HEADER BIOSYNTHETIC PROTEIN 13-AUG-18 6AGM
TITLE MOLECULAR BASIS FOR FEEDBACK INHIBITION OF TYROSINE-REGULATED 3-DEOXY-
TITLE 2 D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYR-SENSITIVE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE,DAHP
COMPND 5 SYNTHASE,PHOSPHO-2-KETO-3-DEOXYHEPTONATE ALDOLASE;
COMPND 6 EC: 2.5.1.54;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: AROF, B2601, JW2582;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE (DAHP SYNTHASE),
KEYWDS 2 ESCHERICHIA COLI, AROMATIC AMINO ACID BIOSYNTHESIS, FEEDBACK
KEYWDS 3 INHIBITION, ALLOSTERIC REGULATION., BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.CUI,J.QI,T.WEN
REVDAT 3 22-NOV-23 6AGM 1 REMARK
REVDAT 2 29-MAY-19 6AGM 1 JRNL
REVDAT 1 17-APR-19 6AGM 0
JRNL AUTH D.CUI,A.DENG,H.BAI,Z.YANG,Y.LIANG,Z.LIU,Q.QIU,L.WANG,S.LIU,
JRNL AUTH 2 Y.ZHANG,Y.SHI,J.QI,T.WEN
JRNL TITL MOLECULAR BASIS FOR FEEDBACK INHIBITION OF
JRNL TITL 2 TYROSINE-REGULATED
JRNL TITL 3 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM
JRNL TITL 4 ESCHERICHIA COLI.
JRNL REF J.STRUCT.BIOL. V. 206 322 2019
JRNL REFN ESSN 1095-8657
JRNL PMID 30946901
JRNL DOI 10.1016/J.JSB.2019.04.001
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 82301
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4111
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 38.2140 - 6.1173 1.00 2842 141 0.1505 0.1665
REMARK 3 2 6.1173 - 4.8586 1.00 2798 138 0.1701 0.2070
REMARK 3 3 4.8586 - 4.2454 1.00 2807 151 0.1500 0.1666
REMARK 3 4 4.2454 - 3.8576 1.00 2782 156 0.1538 0.2052
REMARK 3 5 3.8576 - 3.5813 1.00 2766 158 0.1796 0.2188
REMARK 3 6 3.5813 - 3.3703 1.00 2768 150 0.1870 0.2352
REMARK 3 7 3.3703 - 3.2016 1.00 2777 152 0.2064 0.2551
REMARK 3 8 3.2016 - 3.0623 1.00 2808 131 0.2189 0.2688
REMARK 3 9 3.0623 - 2.9445 1.00 2818 130 0.2256 0.2497
REMARK 3 10 2.9445 - 2.8429 1.00 2747 147 0.2335 0.2731
REMARK 3 11 2.8429 - 2.7540 1.00 2804 148 0.2330 0.2410
REMARK 3 12 2.7540 - 2.6753 1.00 2765 146 0.2254 0.2629
REMARK 3 13 2.6753 - 2.6049 1.00 2767 139 0.2271 0.2543
REMARK 3 14 2.6049 - 2.5414 1.00 2786 163 0.2287 0.2669
REMARK 3 15 2.5414 - 2.4836 1.00 2755 164 0.2263 0.2982
REMARK 3 16 2.4836 - 2.4308 1.00 2734 167 0.2332 0.3011
REMARK 3 17 2.4308 - 2.3822 1.00 2790 153 0.2292 0.2468
REMARK 3 18 2.3822 - 2.3372 1.00 2800 125 0.2326 0.2621
REMARK 3 19 2.3372 - 2.2955 1.00 2779 128 0.2383 0.3020
REMARK 3 20 2.2955 - 2.2566 1.00 2736 145 0.2420 0.2590
REMARK 3 21 2.2566 - 2.2202 0.99 2796 139 0.2420 0.2790
REMARK 3 22 2.2202 - 2.1860 0.98 2712 149 0.2503 0.2651
REMARK 3 23 2.1860 - 2.1539 0.97 2697 123 0.2627 0.3109
REMARK 3 24 2.1539 - 2.1235 0.95 2590 161 0.2769 0.3323
REMARK 3 25 2.1235 - 2.0948 0.92 2537 148 0.2731 0.2926
REMARK 3 26 2.0948 - 2.0676 0.89 2494 134 0.2736 0.3215
REMARK 3 27 2.0676 - 2.0418 0.86 2382 117 0.2775 0.2963
REMARK 3 28 2.0418 - 2.0172 0.82 2300 113 0.2887 0.3240
