HEADER LIGASE/LIGASE INHIBITOR 25-MAR-14 4P72
TITLE PHERS IN COMPLEX WITH COMPOUND 2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLALANINE--TRNA LIGASE BETA SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHENYLALANYL-TRNA SYNTHETASE BETA SUBUNIT,PHERS;
COMPND 5 EC: 6.1.1.20;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT;
COMPND 9 CHAIN: C, D;
COMPND 10 SYNONYM: PHENYLALANYL-TRNA SYNTHETASE ALPHA SUBUNIT,PHERS;
COMPND 11 EC: 6.1.1.20;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: PHET, PA2739;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 10 ORGANISM_TAXID: 208964;
SOURCE 11 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 12 GENE: PHES, PA2740;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHENYLALANINE TRNA SYNTHETASE, PHERS, LIGASE-LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.D.FERGUSON
REVDAT 4 27-SEP-23 4P72 1 REMARK
REVDAT 3 22-NOV-17 4P72 1 SOURCE JRNL REMARK
REVDAT 2 01-OCT-14 4P72 1 JRNL
REVDAT 1 25-JUN-14 4P72 0
JRNL AUTH A.ABIBI,A.D.FERGUSON,P.R.FLEMING,N.GAO,L.I.HAJEC,J.HU,
JRNL AUTH 2 V.A.LAGANAS,D.C.MCKINNEY,S.M.MCLEOD,D.B.PRINCE,A.B.SHAPIRO,
JRNL AUTH 3 E.T.BUURMAN
JRNL TITL THE ROLE OF A NOVEL AUXILIARY POCKET IN BACTERIAL
JRNL TITL 2 PHENYLALANYL-TRNA SYNTHETASE DRUGGABILITY.
JRNL REF J.BIOL.CHEM. V. 289 21651 2014
JRNL REFN ESSN 1083-351X
JRNL PMID 24936059
JRNL DOI 10.1074/JBC.M114.574061
REMARK 2
REMARK 2 RESOLUTION. 2.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 76026
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3822
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.14
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5166
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2337
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4928
REMARK 3 BIN R VALUE (WORKING SET) : 0.2315
REMARK 3 BIN FREE R VALUE : 0.2795
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.61
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 238
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16057
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 86
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.13950
REMARK 3 B22 (A**2) : 11.26260
REMARK 3 B33 (A**2) : -7.12310
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.36790
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.349
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.482
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.255
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.577
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.267
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 16435 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 22296 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5732 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 425 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2461 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 16435 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 2063 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 18350 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.15
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.83
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 51.1416 33.6855 28.6573
REMARK 3 T TENSOR
REMARK 3 T11: 0.1728 T22: 0.0875
REMARK 3 T33: 0.1467 T12: 0.0017
REMARK 3 T13: 0.0278 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.3177 L22: 0.5256
REMARK 3 L33: 0.0488 L12: -0.2999
REMARK 3 L13: 0.0735 L23: 0.0907
REMARK 3 S TENSOR
REMARK 3 S11: -0.0442 S12: -0.0373 S13: -0.0110
REMARK 3 S21: 0.0262 S22: 0.0402 S23: -0.0500
REMARK 3 S31: -0.0145 S32: -0.0216 S33: 0.0039
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 50.6142 -32.1122 21.5939
REMARK 3 T TENSOR
REMARK 3 T11: 0.1331 T22: 0.0410
REMARK 3 T33: 0.1408 T12: 0.0064
