAA ASP J -1 UNP P58154 EXPRESSION TAG
SEQADV 4QAA LYS J 0 UNP P58154 EXPRESSION TAG
SEQRES 1 A 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 A 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 A 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 A 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 A 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 A 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 A 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 A 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 A 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 A 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 A 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 A 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 A 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 A 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 A 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 A 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 A 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 B 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 B 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 B 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 B 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 B 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 B 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 B 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 B 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 B 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 B 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 B 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 B 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 B 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 B 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 B 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 B 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 B 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 C 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 C 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 C 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 C 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 C 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 C 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 C 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 C 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 C 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 C 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 C 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 C 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 C 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 C 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 C 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 C 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 C 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 D 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 D 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 D 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 D 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 D 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 D 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 D 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 D 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 D 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 D 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 D 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 D 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 D 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 D 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 D 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 D 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 D 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 E 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 E 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 E 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 E 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 E 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 E 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 E 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 E 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 E 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 E 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 E 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 E 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 E 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 E 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 E 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 E 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 E 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 F 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 F 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 F 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 F 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 F 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 F 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 F 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 F 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 F 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 F 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 F 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 F 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 F 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 F 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 F 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 F 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 F 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 G 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 G 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 G 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 G 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 G 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 G 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 G 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 G 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 G 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 G 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 G 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 G 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 G 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 G 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 G 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 G 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 G 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 H 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 H 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 H 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 H 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 H 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 H 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 H 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 H 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 H 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 H 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 H 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 H 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 H 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 H 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 