REMARK 3 29 2.0172 - 1.9937 0.74 2053 95 0.2995 0.3577
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.620
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 : 0.009 10408
REMARK 3 ANGLE : 0.737 14104
REMARK 3 CHIRALITY : 0.044 1588
REMARK 3 PLANARITY : 0.005 1880
REMARK 3 DIHEDRAL : 25.479 3900
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3286 17.7391 102.7374
REMARK 3 T TENSOR
REMARK 3 T11: 0.2710 T22: 0.2519
REMARK 3 T33: 0.2565 T12: -0.0059
REMARK 3 T13: -0.0216 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.7133 L22: 0.8225
REMARK 3 L33: 0.7442 L12: 0.0898
REMARK 3 L13: -0.2579 L23: 0.1698
REMARK 3 S TENSOR
REMARK 3 S11: 0.0316 S12: 0.0556 S13: 0.1238
REMARK 3 S21: -0.0872 S22: -0.0110 S23: 0.0596
REMARK 3 S31: -0.0412 S32: -0.0247 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2630 55.7904 119.2073
REMARK 3 T TENSOR
REMARK 3 T11: 0.3502 T22: 0.3380
REMARK 3 T33: 0.3378 T12: 0.0226
REMARK 3 T13: 0.0155 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.5447 L22: 0.6576
REMARK 3 L33: 0.9467 L12: 0.3719
REMARK 3 L13: -0.0950 L23: -0.0677
REMARK 3 S TENSOR
REMARK 3 S11: 0.0350 S12: -0.0306 S13: 0.0700
REMARK 3 S21: 0.0932 S22: 0.0217 S23: 0.0641
REMARK 3 S31: 0.0864 S32: -0.0878 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 10 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9992 53.1506 74.6699
REMARK 3 T TENSOR
REMARK 3 T11: 0.2992 T22: 0.2949
REMARK 3 T33: 0.3088 T12: -0.0029
REMARK 3 T13: 0.0223 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.0755 L22: 1.9543
REMARK 3 L33: 0.8994 L12: -0.3369
REMARK 3 L13: 0.1767 L23: -0.3092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0269 S12: 0.0417 S13: -0.0669
REMARK 3 S21: -0.1441 S22: -0.0116 S23: -0.0489
REMARK 3 S31: 0.0986 S32: -0.0145 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 10 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9427 20.3068 147.6963
REMARK 3 T TENSOR
REMARK 3 T11: 0.3897 T22: 0.3783
REMARK 3 T33: 0.3342 T12: 0.0326
REMARK 3 T13: -0.0063 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.7507 L22: 1.2887
REMARK 3 L33: 0.6112 L12: 0.3621
REMARK 3 L13: 0.0979 L23: -0.2555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0281 S12: 0.0341 S13: 0.0423
REMARK 3 S21: 0.1582 S22: 0.0421 S23: -0.0129
REMARK 3 S31: -0.1585 S32: -0.0419 S33: -0.0000
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 6AGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1300008718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82353
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
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) : 0.78800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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: 1QR7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000, 10% 2-PROPANOL, 0.1 M