REMARK 3 T13: -0.0039 T23: 0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 0.3314 L22: 0.4868
REMARK 3 L33: 0.2886 L12: 0.1671
REMARK 3 L13: 0.0829 L23: 0.2465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: -0.0700 S13: -0.0328
REMARK 3 S21: 0.1211 S22: -0.0323 S23: -0.0201
REMARK 3 S31: 0.0254 S32: -0.0588 S33: -0.0128
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9333 19.4199 25.6742
REMARK 3 T TENSOR
REMARK 3 T11: 0.1723 T22: -0.0389
REMARK 3 T33: 0.1786 T12: 0.0137
REMARK 3 T13: 0.0624 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.5916 L22: 0.6797
REMARK 3 L33: 0.7959 L12: -0.3314
REMARK 3 L13: 0.3514 L23: 0.0220
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0263 S13: 0.0318
REMARK 3 S21: 0.0615 S22: 0.0920 S23: 0.1148
REMARK 3 S31: -0.0813 S32: -0.0515 S33: -0.1038
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8843 -17.6529 23.2367
REMARK 3 T TENSOR
REMARK 3 T11: 0.2329 T22: 0.0215
REMARK 3 T33: 0.2003 T12: 0.0021
REMARK 3 T13: -0.0025 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 2.1246 L22: 0.7823
REMARK 3 L33: 0.7149 L12: 0.3979
REMARK 3 L13: 0.4482 L23: 0.3082
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: -0.0375 S13: -0.0628
REMARK 3 S21: 0.0797 S22: -0.0358 S23: -0.0178
REMARK 3 S31: 0.0863 S32: -0.0440 S33: -0.0262
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4P72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620
REMARK 200 RESOLUTION RANGE LOW (A) : 75.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4P71
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.2M AMMONIUM CITRATE TR
REMARK 280 -BASIC (PH 6.2), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 56.65000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 109.41500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.65000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 109.41500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 24520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 81620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 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 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 792
REMARK 465 LYS B 792
REMARK 465 MET C -78
REMARK 465 GLU C -77
REMARK 465 ASN C -76
REMARK 465 LEU C -75
REMARK 465 ASP C -74
REMARK 465 ALA C -73
REMARK 465 LEU C -72
REMARK 465 VAL C -71
REMARK 465 SER C -70
REMARK 465 GLN C -69
REMARK 465 ALA C -68
REMARK 465 LEU C -67
REMARK 465 GLU C -66
REMARK 465 ALA C -65
REMARK 465 VAL C -64
REMARK 465 ARG C -63
REMARK 465 HIS C -62
REMARK 465 THR C -61
REMARK 465 GLU C -60
REMARK 465 ASP C -59
REMARK 465 VAL C -58
REMARK 465 ASN C -57
REMARK 465 ALA C -56
REMARK 465 LEU C -55
REMARK 465 GLU C -54
REMARK 465 GLN C -53
REMARK 465 ILE C -52
REMARK 465 ARG C -51
REMARK 465 VAL C -50
REMARK 465 HIS C -49
REMARK 465 TYR C -48
REMARK 465 LEU C -47
REMARK 465 GLY C -46
REMARK 465 LYS C -45
REMARK 465 LYS C -44
REMARK 465 GLY C -43
REMARK 465 GLU C -42
REMARK 465 LEU C -41
REMARK 465 THR C -40
REMARK 465 GLN C -39
REMARK 465 VAL C -38
REMARK 465 MET C -37
REMARK 465 LYS C -36
REMARK 465 THR C -35
REMARK 465 LEU C -34
REMARK 465 GLY C -33
REMARK 465 ASP C -32
REMARK 465 LEU C -31
REMARK 465 PRO C -30
REMARK 465 ALA C -29
REMARK 465 GLU C -28
REMARK 465 GLU C -27
REMARK 465 ARG C -26
REMARK 465 PRO C -25
REMARK 465 LYS C -24
REMARK 465 VAL C -23
REMARK 465 GLY C -22
REMARK 465 ALA C -21
REMARK 465 LEU C -20
REMARK 465 ILE C -19
REMARK 465 ASN C -18
REMARK 465 VAL C -17
REMARK 465 ALA C -16
REMARK 465 LYS C -15
REMARK 465 GLU C -14
REMARK 465 LYS C -13
REMARK 465 VAL C -12
REMARK 465 GLN C -11
REMARK 465 ASP C -10
REMARK 465 VAL C -9
REMARK 465 LEU C -8
REMARK 465 ASN C -7
REMARK 465 ALA C -6
REMARK 465 ARG C -5
REMARK 465 LYS C -4
REMARK 465 THR C -3
REMARK 465 GLU C -2