H 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 H 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 H 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 I 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 I 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 I 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 I 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 I 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 I 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 I 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 I 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 I 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 I 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 I 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 I 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 I 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 I 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 I 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 I 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 I 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
SEQRES 1 J 217 ASP TYR LYS ASP ASP ASP ASP LYS LEU ASP ARG ALA ASP
SEQRES 2 J 217 ILE LEU TYR ASN ILE ARG GLN THR SER ARG PRO ASP VAL
SEQRES 3 J 217 ILE PRO THR GLN ARG ASP ARG PRO VAL ALA VAL SER VAL
SEQRES 4 J 217 SER LEU LYS PHE ILE ASN ILE LEU GLU VAL ASN GLU ILE
SEQRES 5 J 217 THR ASN GLU VAL ASP VAL VAL PHE TRP GLN GLN THR THR
SEQRES 6 J 217 TRP SER ASP ARG THR LEU ALA TRP ASN SER SER HIS SER
SEQRES 7 J 217 PRO ASP GLN VAL SER VAL PRO ILE SER SER LEU TRP VAL
SEQRES 8 J 217 PRO ASP LEU ALA ALA TYR ASN ALA ILE SER LYS PRO GLU
SEQRES 9 J 217 VAL LEU THR PRO GLN LEU ALA ARG VAL VAL SER ASP GLY
SEQRES 10 J 217 GLU VAL LEU TYR MET PRO SER ILE ARG GLN ARG PHE SER
SEQRES 11 J 217 CYS ASP VAL SER GLY VAL ASP THR GLU SER GLY ALA THR
SEQRES 12 J 217 CYS ARG ILE LYS ILE GLY SER TRP THR HIS HIS SER ARG
SEQRES 13 J 217 GLU ILE SER VAL ASP PRO THR THR GLU ASN SER ASP ASP
SEQRES 14 J 217 SER GLU TYR PHE SER GLN TYR SER ARG PHE GLU ILE LEU
SEQRES 15 J 217 ASP VAL THR GLN LYS LYS ASN SER VAL THR TYR SER CYS
SEQRES 16 J 217 CYS PRO GLU ALA TYR GLU ASP VAL GLU VAL SER LEU ASN
SEQRES 17 J 217 PHE ARG LYS LYS GLY ARG SER GLU ILE
MODRES 4QAA ASN J 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN B 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN A 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN E 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN F 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN G 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN I 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN C 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN D 66 ASN GLYCOSYLATION SITE
MODRES 4QAA ASN H 66 ASN GLYCOSYLATION SITE
HET KK1 A 301 24
HET NAG A 302 14
HET PO4 A 303 5
HET PO4 A 304 5
HET PO4 A 305 5
HET KK1 B 301 24
HET NAG B 302 14
HET PO4 B 303 5
HET KK1 C 301 24
HET NAG C 302 14
HET PO4 C 303 5
HET PO4 C 304 5
HET PO4 C 305 5
HET KK1 D 301 24
HET NAG D 302 14
HET PO4 D 303 5
HET PO4 D 304 5
HET KK1 E 301 24
HET NAG E 302 14
HET PO4 E 303 5
HET PO4 E 304 5
HET PO4 E 305 5
HET KK1 F 301 24
HET NAG F 302 14
HET PO4 F 303 5
HET PO4 F 304 5
HET KK1 G 301 16
HET NAG G 302 14
HET PO4 G 303 5
HET PO4 G 304 5
HET KK1 H 301 16
HET NAG H 302 14
HET PO4 H 303 5
HET PO4 H 304 5
HET KK1 I 301 24
HET NAG I 302 14
HET KK1 J 301 16
HET NAG J 302 14
HET PO4 J 303 5
HETNAM KK1 6-(4-METHOXYPHENYL)-N~4~-OCTYLPYRIMIDINE-2,4-DIAMINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PO4 PHOSPHATE ION
FORMUL 11 KK1 10(C19 H28 N4 O)
FORMUL 12 NAG 10(C8 H15 N O6)
FORMUL 13 PO4 19(O4 P 3-)
FORMUL 50 HOH *161(H2 O)
HELIX 1 1 ASP A -1 SER A 14 1 16
HELIX 2 2 ARG A 61 ALA A 64 5 4