REMARK 280 SODIUM CITRATE, PH 5.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
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 66.92950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -3.76383
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -66.92950
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 175.29960
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -5.64575
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 66.92950
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 262.94940
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 GLN A 2
REMARK 465 LYS A 3
REMARK 465 ASN A 310
REMARK 465 GLN A 311
REMARK 465 SER A 312
REMARK 465 SER A 313
REMARK 465 GLU A 314
REMARK 465 GLN A 315
REMARK 465 PRO A 316
REMARK 465 ARG A 317
REMARK 465 SER A 318
REMARK 465 GLU A 319
REMARK 465 MET A 320
REMARK 465 LYS A 321
REMARK 465 TYR A 322
REMARK 465 GLY A 323
REMARK 465 VAL A 324
REMARK 465 SER A 325
REMARK 465 VAL A 326
REMARK 465 THR A 327
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 LYS B 3
REMARK 465 ASN B 310
REMARK 465 GLN B 311
REMARK 465 SER B 312
REMARK 465 SER B 313
REMARK 465 GLU B 314
REMARK 465 GLN B 315
REMARK 465 PRO B 316
REMARK 465 ARG B 317
REMARK 465 SER B 318
REMARK 465 GLU B 319
REMARK 465 MET B 320
REMARK 465 LYS B 321
REMARK 465 TYR B 322
REMARK 465 GLY B 323
REMARK 465 VAL B 324
REMARK 465 SER B 325
REMARK 465 VAL B 326
REMARK 465 THR B 327
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 LYS C 3
REMARK 465 ASN C 310
REMARK 465 GLN C 311
REMARK 465 SER C 312
REMARK 465 SER C 313
REMARK 465 GLU C 314
REMARK 465 GLN C 315
REMARK 465 PRO C 316
REMARK 465 ARG C 317
REMARK 465 SER C 318
REMARK 465 GLU C 319
REMARK 465 MET C 320
REMARK 465 LYS C 321
REMARK 465 TYR C 322
REMARK 465 GLY C 323
REMARK 465 VAL C 324
REMARK 465 SER C 325
REMARK 465 VAL C 326
REMARK 465 THR C 327
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 LYS D 3
REMARK 465 ASN D 310
REMARK 465 GLN D 311
REMARK 465 SER D 312
REMARK 465 SER D 313
REMARK 465 GLU D 314
REMARK 465 GLN D 315
REMARK 465 PRO D 316
REMARK 465 ARG D 317
REMARK 465 SER D 318
REMARK 465 GLU D 319
REMARK 465 MET D 320
REMARK 465 LYS D 321
REMARK 465 TYR D 322
REMARK 465 GLY D 323
REMARK 465 VAL D 324
REMARK 465 SER D 325
REMARK 465 VAL D 326
REMARK 465 THR D 327
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 OE1 GLN C 289 O HOH C 701 2.05
REMARK 500 O PRO C 240 O HOH C 702 2.07
REMARK 500 N HIS A 307 O HOH A 701 2.07
REMARK 500 O HOH D 747 O HOH D 752 2.07
REMARK 500 OG1 THR C 101 O VAL C 103 2.12
REMARK 500 OE2 GLU C 133 O HOH C 703 2.12
REMARK 500 O ASN B 294 NE ARG B 354 2.12
REMARK 500 O PHE C 96 O HOH C 704 2.15
REMARK 500 N PHE A 118 O HOH A 702 2.17
REMARK 500 O ALA A 145 O HOH A 703 2.19
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 SER A 268 -143.76 -91.34
REMARK 500 HIS A 269 -64.52 -27.66