REMARK 465 LEU C -1
REMARK 465 GLU C 0
REMARK 465 GLY C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 3
REMARK 465 LEU C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 6
REMARK 465 ARG C 7
REMARK 465 LEU C 8
REMARK 465 ALA C 9
REMARK 465 ALA C 10
REMARK 465 VAL C 183
REMARK 465 ILE C 184
REMARK 465 CYS C 185
REMARK 465 SER C 186
REMARK 465 GLY C 187
REMARK 465 ASN C 188
REMARK 465 GLY C 189
REMARK 465 CYS C 190
REMARK 465 ARG C 191
REMARK 465 VAL C 192
REMARK 465 CYS C 193
REMARK 465 LYS C 194
REMARK 465 GLN C 195
REMARK 465 THR C 196
REMARK 465 MET D -78
REMARK 465 GLU D -77
REMARK 465 ASN D -76
REMARK 465 LEU D -75
REMARK 465 ASP D -74
REMARK 465 ALA D -73
REMARK 465 LEU D -72
REMARK 465 VAL D -71
REMARK 465 SER D -70
REMARK 465 GLN D -69
REMARK 465 ALA D -68
REMARK 465 LEU D -67
REMARK 465 GLU D -66
REMARK 465 ALA D -65
REMARK 465 VAL D -64
REMARK 465 ARG D -63
REMARK 465 HIS D -62
REMARK 465 THR D -61
REMARK 465 GLU D -60
REMARK 465 ASP D -59
REMARK 465 VAL D -58
REMARK 465 ASN D -57
REMARK 465 ALA D -56
REMARK 465 LEU D -55
REMARK 465 GLU D -54
REMARK 465 GLN D -53
REMARK 465 ILE D -52
REMARK 465 ARG D -51
REMARK 465 VAL D -50
REMARK 465 HIS D -49
REMARK 465 TYR D -48
REMARK 465 LEU D -47
REMARK 465 GLY D -46
REMARK 465 LYS D -45
REMARK 465 LYS D -44
REMARK 465 GLY D -43
REMARK 465 GLU D -42
REMARK 465 LEU D -41
REMARK 465 THR D -40
REMARK 465 GLN D -39
REMARK 465 VAL D -38
REMARK 465 MET D -37
REMARK 465 LYS D -36
REMARK 465 THR D -35
REMARK 465 LEU D -34
REMARK 465 GLY D -33
REMARK 465 ASP D -32
REMARK 465 LEU D -31
REMARK 465 PRO D -30
REMARK 465 ALA D -29
REMARK 465 GLU D -28
REMARK 465 GLU D -27
REMARK 465 ARG D -26
REMARK 465 PRO D -25
REMARK 465 LYS D -24
REMARK 465 VAL D -23
REMARK 465 GLY D -22
REMARK 465 ALA D -21
REMARK 465 LEU D -20
REMARK 465 ILE D -19
REMARK 465 ASN D -18
REMARK 465 VAL D -17
REMARK 465 ALA D -16
REMARK 465 LYS D -15
REMARK 465 GLU D -14
REMARK 465 LYS D -13
REMARK 465 VAL D -12
REMARK 465 GLN D -11
REMARK 465 ASP D -10
REMARK 465 VAL D -9
REMARK 465 LEU D -8
REMARK 465 ASN D -7
REMARK 465 ALA D -6
REMARK 465 ARG D -5
REMARK 465 LYS D -4
REMARK 465 THR D -3
REMARK 465 GLU D -2
REMARK 465 LEU D -1
REMARK 465 GLU D 0
REMARK 465 GLY D 1
REMARK 465 ALA D 2
REMARK 465 ALA D 3
REMARK 465 LEU D 4
REMARK 465 ALA D 5
REMARK 465 ALA D 6
REMARK 465 ARG D 7
REMARK 465 GLY D 189
REMARK 465 CYS D 190
REMARK 465 ARG D 191
REMARK 465 VAL D 192
REMARK 465 CYS D 193
REMARK 465 LYS D 194
REMARK 465 GLN D 195
REMARK 465 THR D 196
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 O ILE A 94 O ILE A 104 2.12
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 ARG B 575 CB - CA - C ANGL. DEV. = -15.0 DEGREES
REMARK 500 SER C 119 C - N - CA ANGL. DEV. = 20.7 DEGREES
REMARK 500 ARG D 153 CD - NE - CZ ANGL. DEV. = 9.1 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 ALA A 59 109.01 -165.38
REMARK 500 PHE A 115 49.04 -105.75
REMARK 500 LEU A 134 95.49 -67.25
REMARK 500 ARG A 165 50.56 -108.21
REMARK 500 LEU A 169 31.20 -88.70
REMARK 500 ASP A 305 -157.72 -108.50
REMARK 500 VAL A 315 -62.54 -128.73
REMARK 500 SER A 456 -20.04 -140.18
REMARK 500 MET A 541 38.50 -140.78
REMARK 500 ARG A 606 30.98 -99.19
REMARK 500 ALA B 59 109.88 -166.80
REMARK 500 PHE B 115 49.42 -106.24
REMARK 500 LEU B 134 94.63 -67.42
REMARK 500 ARG B 165 51.97 -109.11
REMARK 500 LEU B 169 30.93 -88.58
REMARK 500 ASP B 305 -158.53 -108.63
REMARK 500 VAL B 315 -62.31 -128.65
REMARK 500 SER B 456 -19.90 -141.99
REMARK 500 MET B 541 38.86 -142.37
REMARK 500 ARG B 606 32.16 -98.92
REMARK 500 ARG C 12 32.31 -93.08
REMARK 500 PHE C 61 -63.07 -125.40
REMARK 500 LEU C 121 -112.69 44.64
REMARK 500 THR C 122 -10.11 -46.98
REMARK 500 SER C 167 -155.53 -130.58
REMARK 500 GLU C 173 116.58 -168.21