HELIX 3 3 SER A 79 LEU A 81 5 3
HELIX 4 4 ASP B -1 SER B 14 1 16
HELIX 5 5 ARG B 61 ALA B 64 5 4
HELIX 6 6 SER B 79 LEU B 81 5 3
HELIX 7 7 ASP C -7 ASP C -3 5 5
HELIX 8 8 ASP C -1 SER C 14 1 16
HELIX 9 9 ARG C 61 ALA C 64 5 4
HELIX 10 10 SER C 79 LEU C 81 5 3
HELIX 11 11 ASP D -7 ASP D -3 5 5
HELIX 12 12 ASP D -1 SER D 14 1 16
HELIX 13 13 ARG D 61 ALA D 64 5 4
HELIX 14 14 SER D 79 LEU D 81 5 3
HELIX 15 15 ASP E -7 ASP E -3 5 5
HELIX 16 16 ASP E -1 SER E 14 1 16
HELIX 17 17 ARG E 61 ALA E 64 5 4
HELIX 18 18 SER E 79 LEU E 81 5 3
HELIX 19 19 LYS F -5 ASP F -2 5 4
HELIX 20 20 ASP F -1 SER F 14 1 16
HELIX 21 21 ARG F 61 ALA F 64 5 4
HELIX 22 22 PRO F 77 LEU F 81 5 5
HELIX 23 23 ASP G -7 ASP G -3 5 5
HELIX 24 24 ASP G -1 SER G 14 1 16
HELIX 25 25 ARG G 61 ALA G 64 5 4
HELIX 26 26 SER G 79 LEU G 81 5 3
HELIX 27 27 ASP H -7 ASP H -3 5 5
HELIX 28 28 ASP H -1 SER H 14 1 16
HELIX 29 29 ARG H 61 ALA H 64 5 4
HELIX 30 30 SER H 79 LEU H 81 5 3
HELIX 31 31 ASP I -7 ASP I -3 5 5
HELIX 32 32 ASP I -1 SER I 14 1 16
HELIX 33 33 ARG I 61 ALA I 64 5 4
HELIX 34 34 SER I 79 LEU I 81 5 3
HELIX 35 35 ASP J -1 SER J 14 1 16
HELIX 36 36 ARG J 61 ALA J 64 5 4
HELIX 37 37 SER J 79 LEU J 81 5 3
SHEET 1 A 6 GLN A 73 PRO A 77 0
SHEET 2 A 6 LEU A 102 VAL A 106 -1 O ALA A 103 N VAL A 76
SHEET 3 A 6 GLU A 110 TYR A 113 -1 O GLU A 110 N VAL A 106
SHEET 4 A 6 GLU A 47 SER A 59 -1 N THR A 56 O TYR A 113
SHEET 5 A 6 SER A 116 SER A 122 -1 O ILE A 117 N PHE A 52
SHEET 6 A 6 GLU A 96 VAL A 97 -1 N GLU A 96 O ARG A 118
SHEET 1 B 6 GLN A 73 PRO A 77 0
SHEET 2 B 6 LEU A 102 VAL A 106 -1 O ALA A 103 N VAL A 76
SHEET 3 B 6 GLU A 110 TYR A 113 -1 O GLU A 110 N VAL A 106
SHEET 4 B 6 GLU A 47 SER A 59 -1 N THR A 56 O TYR A 113
SHEET 5 B 6 VAL A 27 ASN A 42 -1 N SER A 30 O THR A 57
SHEET 6 B 6 ILE A 150 PRO A 154 1 O ASP A 153 N VAL A 29
SHEET 1 C 4 LEU A 86 ALA A 88 0
SHEET 2 C 4 ALA A 134 SER A 142 -1 O GLY A 141 N ALA A 87
SHEET 3 C 4 ASP A 194 LYS A 203 -1 O VAL A 197 N ILE A 138
SHEET 4 C 4 PHE A 171 ASN A 181 -1 N THR A 177 O SER A 198
SHEET 1 D 6 GLN B 73 PRO B 77 0
SHEET 2 D 6 LEU B 102 VAL B 106 -1 O ALA B 103 N VAL B 76
SHEET 3 D 6 GLU B 110 TYR B 113 -1 O GLU B 110 N VAL B 106
SHEET 4 D 6 GLU B 47 SER B 59 -1 N TRP B 58 O VAL B 111
SHEET 5 D 6 SER B 116 SER B 122 -1 O ILE B 117 N PHE B 52
SHEET 6 D 6 GLU B 96 VAL B 97 -1 N GLU B 96 O ARG B 118
SHEET 1 E 6 GLN B 73 PRO B 77 0
SHEET 2 E 6 LEU B 102 VAL B 106 -1 O ALA B 103 N VAL B 76
SHEET 3 E 6 GLU B 110 TYR B 113 -1 O GLU B 110 N VAL B 106
SHEET 4 E 6 GLU B 47 SER B 59 -1 N TRP B 58 O VAL B 111
SHEET 5 E 6 VAL B 27 ASN B 42 -1 N ILE B 36 O VAL B 51
SHEET 6 E 6 ILE B 150 PRO B 154 1 O SER B 151 N VAL B 27
SHEET 1 F 4 LEU B 86 ALA B 88 0
SHEET 2 F 4 ALA B 134 SER B 142 -1 O GLY B 141 N ALA B 87
SHEET 3 F 4 TYR B 192 LYS B 203 -1 O VAL B 197 N ILE B 138
SHEET 4 F 4 PHE B 171 VAL B 183 -1 N ASP B 175 O ASN B 200
SHEET 1 G 6 GLN C 73 PRO C 77 0
SHEET 2 G 6 LEU C 102 VAL C 106 -1 O ALA C 103 N VAL C 76
SHEET 3 G 6 GLU C 110 TYR C 113 -1 O GLU C 110 N VAL C 106
SHEET 4 G 6 GLU C 47 SER C 59 -1 N TRP C 58 O VAL C 111
SHEET 5 G 6 SER C 116 SER C 122 -1 O ILE C 117 N PHE C 52
SHEET 6 G 6 GLU C 96 VAL C 97 -1 N GLU C 96 O ARG C 118
SHEET 1 H 6 GLN C 73 PRO C 77 0
SHEET 2 H 6 LEU C 102 VAL C 106 -1 O ALA C 103 N VAL C 76
SHEET 3 H 6 GLU C 110 TYR C 113 -1 O GLU C 110 N VAL C 106
SHEET 4 H 6 GLU C 47 SER C 59 -1 N TRP C 58 O VAL C 111
SHEET 5 H 6 VAL C 27 ILE C 38 -1 N ILE C 36 O VAL C 51
SHEET 6 H 6 ILE C 150 ASP C 153 1 O SER C 151 N VAL C 29
SHEET 1 I 5 LEU C 86 ALA C 88 0
SHEET 2 I 5 ALA C 134 SER C 142 -1 O GLY C 141 N ALA C 87
SHEET 3 I 5 TYR C 192 LYS C 203 -1 O LEU C 199 N CYS C 136
SHEET 4 I 5 PHE C 171 VAL C 183 -1 N THR C 177 O SER C 198