REMARK 500 ARG B 100 71.15 62.38
REMARK 500 ASP B 115 -0.66 -141.25
REMARK 500 ASP B 229 68.93 -101.10
REMARK 500 SER B 268 -146.05 -92.85
REMARK 500 HIS B 269 -62.86 -27.08
REMARK 500 HIS C 65 -61.43 -95.23
REMARK 500 ARG C 100 72.03 62.81
REMARK 500 HIS C 173 32.32 -142.08
REMARK 500 SER C 268 -144.44 -80.22
REMARK 500 HIS C 269 -64.58 -28.74
REMARK 500 LEU C 347 36.57 -98.39
REMARK 500 PRO D 99 40.33 -78.43
REMARK 500 SER D 268 -141.30 -90.41
REMARK 500 HIS D 269 -66.30 -29.29
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 SER A 268 HIS A 269 -136.37
REMARK 500 SER B 268 HIS B 269 -138.99
REMARK 500 SER C 268 HIS C 269 -137.72
REMARK 500 SER D 268 HIS D 269 -134.72
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 TYR A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TYR B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TYR C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TYR D 601
DBREF 6AGM A 1 355 UNP P00888 AROF_ECOLI 1 355
DBREF 6AGM B 1 355 UNP P00888 AROF_ECOLI 1 355
DBREF 6AGM C 1 355 UNP P00888 AROF_ECOLI 1 355
DBREF 6AGM D 1 355 UNP P00888 AROF_ECOLI 1 355
SEQRES 1 A 355 MET GLN LYS ASP ALA LEU ASN ASN VAL HIS ILE THR ASP
SEQRES 2 A 355 GLU GLN VAL LEU MET THR PRO GLU GLN LEU LYS ALA ALA
SEQRES 3 A 355 PHE PRO LEU SER LEU GLN GLN GLU ALA GLN ILE ALA ASP
SEQRES 4 A 355 SER ARG LYS SER ILE SER ASP ILE ILE ALA GLY ARG ASP
SEQRES 5 A 355 PRO ARG LEU LEU VAL VAL CYS GLY PRO CYS SER ILE HIS
SEQRES 6 A 355 ASP PRO GLU THR ALA LEU GLU TYR ALA ARG ARG PHE LYS
SEQRES 7 A 355 ALA LEU ALA ALA GLU VAL SER ASP SER LEU TYR LEU VAL
SEQRES 8 A 355 MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL GLY
SEQRES 9 A 355 TRP LYS GLY LEU ILE ASN ASP PRO HIS MET ASP GLY SER
SEQRES 10 A 355 PHE ASP VAL GLU ALA GLY LEU GLN ILE ALA ARG LYS LEU
SEQRES 11 A 355 LEU LEU GLU LEU VAL ASN MET GLY LEU PRO LEU ALA THR
SEQRES 12 A 355 GLU ALA LEU ASP PRO ASN SER PRO GLN TYR LEU GLY ASP
SEQRES 13 A 355 LEU PHE SER TRP SER ALA ILE GLY ALA ARG THR THR GLU
SEQRES 14 A 355 SER GLN THR HIS ARG GLU MET ALA SER GLY LEU SER MET
SEQRES 15 A 355 PRO VAL GLY PHE LYS ASN GLY THR ASP GLY SER LEU ALA
SEQRES 16 A 355 THR ALA ILE ASN ALA MET ARG ALA ALA ALA GLN PRO HIS
SEQRES 17 A 355 ARG PHE VAL GLY ILE ASN GLN ALA GLY GLN VAL ALA LEU
SEQRES 18 A 355 LEU GLN THR GLN GLY ASN PRO ASP GLY HIS VAL ILE LEU
SEQRES 19 A 355 ARG GLY GLY LYS ALA PRO ASN TYR SER PRO ALA ASP VAL
SEQRES 20 A 355 ALA GLN CYS GLU LYS GLU MET GLU GLN ALA GLY LEU ARG
SEQRES 21 A 355 PRO SER LEU MET VAL ASP CYS SER HIS GLY ASN SER ASN
SEQRES 22 A 355 LYS ASP TYR ARG ARG GLN PRO ALA VAL ALA GLU SER VAL
SEQRES 23 A 355 VAL ALA GLN ILE LYS ASP GLY ASN ARG SER ILE ILE GLY
SEQRES 24 A 355 LEU MET ILE GLU SER ASN ILE HIS GLU GLY ASN GLN SER
SEQRES 25 A 355 SER GLU GLN PRO ARG SER GLU MET LYS TYR GLY VAL SER
SEQRES 26 A 355 VAL THR ASP ALA CYS ILE SER TRP GLU MET THR ASP ALA