REMARK 500 PHE D 61 -63.63 -125.79
REMARK 500 ASP D 118 103.79 -51.91
REMARK 500 ASP D 120 -148.89 164.94
REMARK 500 THR D 122 -19.40 58.47
REMARK 500 SER D 167 -156.78 -130.97
REMARK 500 GLU D 173 114.28 -169.46
REMARK 500 CYS D 185 -169.99 53.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 GLU A 386 0.07 SIDE CHAIN
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 2NL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2NL D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P71 RELATED DB: PDB
REMARK 900 RELATED ID: 4P73 RELATED DB: PDB
REMARK 900 RELATED ID: 4P74 RELATED DB: PDB
REMARK 900 RELATED ID: 4P75 RELATED DB: PDB
DBREF 4P72 A 1 792 UNP Q9I0A4 SYFB_PSEAE 1 792
DBREF 4P72 B 1 792 UNP Q9I0A4 SYFB_PSEAE 1 792
DBREF 4P72 C -78 259 UNP Q9I0A3 SYFA_PSEAE 1 338
DBREF 4P72 D -78 259 UNP Q9I0A3 SYFA_PSEAE 1 338
SEQRES 1 A 792 MET LYS PHE SER GLU LYS TRP LEU ARG SER TRP ALA ASN
SEQRES 2 A 792 PRO GLN VAL SER HIS ASP GLU LEU VAL ALA ARG LEU SER
SEQRES 3 A 792 MET VAL GLY LEU GLU VAL ASP ALA ASP LEU PRO VAL ALA
SEQRES 4 A 792 GLY ALA PHE SER GLY VAL VAL VAL GLY GLU VAL LEU SER
SEQRES 5 A 792 THR GLU GLN HIS PRO ASP ALA ASP LYS LEU ARG VAL CYS
SEQRES 6 A 792 GLN VAL SER ASN GLY SER GLU THR PHE GLN VAL VAL CYS
SEQRES 7 A 792 GLY ALA PRO ASN VAL ARG ALA GLY LEU LYS ILE PRO PHE
SEQRES 8 A 792 ALA MET ILE GLY ALA GLU LEU PRO ASP ASP PHE LYS ILE
SEQRES 9 A 792 LYS LYS ALA LYS LEU ARG GLY VAL GLU SER PHE GLY MET
SEQRES 10 A 792 LEU CYS SER ALA LYS GLU LEU GLN ILE SER GLU GLU ASN
SEQRES 11 A 792 ALA GLY LEU LEU GLU LEU PRO ALA ASP ALA PRO VAL GLY
SEQRES 12 A 792 GLN ASP VAL ARG THR TYR LEU GLU LEU ALA ASP TYR THR
SEQRES 13 A 792 ILE GLU VAL GLY LEU THR PRO ASN ARG GLY ASP CYS LEU
SEQRES 14 A 792 SER LEU ALA GLY LEU ALA ARG GLU VAL SER ALA ILE TYR
SEQRES 15 A 792 ASP VAL PRO LEU ALA PRO VAL ALA VAL ASP ALA VAL ALA
SEQRES 16 A 792 ALA GLN HIS ASP GLU THR ARG PRO VAL GLU LEU ALA ALA
SEQRES 17 A 792 PRO ALA ALA CYS PRO ARG TYR LEU GLY ARG VAL ILE ARG
SEQRES 18 A 792 ASN VAL ASP LEU SER ARG PRO THR PRO LEU TRP MET VAL
SEQRES 19 A 792 GLU ARG LEU ARG ARG SER ASP ILE ARG SER ILE ASP PRO
SEQRES 20 A 792 VAL VAL ASP VAL THR ASN TYR VAL MET ILE GLU LEU GLY
SEQRES 21 A 792 GLN PRO MET HIS ALA PHE ASP LEU ALA GLU ILE ASN GLY
SEQRES 22 A 792 GLY VAL ARG VAL ARG MET ALA GLU ASP GLY GLU LYS LEU
SEQRES 23 A 792 VAL LEU LEU ASP GLY GLN GLU ILE THR LEU ARG ALA ASP
SEQRES 24 A 792 THR LEU VAL ILE ALA ASP HIS GLN ARG ALA LEU ALA ILE
SEQRES 25 A 792 ALA GLY VAL MET GLY GLY GLU HIS SER GLY VAL SER ASP
SEQRES 26 A 792 SER THR ARG ASP LEU PHE LEU GLU ALA ALA PHE PHE ASP
SEQRES 27 A 792 THR ILE ALA LEU ALA GLY LYS ALA ARG SER TYR GLY LEU
SEQRES 28 A 792 HIS THR ASP SER SER HIS ARG PHE GLU ARG GLY VAL ASP
SEQRES 29 A 792 SER GLN LEU ALA ARG LYS ALA MET GLU ARG ALA THR ARG
SEQRES 30 A 792 LEU ILE LEU ASP ILE VAL GLY GLY GLU PRO GLY PRO ILE
SEQRES 31 A 792 VAL GLU GLN VAL SER GLU ALA HIS LEU PRO LYS VAL ALA
SEQRES 32 A 792 PRO ILE THR LEU ARG ALA GLU ARG VAL THR GLN MET LEU
SEQRES 33 A 792 GLY MET PRO LEU ASP ALA ALA GLU ILE VAL ARG LEU LEU
SEQRES 34 A 792 GLN ALA LEU GLU LEU THR VAL VAL ALA ASP GLY GLU GLY
SEQRES 35 A 792 GLN TRP SER VAL GLY VAL PRO SER HIS ARG PHE ASP ILE
SEQRES 36 A 792 SER LEU GLU VAL ASP LEU ILE GLU GLU LEU ALA ARG LEU
SEQRES 37 A 792 TYR GLY TYR ASN ARG LEU PRO VAL ARG TYR PRO GLN ALA
SEQRES 38 A 792 ARG LEU ALA PRO ASN ASN LYS PRO GLU ALA ARG ALA ALA
SEQRES 39 A 792 LEU PRO LEU LEU ARG ARG LEU LEU VAL ALA ARG GLY TYR
SEQRES 40 A 792 GLN GLU ALA ILE THR PHE SER PHE ILE ASP PRO ALA LEU
SEQRES 41 A 792 PHE GLU LEU PHE ASP PRO GLY THR GLN PRO LEU THR LEU
SEQRES 42 A 792 ALA ASN PRO ILE SER ALA ASP MET ALA ALA MET ARG SER
SEQRES 43 A 792 SER LEU TRP PRO GLY LEU VAL LYS ALA LEU GLN HIS ASN
SEQRES 44 A 792 LEU ASN ARG GLN GLN SER ARG VAL ARG LEU PHE GLU SER