SHEET 5 I 5 ASN C 158 SER C 159 -1 N SER C 159 O VAL C 176
SHEET 1 J 6 GLN D 73 PRO D 77 0
SHEET 2 J 6 LEU D 102 VAL D 106 -1 O ALA D 103 N VAL D 76
SHEET 3 J 6 GLU D 110 TYR D 113 -1 O GLU D 110 N VAL D 106
SHEET 4 J 6 GLU D 47 SER D 59 -1 N THR D 56 O TYR D 113
SHEET 5 J 6 SER D 116 SER D 122 -1 O PHE D 121 N VAL D 48
SHEET 6 J 6 GLU D 96 VAL D 97 -1 N GLU D 96 O ARG D 118
SHEET 1 K 6 GLN D 73 PRO D 77 0
SHEET 2 K 6 LEU D 102 VAL D 106 -1 O ALA D 103 N VAL D 76
SHEET 3 K 6 GLU D 110 TYR D 113 -1 O GLU D 110 N VAL D 106
SHEET 4 K 6 GLU D 47 SER D 59 -1 N THR D 56 O TYR D 113
SHEET 5 K 6 VAL D 27 ASN D 42 -1 N ILE D 36 O VAL D 51
SHEET 6 K 6 ILE D 150 PRO D 154 1 O ASP D 153 N VAL D 31
SHEET 1 L 4 LEU D 86 ALA D 88 0
SHEET 2 L 4 ALA D 134 SER D 142 -1 O GLY D 141 N ALA D 87
SHEET 3 L 4 TYR D 192 LYS D 203 -1 O PHE D 201 N ALA D 134
SHEET 4 L 4 PHE D 171 VAL D 183 -1 N ASN D 181 O ASP D 194
SHEET 1 M 6 GLN E 73 PRO E 77 0
SHEET 2 M 6 LEU E 102 VAL E 106 -1 O ALA E 103 N VAL E 76
SHEET 3 M 6 GLU E 110 TYR E 113 -1 O GLU E 110 N VAL E 106
SHEET 4 M 6 GLU E 47 SER E 59 -1 N THR E 56 O TYR E 113
SHEET 5 M 6 SER E 116 SER E 122 -1 O ILE E 117 N PHE E 52
SHEET 6 M 6 GLU E 96 VAL E 97 -1 N GLU E 96 O ARG E 118
SHEET 1 N 6 GLN E 73 PRO E 77 0
SHEET 2 N 6 LEU E 102 VAL E 106 -1 O ALA E 103 N VAL E 76
SHEET 3 N 6 GLU E 110 TYR E 113 -1 O GLU E 110 N VAL E 106
SHEET 4 N 6 GLU E 47 SER E 59 -1 N THR E 56 O TYR E 113
SHEET 5 N 6 VAL E 27 ASN E 42 -1 N SER E 30 O THR E 57
SHEET 6 N 6 ILE E 150 ASP E 153 1 O SER E 151 N VAL E 27
SHEET 1 O 4 LEU E 86 ALA E 88 0
SHEET 2 O 4 ALA E 134 SER E 142 -1 O GLY E 141 N ALA E 87
SHEET 3 O 4 TYR E 192 LYS E 203 -1 O LEU E 199 N CYS E 136
SHEET 4 O 4 PHE E 171 VAL E 183 -1 N LEU E 174 O ASN E 200
SHEET 1 P 6 GLN F 73 VAL F 76 0
SHEET 2 P 6 ALA F 103 VAL F 106 -1 O ALA F 103 N VAL F 76
SHEET 3 P 6 GLU F 110 TYR F 113 -1 O LEU F 112 N ARG F 104
SHEET 4 P 6 GLU F 47 SER F 59 -1 N TRP F 58 O VAL F 111
SHEET 5 P 6 SER F 116 SER F 122 -1 O ILE F 117 N PHE F 52
SHEET 6 P 6 GLU F 96 VAL F 97 -1 N GLU F 96 O ARG F 118
SHEET 1 Q 6 GLN F 73 VAL F 76 0
SHEET 2 Q 6 ALA F 103 VAL F 106 -1 O ALA F 103 N VAL F 76
SHEET 3 Q 6 GLU F 110 TYR F 113 -1 O LEU F 112 N ARG F 104
SHEET 4 Q 6 GLU F 47 SER F 59 -1 N TRP F 58 O VAL F 111
SHEET 5 Q 6 VAL F 27 ASN F 42 -1 N SER F 30 O THR F 57
SHEET 6 Q 6 ILE F 150 ASP F 153 1 O SER F 151 N VAL F 27
SHEET 1 R 5 LEU F 86 ALA F 88 0
SHEET 2 R 5 ALA F 134 SER F 142 -1 O GLY F 141 N ALA F 87
SHEET 3 R 5 TYR F 192 LYS F 203 -1 O VAL F 197 N ILE F 138
SHEET 4 R 5 PHE F 171 VAL F 183 -1 N LYS F 179 O GLU F 196
SHEET 5 R 5 ASN F 158 SER F 159 -1 N SER F 159 O VAL F 176
SHEET 1 S 6 GLN G 73 PRO G 77 0
SHEET 2 S 6 LEU G 102 VAL G 106 -1 O VAL G 105 N VAL G 74
SHEET 3 S 6 GLU G 110 TYR G 113 -1 O GLU G 110 N VAL G 106
SHEET 4 S 6 GLU G 47 SER G 59 -1 N THR G 56 O TYR G 113
SHEET 5 S 6 SER G 116 SER G 122 -1 O ILE G 117 N PHE G 52
SHEET 6 S 6 GLU G 96 VAL G 97 -1 N GLU G 96 O ARG G 118
SHEET 1 T 6 GLN G 73 PRO G 77 0
SHEET 2 T 6 LEU G 102 VAL G 106 -1 O VAL G 105 N VAL G 74
SHEET 3 T 6 GLU G 110 TYR G 113 -1 O GLU G 110 N VAL G 106
SHEET 4 T 6 GLU G 47 SER G 59 -1 N THR G 56 O TYR G 113
SHEET 5 T 6 VAL G 27 ASN G 42 -1 N LEU G 39 O ASP G 49
SHEET 6 T 6 ILE G 150 ASP G 153 1 O SER G 151 N VAL G 27
SHEET 1 U 5 LEU G 86 ALA G 88 0
SHEET 2 U 5 ALA G 134 SER G 142 -1 O GLY G 141 N ALA G 87
SHEET 3 U 5 TYR G 192 LYS G 203 -1 O LEU G 199 N CYS G 136
SHEET 4 U 5 PHE G 171 VAL G 183 -1 N THR G 177 O SER G 198
SHEET 5 U 5 ASN G 158 SER G 159 -1 N SER G 159 O VAL G 176
SHEET 1 V 6 GLN H 73 PRO H 77 0
SHEET 2 V 6 LEU H 102 VAL H 106 -1 O ALA H 103 N VAL H 76
SHEET 3 V 6 GLU H 110 TYR H 113 -1 O GLU H 110 N VAL H 106
SHEET 4 V 6 GLU H 47 SER H 59 -1 N TRP H 58 O VAL H 111
SHEET 5 V 6 SER H 116 SER H 122 -1 O ILE H 117 N PHE H 52