SEQRES 27 A 355 LEU LEU ARG GLU ILE HIS GLN ASP LEU ASN GLY GLN LEU
SEQRES 28 A 355 THR ALA ARG VAL
SEQRES 1 B 355 MET GLN LYS ASP ALA LEU ASN ASN VAL HIS ILE THR ASP
SEQRES 2 B 355 GLU GLN VAL LEU MET THR PRO GLU GLN LEU LYS ALA ALA
SEQRES 3 B 355 PHE PRO LEU SER LEU GLN GLN GLU ALA GLN ILE ALA ASP
SEQRES 4 B 355 SER ARG LYS SER ILE SER ASP ILE ILE ALA GLY ARG ASP
SEQRES 5 B 355 PRO ARG LEU LEU VAL VAL CYS GLY PRO CYS SER ILE HIS
SEQRES 6 B 355 ASP PRO GLU THR ALA LEU GLU TYR ALA ARG ARG PHE LYS
SEQRES 7 B 355 ALA LEU ALA ALA GLU VAL SER ASP SER LEU TYR LEU VAL
SEQRES 8 B 355 MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL GLY
SEQRES 9 B 355 TRP LYS GLY LEU ILE ASN ASP PRO HIS MET ASP GLY SER
SEQRES 10 B 355 PHE ASP VAL GLU ALA GLY LEU GLN ILE ALA ARG LYS LEU
SEQRES 11 B 355 LEU LEU GLU LEU VAL ASN MET GLY LEU PRO LEU ALA THR
SEQRES 12 B 355 GLU ALA LEU ASP PRO ASN SER PRO GLN TYR LEU GLY ASP
SEQRES 13 B 355 LEU PHE SER TRP SER ALA ILE GLY ALA ARG THR THR GLU
SEQRES 14 B 355 SER GLN THR HIS ARG GLU MET ALA SER GLY LEU SER MET
SEQRES 15 B 355 PRO VAL GLY PHE LYS ASN GLY THR ASP GLY SER LEU ALA
SEQRES 16 B 355 THR ALA ILE ASN ALA MET ARG ALA ALA ALA GLN PRO HIS
SEQRES 17 B 355 ARG PHE VAL GLY ILE ASN GLN ALA GLY GLN VAL ALA LEU
SEQRES 18 B 355 LEU GLN THR GLN GLY ASN PRO ASP GLY HIS VAL ILE LEU
SEQRES 19 B 355 ARG GLY GLY LYS ALA PRO ASN TYR SER PRO ALA ASP VAL
SEQRES 20 B 355 ALA GLN CYS GLU LYS GLU MET GLU GLN ALA GLY LEU ARG
SEQRES 21 B 355 PRO SER LEU MET VAL ASP CYS SER HIS GLY ASN SER ASN
SEQRES 22 B 355 LYS ASP TYR ARG ARG GLN PRO ALA VAL ALA GLU SER VAL
SEQRES 23 B 355 VAL ALA GLN ILE LYS ASP GLY ASN ARG SER ILE ILE GLY
SEQRES 24 B 355 LEU MET ILE GLU SER ASN ILE HIS GLU GLY ASN GLN SER
SEQRES 25 B 355 SER GLU GLN PRO ARG SER GLU MET LYS TYR GLY VAL SER
SEQRES 26 B 355 VAL THR ASP ALA CYS ILE SER TRP GLU MET THR ASP ALA
SEQRES 27 B 355 LEU LEU ARG GLU ILE HIS GLN ASP LEU ASN GLY GLN LEU
SEQRES 28 B 355 THR ALA ARG VAL
SEQRES 1 C 355 MET GLN LYS ASP ALA LEU ASN ASN VAL HIS ILE THR ASP
SEQRES 2 C 355 GLU GLN VAL LEU MET THR PRO GLU GLN LEU LYS ALA ALA
SEQRES 3 C 355 PHE PRO LEU SER LEU GLN GLN GLU ALA GLN ILE ALA ASP
SEQRES 4 C 355 SER ARG LYS SER ILE SER ASP ILE ILE ALA GLY ARG ASP
SEQRES 5 C 355 PRO ARG LEU LEU VAL VAL CYS GLY PRO CYS SER ILE HIS
SEQRES 6 C 355 ASP PRO GLU THR ALA LEU GLU TYR ALA ARG ARG PHE LYS
SEQRES 7 C 355 ALA LEU ALA ALA GLU VAL SER ASP SER LEU TYR LEU VAL
SEQRES 8 C 355 MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL GLY
SEQRES 9 C 355 TRP LYS GLY LEU ILE ASN ASP PRO HIS MET ASP GLY SER
SEQRES 10 C 355 PHE ASP VAL GLU ALA GLY LEU GLN ILE ALA ARG LYS LEU
SEQRES 11 C 355 LEU LEU GLU LEU VAL ASN MET GLY LEU PRO LEU ALA THR
SEQRES 12 C 355 GLU ALA LEU ASP PRO ASN SER PRO GLN TYR LEU GLY ASP
SEQRES 13 C 355 LEU PHE SER TRP SER ALA ILE GLY ALA ARG THR THR GLU