SEQRES 45 A 792 GLY LEU ARG PHE VAL GLY GLN LEU GLU GLY LEU LYS GLN
SEQRES 46 A 792 GLU ALA MET LEU ALA GLY ALA ILE CYS GLY LYS ARG LEU
SEQRES 47 A 792 PRO GLU GLY TRP ALA ASN GLY ARG ASP GLY VAL ASP PHE
SEQRES 48 A 792 PHE ASP ALA LYS ALA ASP VAL GLU ALA VAL LEU ALA SER
SEQRES 49 A 792 ALA GLY ALA LEU GLY ASP PHE SER PHE VAL PRO GLY GLU
SEQRES 50 A 792 HIS PRO ALA LEU HIS PRO GLY GLN THR ALA ARG ILE GLU
SEQRES 51 A 792 ARG GLU GLY ARG LEU VAL GLY TYR LEU GLY ALA LEU HIS
SEQRES 52 A 792 PRO GLU LEU ALA LYS LYS LEU ASP LEU GLU GLN PRO VAL
SEQRES 53 A 792 PHE LEU PHE GLU LEU LEU LEU ALA GLU VAL VAL ASP GLY
SEQRES 54 A 792 HIS LEU PRO LYS PHE ARG GLU LEU SER ARG PHE PRO GLU
SEQRES 55 A 792 VAL ARG ARG ASP LEU ALA LEU LEU VAL ASP GLN ASP VAL
SEQRES 56 A 792 PRO ALA GLN ASP ILE LEU THR GLN ILE ARG ALA ALA ALA
SEQRES 57 A 792 GLY GLU TRP LEU THR ASP LEU ARG LEU PHE ASP VAL TYR
SEQRES 58 A 792 HIS GLY LYS GLY ILE ASP PRO HIS ARG LYS SER LEU ALA
SEQRES 59 A 792 VAL GLY LEU THR TRP GLN HIS PRO SER ARG THR LEU ASN
SEQRES 60 A 792 ASP ASP GLU VAL ASN SER THR THR GLN ASN ILE VAL THR
SEQRES 61 A 792 SER LEU GLU GLU ARG PHE ASN ALA THR LEU ARG LYS
SEQRES 1 B 792 MET LYS PHE SER GLU LYS TRP LEU ARG SER TRP ALA ASN
SEQRES 2 B 792 PRO GLN VAL SER HIS ASP GLU LEU VAL ALA ARG LEU SER
SEQRES 3 B 792 MET VAL GLY LEU GLU VAL ASP ALA ASP LEU PRO VAL ALA
SEQRES 4 B 792 GLY ALA PHE SER GLY VAL VAL VAL GLY GLU VAL LEU SER
SEQRES 5 B 792 THR GLU GLN HIS PRO ASP ALA ASP LYS LEU ARG VAL CYS
SEQRES 6 B 792 GLN VAL SER ASN GLY SER GLU THR PHE GLN VAL VAL CYS
SEQRES 7 B 792 GLY ALA PRO ASN VAL ARG ALA GLY LEU LYS ILE PRO PHE
SEQRES 8 B 792 ALA MET ILE GLY ALA GLU LEU PRO ASP ASP PHE LYS ILE
SEQRES 9 B 792 LYS LYS ALA LYS LEU ARG GLY VAL GLU SER PHE GLY MET
SEQRES 10 B 792 LEU CYS SER ALA LYS GLU LEU GLN ILE SER GLU GLU ASN
SEQRES 11 B 792 ALA GLY LEU LEU GLU LEU PRO ALA ASP ALA PRO VAL GLY
SEQRES 12 B 792 GLN ASP VAL ARG THR TYR LEU GLU LEU ALA ASP TYR THR
SEQRES 13 B 792 ILE GLU VAL GLY LEU THR PRO ASN ARG GLY ASP CYS LEU
SEQRES 14 B 792 SER LEU ALA GLY LEU ALA ARG GLU VAL SER ALA ILE TYR
SEQRES 15 B 792 ASP VAL PRO LEU ALA PRO VAL ALA VAL ASP ALA VAL ALA
SEQRES 16 B 792 ALA GLN HIS ASP GLU THR ARG PRO VAL GLU LEU ALA ALA
SEQRES 17 B 792 PRO ALA ALA CYS PRO ARG TYR LEU GLY ARG VAL ILE ARG
SEQRES 18 B 792 ASN VAL ASP LEU SER ARG PRO THR PRO LEU TRP MET VAL
SEQRES 19 B 792 GLU ARG LEU ARG ARG SER ASP ILE ARG SER ILE ASP PRO
SEQRES 20 B 792 VAL VAL ASP VAL THR ASN TYR VAL MET ILE GLU LEU GLY
SEQRES 21 B 792 GLN PRO MET HIS ALA PHE ASP LEU ALA GLU ILE ASN GLY
SEQRES 22 B 792 GLY VAL ARG VAL ARG MET ALA GLU ASP GLY GLU LYS LEU
SEQRES 23 B 792 VAL LEU LEU ASP GLY GLN GLU ILE THR LEU ARG ALA ASP
SEQRES 24 B 792 THR LEU VAL ILE ALA ASP HIS GLN ARG ALA LEU ALA ILE
SEQRES 25 B 792 ALA GLY VAL MET GLY GLY GLU HIS SER GLY VAL SER ASP
SEQRES 26 B 792 SER THR ARG ASP LEU PHE LEU GLU ALA ALA PHE PHE ASP
SEQRES 27 B 792 THR ILE ALA LEU ALA GLY LYS ALA ARG SER TYR GLY LEU
SEQRES 28 B 792 HIS THR ASP SER SER HIS ARG PHE GLU ARG GLY VAL ASP
SEQRES 29 B 792 SER GLN LEU ALA ARG LYS ALA MET GLU ARG ALA THR ARG
SEQRES 30 B 792 LEU ILE LEU ASP ILE VAL GLY GLY GLU PRO GLY PRO ILE
SEQRES 31 B 792 VAL GLU GLN VAL SER GLU ALA HIS LEU PRO LYS VAL ALA
SEQRES 32 B 792 PRO ILE THR LEU ARG ALA GLU ARG VAL THR GLN MET LEU
SEQRES 33 B 792 GLY MET PRO LEU ASP ALA ALA GLU ILE VAL ARG LEU LEU
SEQRES 34 B 792 GLN ALA LEU GLU LEU THR VAL VAL ALA ASP GLY GLU GLY
SEQRES 35 B 792 GLN TRP SER VAL GLY VAL PRO SER HIS ARG PHE ASP ILE
SEQRES 36 B 792 SER LEU GLU VAL ASP LEU ILE GLU GLU LEU ALA ARG LEU
SEQRES 37 B 792 TYR GLY TYR ASN ARG LEU PRO VAL ARG TYR PRO GLN ALA
SEQRES 38 B 792 ARG LEU ALA PRO ASN ASN LYS PRO GLU ALA ARG ALA ALA