SHEET 6 V 6 GLU H 96 VAL H 97 -1 N GLU H 96 O ARG H 118
SHEET 1 W 6 GLN H 73 PRO H 77 0
SHEET 2 W 6 LEU H 102 VAL H 106 -1 O ALA H 103 N VAL H 76
SHEET 3 W 6 GLU H 110 TYR H 113 -1 O GLU H 110 N VAL H 106
SHEET 4 W 6 GLU H 47 SER H 59 -1 N TRP H 58 O VAL H 111
SHEET 5 W 6 VAL H 27 ILE H 38 -1 N SER H 30 O THR H 57
SHEET 6 W 6 ILE H 150 ASP H 153 1 O SER H 151 N VAL H 27
SHEET 1 X 4 LEU H 86 ALA H 88 0
SHEET 2 X 4 ALA H 134 SER H 142 -1 O GLY H 141 N ALA H 87
SHEET 3 X 4 ALA H 191 LYS H 203 -1 O VAL H 195 N ILE H 140
SHEET 4 X 4 PHE H 171 THR H 184 -1 N LYS H 179 O GLU H 196
SHEET 1 Y 6 GLN I 73 PRO I 77 0
SHEET 2 Y 6 LEU I 102 VAL I 106 -1 O ALA I 103 N VAL I 76
SHEET 3 Y 6 GLU I 110 TYR I 113 -1 O GLU I 110 N VAL I 106
SHEET 4 Y 6 GLU I 47 SER I 59 -1 N TRP I 58 O VAL I 111
SHEET 5 Y 6 SER I 116 SER I 122 -1 O PHE I 121 N VAL I 48
SHEET 6 Y 6 GLU I 96 VAL I 97 -1 N GLU I 96 O ARG I 118
SHEET 1 Z 6 GLN I 73 PRO I 77 0
SHEET 2 Z 6 LEU I 102 VAL I 106 -1 O ALA I 103 N VAL I 76
SHEET 3 Z 6 GLU I 110 TYR I 113 -1 O GLU I 110 N VAL I 106
SHEET 4 Z 6 GLU I 47 SER I 59 -1 N TRP I 58 O VAL I 111
SHEET 5 Z 6 VAL I 27 ASN I 42 -1 N ILE I 36 O VAL I 51
SHEET 6 Z 6 ILE I 150 VAL I 152 1 O SER I 151 N VAL I 27
SHEET 1 AA 4 LEU I 86 ALA I 88 0
SHEET 2 AA 4 ALA I 134 SER I 142 -1 O GLY I 141 N ALA I 87
SHEET 3 AA 4 ASP I 194 LYS I 203 -1 O VAL I 197 N ILE I 138
SHEET 4 AA 4 PHE I 171 ASN I 181 -1 N LEU I 174 O ASN I 200
SHEET 1 AB 6 GLN J 73 PRO J 77 0
SHEET 2 AB 6 LEU J 102 VAL J 106 -1 O ALA J 103 N VAL J 76
SHEET 3 AB 6 GLU J 110 TYR J 113 -1 O GLU J 110 N VAL J 106
SHEET 4 AB 6 GLU J 47 SER J 59 -1 N TRP J 58 O VAL J 111
SHEET 5 AB 6 SER J 116 SER J 122 -1 O ILE J 117 N PHE J 52
SHEET 6 AB 6 GLU J 96 VAL J 97 -1 N GLU J 96 O ARG J 118
SHEET 1 AC 6 GLN J 73 PRO J 77 0
SHEET 2 AC 6 LEU J 102 VAL J 106 -1 O ALA J 103 N VAL J 76
SHEET 3 AC 6 GLU J 110 TYR J 113 -1 O GLU J 110 N VAL J 106
SHEET 4 AC 6 GLU J 47 SER J 59 -1 N TRP J 58 O VAL J 111
SHEET 5 AC 6 VAL J 27 ASN J 42 -1 N SER J 30 O THR J 57
SHEET 6 AC 6 ILE J 150 PRO J 154 1 O ASP J 153 N VAL J 31
SHEET 1 AD 5 LEU J 86 ALA J 88 0
SHEET 2 AD 5 ALA J 134 SER J 142 -1 O GLY J 141 N ALA J 87
SHEET 3 AD 5 ASP J 194 LYS J 203 -1 O LEU J 199 N CYS J 136
SHEET 4 AD 5 PHE J 171 ASN J 181 -1 N THR J 177 O SER J 198
SHEET 5 AD 5 ASN J 158 SER J 159 -1 N SER J 159 O VAL J 176
SSBOND 1 CYS A 123 CYS A 136 1555 1555 2.46
SSBOND 2 CYS B 123 CYS B 136 1555 1555 2.27
SSBOND 3 CYS C 123 CYS C 136 1555 1555 2.22
SSBOND 4 CYS D 123 CYS D 136 1555 1555 2.57
SSBOND 5 CYS D 187 CYS D 188 1555 1555 2.05
SSBOND 6 CYS E 123 CYS E 136 1555 1555 2.30
SSBOND 7 CYS F 123 CYS F 136 1555 1555 2.37
SSBOND 8 CYS G 123 CYS G 136 1555 1555 2.42
SSBOND 9 CYS H 123 CYS H 136 1555 1555 2.41
SSBOND 10 CYS I 123 CYS I 136 1555 1555 2.38
SSBOND 11 CYS J 123 CYS J 136 1555 1555 2.47
LINK ND2 ASN A 66 C1 NAG A 302 1555 1555 1.45
LINK ND2 ASN B 66 C1 NAG B 302 1555 1555 1.44
LINK ND2 ASN C 66 C1 NAG C 302 1555 1555 1.41
LINK ND2 ASN D 66 C1 NAG D 302 1555 1555 1.50
LINK ND2 ASN E 66 C1 NAG E 302 1555 1555 1.45
LINK ND2 ASN F 66 C1 NAG F 302 1555 1555 1.52
LINK ND2 ASN G 66 C1 NAG G 302 1555 1555 1.55
LINK ND2 ASN H 66 C1 NAG H 302 1555 1555 1.54
LINK ND2 ASN I 66 C1 NAG I 302 1555 1555 1.58
LINK ND2 ASN J 66 C1 NAG J 302 1555 1555 1.36
CISPEP 1 THR A 155 THR A 156 0 -3.13
CISPEP 2 GLU A 157 ASN A 158 0 4.64
CISPEP 3 ASP A 160 ASP A 161 0 7.97
CISPEP 4 ASP D 160 ASP D 161 0 -4.52
CRYST1 83.414 129.934 122.752 90.00 106.21 90.00 P 1 21 1 20
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 0.011988 0.000000 0.003485 0.00000
SCALE2 0.000000 0.007696 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008484 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