SEQRES 14 C 355 SER GLN THR HIS ARG GLU MET ALA SER GLY LEU SER MET
SEQRES 15 C 355 PRO VAL GLY PHE LYS ASN GLY THR ASP GLY SER LEU ALA
SEQRES 16 C 355 THR ALA ILE ASN ALA MET ARG ALA ALA ALA GLN PRO HIS
SEQRES 17 C 355 ARG PHE VAL GLY ILE ASN GLN ALA GLY GLN VAL ALA LEU
SEQRES 18 C 355 LEU GLN THR GLN GLY ASN PRO ASP GLY HIS VAL ILE LEU
SEQRES 19 C 355 ARG GLY GLY LYS ALA PRO ASN TYR SER PRO ALA ASP VAL
SEQRES 20 C 355 ALA GLN CYS GLU LYS GLU MET GLU GLN ALA GLY LEU ARG
SEQRES 21 C 355 PRO SER LEU MET VAL ASP CYS SER HIS GLY ASN SER ASN
SEQRES 22 C 355 LYS ASP TYR ARG ARG GLN PRO ALA VAL ALA GLU SER VAL
SEQRES 23 C 355 VAL ALA GLN ILE LYS ASP GLY ASN ARG SER ILE ILE GLY
SEQRES 24 C 355 LEU MET ILE GLU SER ASN ILE HIS GLU GLY ASN GLN SER
SEQRES 25 C 355 SER GLU GLN PRO ARG SER GLU MET LYS TYR GLY VAL SER
SEQRES 26 C 355 VAL THR ASP ALA CYS ILE SER TRP GLU MET THR ASP ALA
SEQRES 27 C 355 LEU LEU ARG GLU ILE HIS GLN ASP LEU ASN GLY GLN LEU
SEQRES 28 C 355 THR ALA ARG VAL
SEQRES 1 D 355 MET GLN LYS ASP ALA LEU ASN ASN VAL HIS ILE THR ASP
SEQRES 2 D 355 GLU GLN VAL LEU MET THR PRO GLU GLN LEU LYS ALA ALA
SEQRES 3 D 355 PHE PRO LEU SER LEU GLN GLN GLU ALA GLN ILE ALA ASP
SEQRES 4 D 355 SER ARG LYS SER ILE SER ASP ILE ILE ALA GLY ARG ASP
SEQRES 5 D 355 PRO ARG LEU LEU VAL VAL CYS GLY PRO CYS SER ILE HIS
SEQRES 6 D 355 ASP PRO GLU THR ALA LEU GLU TYR ALA ARG ARG PHE LYS
SEQRES 7 D 355 ALA LEU ALA ALA GLU VAL SER ASP SER LEU TYR LEU VAL
SEQRES 8 D 355 MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL GLY
SEQRES 9 D 355 TRP LYS GLY LEU ILE ASN ASP PRO HIS MET ASP GLY SER
SEQRES 10 D 355 PHE ASP VAL GLU ALA GLY LEU GLN ILE ALA ARG LYS LEU
SEQRES 11 D 355 LEU LEU GLU LEU VAL ASN MET GLY LEU PRO LEU ALA THR
SEQRES 12 D 355 GLU ALA LEU ASP PRO ASN SER PRO GLN TYR LEU GLY ASP
SEQRES 13 D 355 LEU PHE SER TRP SER ALA ILE GLY ALA ARG THR THR GLU
SEQRES 14 D 355 SER GLN THR HIS ARG GLU MET ALA SER GLY LEU SER MET
SEQRES 15 D 355 PRO VAL GLY PHE LYS ASN GLY THR ASP GLY SER LEU ALA
SEQRES 16 D 355 THR ALA ILE ASN ALA MET ARG ALA ALA ALA GLN PRO HIS
SEQRES 17 D 355 ARG PHE VAL GLY ILE ASN GLN ALA GLY GLN VAL ALA LEU
SEQRES 18 D 355 LEU GLN THR GLN GLY ASN PRO ASP GLY HIS VAL ILE LEU
SEQRES 19 D 355 ARG GLY GLY LYS ALA PRO ASN TYR SER PRO ALA ASP VAL
SEQRES 20 D 355 ALA GLN CYS GLU LYS GLU MET GLU GLN ALA GLY LEU ARG
SEQRES 21 D 355 PRO SER LEU MET VAL ASP CYS SER HIS GLY ASN SER ASN
SEQRES 22 D 355 LYS ASP TYR ARG ARG GLN PRO ALA VAL ALA GLU SER VAL
SEQRES 23 D 355 VAL ALA GLN ILE LYS ASP GLY ASN ARG SER ILE ILE GLY
SEQRES 24 D 355 LEU MET ILE GLU SER ASN ILE HIS GLU GLY ASN GLN SER
SEQRES 25 D 355 SER GLU GLN PRO ARG SER GLU MET LYS TYR GLY VAL SER
SEQRES 26 D 355 VAL THR ASP ALA CYS ILE SER TRP GLU MET THR ASP ALA
SEQRES 27 D 355 LEU LEU ARG GLU ILE HIS GLN ASP LEU ASN GLY GLN LEU
SEQRES 28 D 355 THR ALA ARG VAL
HET TYR A 601 13