SEQRES 39 B 792 LEU PRO LEU LEU ARG ARG LEU LEU VAL ALA ARG GLY TYR
SEQRES 40 B 792 GLN GLU ALA ILE THR PHE SER PHE ILE ASP PRO ALA LEU
SEQRES 41 B 792 PHE GLU LEU PHE ASP PRO GLY THR GLN PRO LEU THR LEU
SEQRES 42 B 792 ALA ASN PRO ILE SER ALA ASP MET ALA ALA MET ARG SER
SEQRES 43 B 792 SER LEU TRP PRO GLY LEU VAL LYS ALA LEU GLN HIS ASN
SEQRES 44 B 792 LEU ASN ARG GLN GLN SER ARG VAL ARG LEU PHE GLU SER
SEQRES 45 B 792 GLY LEU ARG PHE VAL GLY GLN LEU GLU GLY LEU LYS GLN
SEQRES 46 B 792 GLU ALA MET LEU ALA GLY ALA ILE CYS GLY LYS ARG LEU
SEQRES 47 B 792 PRO GLU GLY TRP ALA ASN GLY ARG ASP GLY VAL ASP PHE
SEQRES 48 B 792 PHE ASP ALA LYS ALA ASP VAL GLU ALA VAL LEU ALA SER
SEQRES 49 B 792 ALA GLY ALA LEU GLY ASP PHE SER PHE VAL PRO GLY GLU
SEQRES 50 B 792 HIS PRO ALA LEU HIS PRO GLY GLN THR ALA ARG ILE GLU
SEQRES 51 B 792 ARG GLU GLY ARG LEU VAL GLY TYR LEU GLY ALA LEU HIS
SEQRES 52 B 792 PRO GLU LEU ALA LYS LYS LEU ASP LEU GLU GLN PRO VAL
SEQRES 53 B 792 PHE LEU PHE GLU LEU LEU LEU ALA GLU VAL VAL ASP GLY
SEQRES 54 B 792 HIS LEU PRO LYS PHE ARG GLU LEU SER ARG PHE PRO GLU
SEQRES 55 B 792 VAL ARG ARG ASP LEU ALA LEU LEU VAL ASP GLN ASP VAL
SEQRES 56 B 792 PRO ALA GLN ASP ILE LEU THR GLN ILE ARG ALA ALA ALA
SEQRES 57 B 792 GLY GLU TRP LEU THR ASP LEU ARG LEU PHE ASP VAL TYR
SEQRES 58 B 792 HIS GLY LYS GLY ILE ASP PRO HIS ARG LYS SER LEU ALA
SEQRES 59 B 792 VAL GLY LEU THR TRP GLN HIS PRO SER ARG THR LEU ASN
SEQRES 60 B 792 ASP ASP GLU VAL ASN SER THR THR GLN ASN ILE VAL THR
SEQRES 61 B 792 SER LEU GLU GLU ARG PHE ASN ALA THR LEU ARG LYS
SEQRES 1 C 338 MET GLU ASN LEU ASP ALA LEU VAL SER GLN ALA LEU GLU
SEQRES 2 C 338 ALA VAL ARG HIS THR GLU ASP VAL ASN ALA LEU GLU GLN
SEQRES 3 C 338 ILE ARG VAL HIS TYR LEU GLY LYS LYS GLY GLU LEU THR
SEQRES 4 C 338 GLN VAL MET LYS THR LEU GLY ASP LEU PRO ALA GLU GLU
SEQRES 5 C 338 ARG PRO LYS VAL GLY ALA LEU ILE ASN VAL ALA LYS GLU
SEQRES 6 C 338 LYS VAL GLN ASP VAL LEU ASN ALA ARG LYS THR GLU LEU
SEQRES 7 C 338 GLU GLY ALA ALA LEU ALA ALA ARG LEU ALA ALA GLU ARG
SEQRES 8 C 338 ILE ASP VAL THR LEU PRO GLY ARG GLY GLN LEU SER GLY
SEQRES 9 C 338 GLY LEU HIS PRO VAL THR ARG THR LEU GLU ARG ILE GLU
SEQRES 10 C 338 GLN CYS PHE SER ARG ILE GLY TYR GLU VAL ALA GLU GLY
SEQRES 11 C 338 PRO GLU VAL GLU ASP ASP TYR HIS ASN PHE GLU ALA LEU
SEQRES 12 C 338 ASN ILE PRO GLY HIS HIS PRO ALA ARG ALA MET HIS ASP
SEQRES 13 C 338 THR PHE TYR PHE ASN ALA ASN MET LEU LEU ARG THR HIS
SEQRES 14 C 338 THR SER PRO VAL GLN VAL ARG THR MET GLU SER GLN GLN
SEQRES 15 C 338 PRO PRO ILE ARG ILE VAL CYS PRO GLY ARG VAL TYR ARG
SEQRES 16 C 338 CYS ASP SER ASP LEU THR HIS SER PRO MET PHE HIS GLN
SEQRES 17 C 338 VAL GLU GLY LEU LEU VAL ASP GLU GLY VAL SER PHE ALA
SEQRES 18 C 338 ASP LEU LYS GLY THR ILE GLU GLU PHE LEU ARG ALA PHE
SEQRES 19 C 338 PHE GLU LYS GLN LEU GLU VAL ARG PHE ARG PRO SER PHE
SEQRES 20 C 338 PHE PRO PHE THR GLU PRO SER ALA GLU VAL ASP ILE GLN
SEQRES 21 C 338 CYS VAL ILE CYS SER GLY ASN GLY CYS ARG VAL CYS LYS
SEQRES 22 C 338 GLN THR GLY TRP LEU GLU VAL MET GLY CYS GLY MET VAL
SEQRES 23 C 338 HIS PRO ASN VAL LEU ARG MET SER ASN ILE ASP PRO GLU
SEQRES 24 C 338 LYS PHE GLN GLY PHE ALA PHE GLY MET GLY ALA GLU ARG
SEQRES 25 C 338 LEU ALA MET LEU ARG TYR GLY VAL ASN ASP LEU ARG LEU
SEQRES 26 C 338 PHE PHE ASP ASN ASP LEU ARG PHE LEU GLY GLN PHE ARG
SEQRES 1 D 338 MET GLU ASN LEU ASP ALA LEU VAL SER GLN ALA LEU GLU
SEQRES 2 D 338 ALA VAL ARG HIS THR GLU ASP VAL ASN ALA LEU GLU GLN
SEQRES 3 D 338 ILE ARG VAL HIS TYR LEU GLY LYS LYS GLY GLU LEU THR
SEQRES 4 D 338 GLN VAL MET LYS THR LEU GLY ASP LEU PRO ALA GLU GLU
SEQRES 5 D 338 ARG PRO LYS VAL GLY ALA LEU ILE ASN VAL ALA LYS GLU
SEQRES 6 D 338 LYS VAL GLN ASP VAL LEU ASN ALA ARG LYS THR GLU LEU
SEQRES 7 D 338 GLU GLY ALA ALA LEU ALA ALA ARG LEU ALA ALA GLU ARG
SEQRES 8 D 338 ILE ASP VAL THR LEU PRO GLY ARG GLY GLN LEU SER GLY
SEQRES 9 D 338 GLY LEU HIS PRO VAL THR ARG THR LEU GLU ARG ILE GLU
SEQRES 10 D 338 GLN CYS PHE SER ARG ILE GLY TYR GLU VAL ALA GLU GLY
SEQRES 11 D 338 PRO GLU VAL GLU ASP ASP TYR HIS ASN PHE GLU ALA LEU
SEQRES 12 D 338 ASN ILE PRO GLY HIS HIS PRO ALA ARG ALA MET HIS ASP
SEQRES 13 D 338 THR PHE TYR PHE ASN ALA ASN MET LEU LEU ARG THR HIS
SEQRES 14 D 338 THR SER PRO VAL GLN VAL ARG THR MET GLU SER GLN GLN
SEQRES 15 D 338 PRO PRO ILE ARG ILE VAL CYS PRO GLY ARG VAL TYR ARG
SEQRES 16 D 338 CYS ASP SER ASP LEU THR HIS SER PRO MET PHE HIS GLN
SEQRES 17 D 338 VAL GLU GLY LEU LEU VAL ASP GLU GLY VAL SER PHE ALA
SEQRES 18 D 338 ASP LEU LYS GLY THR ILE GLU GLU PHE LEU ARG ALA PHE
SEQRES 19 D 338 PHE GLU LYS GLN LEU GLU VAL ARG PHE ARG PRO SER PHE
SEQRES 20 D 338 PHE PRO PHE THR GLU PRO SER ALA GLU VAL ASP ILE GLN
SEQRES 21 D 338 CYS VAL ILE CYS SER GLY ASN GLY CYS ARG VAL CYS LYS
SEQRES 22 D 338 GLN THR GLY TRP LEU GLU VAL MET GLY CYS GLY MET VAL
SEQRES 23 D 338 HIS PRO ASN VAL LEU ARG MET SER ASN ILE ASP PRO GLU
SEQRES 24 D 338 LYS PHE GLN GLY PHE ALA PHE GLY MET GLY ALA GLU ARG
SEQRES 25 D 338 LEU ALA MET LEU ARG TYR GLY VAL ASN ASP LEU ARG LEU
SEQRES 26 D 338 PHE PHE ASP ASN ASP LEU ARG PHE LEU GLY GLN PHE ARG
HET 2NL C 301 20
HET 2NL D 301 20
HETNAM 2NL 2-{3-[(4-CHLOROPYRIDIN-2-YL)AMINO]PHENOXY}-N-
HETNAM 2 2NL METHYLACETAMIDE
FORMUL 5 2NL 2(C14 H14 CL N3 O2)
FORMUL 7 HOH *86(H2 O)
HELIX 1 AA1 GLU A 5 ALA A 12 1 8
HELIX 2 AA2 SER A 17 VAL A 28 1 12
HELIX 3 AA3 ALA A 121 GLN A 125 5 5
HELIX 4 AA4 ASP A 145 LEU A 150 1 6
HELIX 5 AA5 ARG A 165 LEU A 169 5 5
HELIX 6 AA6 SER A 170 ASP A 183 1 14
HELIX 7 AA7 PRO A 230 ARG A 239 1 10
HELIX 8 AA8 ASP A 246 GLY A 260 1 15
HELIX 9 AA9 ALA A 269 ILE A 271 5 3
HELIX 10 AB1 ASP A 338 ALA A 343 1 6
HELIX 11 AB2 ALA A 346 GLY A 350 5 5
HELIX 12 AB3 THR A 353 GLY A 362 1 10
HELIX 13 AB4 LEU A 367 GLY A 384 1 18
HELIX 14 AB5 GLU A 396 LEU A 399 5 4
HELIX 15 AB6 ALA A 409 GLY A 417 1 9
HELIX 16 AB7 ASP A 421 LEU A 432 1 12
HELIX 17 AB8 LEU A 457 GLY A 470 1 14
HELIX 18 AB9 TYR A 471 LEU A 474 5 4
HELIX 19 AC1 ALA A 494 ARG A 505 1 12
HELIX 20 AC2 ASP A 517 ASP A 525 1 9
HELIX 21 AC3 SER A 538 MET A 541 5 4
HELIX 22 AC4 LEU A 548 ASN A 561 1 14
HELIX 23 AC5 ASP A 610 ALA A 623 1 14
HELIX 24 AC6 ALA A 627 GLY A 629 5 3
HELIX 25 AC7 HIS A 663 LEU A 670 1 8
HELIX 26 AC8 ALA A 684 VAL A 686 5 3
HELIX 27 AC9 PRO A 716 ALA A 728 1 13
HELIX 28 AD1 ASN A 767 ASN A 787 1 21
HELIX 29 AD2 GLU B 5 ALA B 12 1 8
HELIX 30 AD3 SER B 17 VAL B 28 1 12
HELIX 31 AD4 ALA B 121 GLN B 125 5 5
HELIX 32 AD5 ASP B 145 LEU B 150 1 6
HELIX 33 AD6 ARG B 165 LEU B 169 5 5
HELIX 34 AD7 SER B 170 ASP B 183 1 14
HELIX 35 AD8 PRO B 230 ARG B 239 1 10
HELIX 36 AD9 ASP B 246 GLY B 260 1 15
HELIX 37 AE1 ALA B 269 ILE B 271 5 3
HELIX 38 AE2 ASP B 338 ALA B 343 1 6
HELIX 39 AE3 ALA B 346 GLY B 350 5 5
HELIX 40 AE4 THR B 353 GLY B 362 1 10
HELIX 41 AE5 LEU B 367 GLY B 384 1 18
HELIX 42 AE6 GLU B 396 LEU B 399 5 4
HELIX 43 AE7 ALA B 409 GLY B 417 1 9
HELIX 44 AE8 ASP B 421 LEU B 432 1 12
HELIX 45 AE9 LEU B 457 GLY B 470 1 14
HELIX 46 AF1 TYR B 471 LEU B 474 5 4
HELIX 47 AF2 ALA B 494 ARG B 505 1 12
HELIX 48 AF3 ASP B 517 ASP B 525 1 9
HELIX 49 AF4 SER B 538 MET B 541 5 4
HELIX 50 AF5 LEU B 548 ASN B 561 1 14
HELIX 51 AF6 ASP B 610 ALA B 623 1 14
HELIX 52 AF7 ALA B 627 GLY B 629 5 3
HELIX 53 AF8 HIS B 663 LEU B 670 1 8
HELIX 54 AF9 ALA B 684 VAL B 686 5 3
HELIX 55 AG1 PRO B 716 ALA B 728 1 13
HELIX 56 AG2 ASN B 767 ASN B 787 1 21
HELIX 57 AG3 HIS C 28 ARG C 43 1 16
HELIX 58 AG4 ASP C 57 PHE C 61 1 5
HELIX 59 AG5 GLU C 62 ASN C 65 5 4
HELIX 60 AG6 HIS C 70 ALA C 74 5 5
HELIX 61 AG7 THR C 91 GLN C 102 1 12
HELIX 62 AG8 SER C 140 PHE C 156 1 17
HELIX 63 AG9 HIS C 208 SER C 215 1 8