HET TYR B 601 13
HET TYR C 601 13
HET TYR D 601 13
HETNAM TYR TYROSINE
FORMUL 5 TYR 4(C9 H11 N O3)
FORMUL 9 HOH *282(H2 O)
HELIX 1 AA1 THR A 19 PHE A 27 1 9
HELIX 2 AA2 SER A 30 ALA A 49 1 20
HELIX 3 AA3 ASP A 66 SER A 85 1 20
HELIX 4 AA4 LYS A 106 ASP A 111 1 6
HELIX 5 AA5 ASP A 119 MET A 137 1 19
HELIX 6 AA6 ASN A 149 GLY A 155 1 7
HELIX 7 AA7 ASP A 156 PHE A 158 5 3
HELIX 8 AA8 GLY A 164 GLU A 169 1 6
HELIX 9 AA9 GLU A 175 LEU A 180 5 6
HELIX 10 AB1 LEU A 194 ALA A 205 1 12
HELIX 11 AB2 SER A 243 ALA A 257 1 15
HELIX 12 AB3 SER A 268 ASN A 273 1 6
HELIX 13 AB4 ASP A 275 ARG A 277 5 3
HELIX 14 AB5 ARG A 278 ASP A 292 1 15
HELIX 15 AB6 SER A 332 ASN A 348 1 17
HELIX 16 AB7 THR B 19 PHE B 27 1 9
HELIX 17 AB8 SER B 30 ALA B 49 1 20
HELIX 18 AB9 ASP B 66 VAL B 84 1 19
HELIX 19 AC1 ASP B 119 MET B 137 1 19
HELIX 20 AC2 PRO B 148 GLY B 155 1 8
HELIX 21 AC3 ASP B 156 PHE B 158 5 3
HELIX 22 AC4 GLY B 164 GLU B 169 1 6
HELIX 23 AC5 GLU B 175 LEU B 180 5 6
HELIX 24 AC6 SER B 193 ALA B 205 1 13
HELIX 25 AC7 SER B 243 ALA B 257 1 15
HELIX 26 AC8 ASP B 275 ARG B 277 5 3
HELIX 27 AC9 ARG B 278 ASP B 292 1 15
HELIX 28 AD1 SER B 332 ASN B 348 1 17
HELIX 29 AD2 THR C 19 PHE C 27 1 9
HELIX 30 AD3 SER C 30 ALA C 49 1 20
HELIX 31 AD4 ASP C 66 SER C 85 1 20
HELIX 32 AD5 LYS C 106 ASP C 111 1 6
HELIX 33 AD6 ASP C 119 MET C 137 1 19
HELIX 34 AD7 ASN C 149 GLY C 155 1 7
HELIX 35 AD8 ASP C 156 PHE C 158 5 3
HELIX 36 AD9 GLY C 164 GLU C 169 1 6
HELIX 37 AE1 GLU C 175 LEU C 180 5 6
HELIX 38 AE2 SER C 193 ALA C 205 1 13
HELIX 39 AE3 SER C 243 ALA C 257 1 15
HELIX 40 AE4 SER C 268 ASN C 273 1 6
HELIX 41 AE5 ASP C 275 ARG C 277 5 3
HELIX 42 AE6 ARG C 278 ASP C 292 1 15
HELIX 43 AE7 SER C 332 LEU C 347 1 16
HELIX 44 AE8 LEU C 351 VAL C 355 5 5
HELIX 45 AE9 THR D 19 PHE D 27 1 9
HELIX 46 AF1 SER D 30 ALA D 49 1 20
HELIX 47 AF2 ASP D 66 SER D 85 1 20
HELIX 48 AF3 LYS D 106 ASP D 111 1 6
HELIX 49 AF4 ASP D 119 MET D 137 1 19
HELIX 50 AF5 ASN D 149 GLY D 155 1 7
HELIX 51 AF6 ASP D 156 PHE D 158 5 3
HELIX 52 AF7 GLY D 164 GLU D 169 1 6
HELIX 53 AF8 GLU D 175 LEU D 180 5 6
HELIX 54 AF9 SER D 193 ALA D 205 1 13
HELIX 55 AG1 SER D 243 ALA D 257 1 15
HELIX 56 AG2 SER D 268 ASN D 273 1 6
HELIX 57 AG3 ASP D 275 ARG D 277 5 3
HELIX 58 AG4 ARG D 278 ASP D 292 1 15
HELIX 59 AG5 SER D 332 LEU D 347 1 16
SHEET 1 AA1 9 LEU A 55 GLY A 60 0
SHEET 2 AA1 9 LEU A 88 ARG A 93 1 O VAL A 91 N VAL A 57
SHEET 3 AA1 9 LEU A 141 ALA A 145 1 O ALA A 142 N MET A 92
SHEET 4 AA1 9 TRP A 160 ILE A 163 1 O ALA A 162 N ALA A 145
SHEET 5 AA1 9 VAL A 184 LYS A 187 1 O LYS A 187 N ILE A 163
SHEET 6 AA1 9 GLY A 230 LEU A 234 1 O HIS A 231 N PHE A 186
SHEET 7 AA1 9 LEU A 263 ASP A 266 1 O ASP A 266 N LEU A 234
SHEET 8 AA1 9 ILE A 297 GLU A 303 1 O ILE A 298 N LEU A 263
SHEET 9 AA1 9 LEU A 55 GLY A 60 1 N VAL A 58 O LEU A 300
SHEET 1 AA2 2 ARG A 209 ILE A 213 0
SHEET 2 AA2 2 VAL A 219 GLN A 223 -1 O LEU A 222 N PHE A 210
SHEET 1 AA3 9 LEU B 55 GLY B 60 0
SHEET 2 AA3 9 LEU B 88 ARG B 93 1 O TYR B 89 N LEU B 55
SHEET 3 AA3 9 LEU B 141 ALA B 145 1 O ALA B 142 N MET B 92
SHEET 4 AA3 9 TRP B 160 ILE B 163 1 O ALA B 162 N ALA B 145
SHEET 5 AA3 9 VAL B 184 LYS B 187 1 O GLY B 185 N ILE B 163
SHEET 6 AA3 9 GLY B 230 LEU B 234 1 O HIS B 231 N PHE B 186
SHEET 7 AA3 9 LEU B 263 ASP B 266 1 O ASP B 266 N LEU B 234
SHEET 8 AA3 9 ILE B 297 GLU B 303 1 O ILE B 298 N LEU B 263
SHEET 9 AA3 9 LEU B 55 GLY B 60 1 N VAL B 58 O LEU B 300
SHEET 1 AA4 2 ARG B 209 ILE B 213 0
SHEET 2 AA4 2 VAL B 219 GLN B 223 -1 O LEU B 222 N PHE B 210
SHEET 1 AA5 9 LEU C 55 GLY C 60 0
SHEET 2 AA5 9 LEU C 88 ARG C 93 1 O TYR C 89 N LEU C 55
SHEET 3 AA5 9 LEU C 141 ALA C 145 1 O ALA C 142 N MET C 92
SHEET 4 AA5 9 TRP C 160 ILE C 163 1 O ALA C 162 N ALA C 145
SHEET 5 AA5 9 VAL C 184 LYS C 187 1 O GLY C 185 N ILE C 163
SHEET 6 AA5 9 GLY C 230 LEU C 234 1 O HIS C 231 N PHE C 186
SHEET 7 AA5 9 LEU C 263 ASP C 266 1 O MET C 264 N LEU C 234
SHEET 8 AA5 9 ILE C 297 GLU C 303 1 O ILE C 298 N LEU C 263
SHEET 9 AA5 9 LEU C 55 GLY C 60 1 N VAL C 58 O LEU C 300
SHEET 1 AA6 2 ARG C 209 ILE C 213 0
SHEET 2 AA6 2 VAL C 219 GLN C 223 -1 O LEU C 222 N PHE C 210
SHEET 1 AA7 9 LEU D 55 GLY D 60 0
SHEET 2 AA7 9 LEU D 88 ARG D 93 1 O VAL D 91 N VAL D 57
SHEET 3 AA7 9 LEU D 141 ALA D 145 1 O ALA D 142 N MET D 92
SHEET 4 AA7 9 TRP D 160 ILE D 163 1 O ALA D 162 N ALA D 145
SHEET 5 AA7 9 VAL D 184 LYS D 187 1 O LYS D 187 N ILE D 163
SHEET 6 AA7 9 GLY D 230 LEU D 234 1 O ILE D 233 N PHE D 186
SHEET 7 AA7 9 LEU D 263 ASP D 266 1 O MET D 264 N LEU D 234
SHEET 8 AA7 9 ILE D 297 GLU D 303 1 O ILE D 298 N LEU D 263
SHEET 9 AA7 9 LEU D 55 GLY D 60 1 N LEU D 56 O ILE D 298
SHEET 1 AA8 2 ARG D 209 ILE D 213 0
SHEET 2 AA8 2 VAL D 219 GLN D 223 -1 O LEU D 222 N PHE D 210
SSBOND 1 CYS A 62 CYS A 330 1555 1555 2.90
SSBOND 2 CYS B 62 CYS B 330 1555 1555 2.04
SSBOND 3 CYS C 62 CYS C 330 1555 1555 2.04
SSBOND 4 CYS D 62 CYS D 330 1555 1555 2.04
SITE 1 AC1 11 PRO A 148 PRO A 151 GLN A 152 GLY A 179
SITE 2 AC1 11 LEU A 180 SER A 181 PHE A 210 GLY A 212
SITE 3 AC1 11 ILE A 213 LEU A 222 HOH A 777
SITE 1 AC2 9 PRO B 148 PRO B 151 GLN B 152 GLY B 179
SITE 2 AC2 9 LEU B 180 SER B 181 GLY B 212 ILE B 213
SITE 3 AC2 9 LEU B 222
SITE 1 AC3 10 PRO C 148 PRO C 151 GLN C 152 GLY C 179
SITE 2 AC3 10 LEU C 180 SER C 181 GLY C 212 ILE C 213
SITE 3 AC3 10 LEU C 222 HOH C 750
SITE 1 AC4 10 PRO D 148 PRO D 151 GLN D 152 GLY D 179
SITE 2 AC4 10 LEU D 180 SER D 181 GLY D 212 ILE D 213
SITE 3 AC4 10 LEU D 222 HOH D 746
CRYST1 54.189 133.859 87.670 90.00 91.23 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 0.018454 0.000000 0.000398 0.00000
SCALE2 0.000000 0.007471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011409 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