HELIX 64 AH1 ALA C 231 GLY C 240 1 10
HELIX 65 AH2 ARG C 245 ASN C 250 1 6
HELIX 66 AH3 ASP C 251 GLY C 256 1 6
HELIX 67 AH4 GLN C 257 ARG C 259 5 3
HELIX 68 AH5 HIS D 28 ARG D 43 1 16
HELIX 69 AH6 ASP D 57 PHE D 61 1 5
HELIX 70 AH7 GLU D 62 ASN D 65 5 4
HELIX 71 AH8 HIS D 70 ALA D 74 5 5
HELIX 72 AH9 THR D 91 GLN D 102 1 12
HELIX 73 AI1 SER D 140 PHE D 156 1 17
HELIX 74 AI2 VAL D 183 CYS D 185 5 3
HELIX 75 AI3 HIS D 208 SER D 215 1 8
HELIX 76 AI4 ALA D 231 GLY D 240 1 10
HELIX 77 AI5 ARG D 245 ASN D 250 1 6
HELIX 78 AI6 ASP D 251 GLY D 256 1 6
HELIX 79 AI7 GLN D 257 ARG D 259 5 3
SHEET 1 AA1 3 LYS A 2 SER A 4 0
SHEET 2 AA1 3 TYR A 155 GLY A 160 -1 O ILE A 157 N PHE A 3
SHEET 3 AA1 3 GLU A 31 PRO A 37 -1 N GLU A 31 O GLY A 160
SHEET 1 AA2 5 THR A 73 CYS A 78 0
SHEET 2 AA2 5 ARG A 63 SER A 68 -1 N VAL A 67 O PHE A 74
SHEET 3 AA2 5 SER A 43 GLN A 55 -1 N LEU A 51 O GLN A 66
SHEET 4 AA2 5 LYS A 88 LEU A 98 -1 O PHE A 91 N VAL A 46
SHEET 5 AA2 5 PHE A 102 LYS A 103 -1 O PHE A 102 N LEU A 98
SHEET 1 AA3 5 THR A 73 CYS A 78 0
SHEET 2 AA3 5 ARG A 63 SER A 68 -1 N VAL A 67 O PHE A 74
SHEET 3 AA3 5 SER A 43 GLN A 55 -1 N LEU A 51 O GLN A 66
SHEET 4 AA3 5 LYS A 88 LEU A 98 -1 O PHE A 91 N VAL A 46
SHEET 5 AA3 5 GLY A 116 LEU A 118 -1 O MET A 117 N ALA A 92
SHEET 1 AA4 2 ALA A 107 LEU A 109 0
SHEET 2 AA4 2 VAL A 112 SER A 114 -1 O SER A 114 N ALA A 107
SHEET 1 AA5 5 VAL A 204 LEU A 206 0
SHEET 2 AA5 5 VAL A 275 MET A 279 1 O VAL A 277 N GLU A 205
SHEET 3 AA5 5 LEU A 301 ALA A 304 -1 O ALA A 304 N ARG A 276
SHEET 4 AA5 5 ALA A 309 ILE A 312 -1 O LEU A 310 N ILE A 303
SHEET 5 AA5 5 MET A 316 GLY A 317 -1 O MET A 316 N ILE A 312
SHEET 1 AA6 4 HIS A 264 ASP A 267 0
SHEET 2 AA6 4 LEU A 330 PHE A 336 -1 O GLU A 333 N HIS A 264
SHEET 3 AA6 4 ARG A 214 ARG A 221 -1 N ILE A 220 O LEU A 330
SHEET 4 AA6 4 GLU A 386 VAL A 394 -1 O VAL A 391 N GLY A 217
SHEET 1 AA7 2 LYS A 285 VAL A 287 0
SHEET 2 AA7 2 GLU A 293 THR A 295 -1 O ILE A 294 N LEU A 286
SHEET 1 AA8 3 ILE A 405 ARG A 408 0
SHEET 2 AA8 3 GLN A 443 GLY A 447 -1 O VAL A 446 N ILE A 405
SHEET 3 AA8 3 THR A 435 ALA A 438 -1 N VAL A 437 O SER A 445
SHEET 1 AA9 2 GLN A 480 ARG A 482 0
SHEET 2 AA9 2 GLN B 480 ARG B 482 -1 O ALA B 481 N ALA A 481
SHEET 1 AB1 7 GLN A 508 GLU A 509 0
SHEET 2 AB1 7 VAL A 567 VAL A 577 1 O ARG A 568 N GLN A 508
SHEET 3 AB1 7 LYS A 584 CYS A 594 -1 O ALA A 590 N GLU A 571
SHEET 4 AB1 7 VAL A 676 LEU A 682 -1 O LEU A 681 N LEU A 589
SHEET 5 AB1 7 ARG A 654 LEU A 662 -1 N LEU A 662 O VAL A 676
SHEET 6 AB1 7 LEU A 641 ARG A 651 -1 N ALA A 647 O LEU A 659
SHEET 7 AB1 7 PHE A 631 PRO A 635 -1 N VAL A 634 O ARG A 648
SHEET 1 AB2 3 PHE A 515 ILE A 516 0
SHEET 2 AB2 3 ALA A 543 MET A 544 -1 O ALA A 543 N ILE A 516
SHEET 3 AB2 3 LEU A 531 THR A 532 -1 N LEU A 531 O MET A 544
SHEET 1 AB3 4 LEU A 732 TYR A 741 0
SHEET 2 AB3 4 ARG A 750 TRP A 759 -1 O GLY A 756 N ARG A 736
SHEET 3 AB3 4 VAL A 703 ASP A 712 -1 N ARG A 705 O LEU A 757
SHEET 4 AB3 4 THR A 789 LEU A 790 -1 O THR A 789 N LEU A 710
SHEET 1 AB4 3 LYS B 2 SER B 4 0
SHEET 2 AB4 3 TYR B 155 GLY B 160 -1 O ILE B 157 N PHE B 3
SHEET 3 AB4 3 GLU B 31 PRO B 37 -1 N GLU B 31 O GLY B 160
SHEET 1 AB5 5 THR B 73 CYS B 78 0
SHEET 2 AB5 5 ARG B 63 SER B 68 -1 N VAL B 67 O PHE B 74
SHEET 3 AB5 5 SER B 43 GLN B 55 -1 N LEU B 51 O GLN B 66
SHEET 4 AB5 5 LYS B 88 LEU B 98 -1 O PHE B 91 N VAL B 46
SHEET 5 AB5 5 PHE B 102 LYS B 103 -1 O PHE B 102 N LEU B 98
SHEET 1 AB6 5 THR B 73 CYS B 78 0
SHEET 2 AB6 5 ARG B 63 SER B 68 -1 N VAL B 67 O PHE B 74
SHEET 3 AB6 5 SER B 43 GLN B 55 -1 N LEU B 51 O GLN B 66
SHEET 4 AB6 5 LYS B 88 LEU B 98 -1 O PHE B 91 N VAL B 46
SHEET 5 AB6 5 GLY B 116 LEU B 118 -1 O MET B 117 N ALA B 92
SHEET 1 AB7 2 ALA B 107 LEU B 109 0
SHEET 2 AB7 2 VAL B 112 SER B 114 -1 O SER B 114 N ALA B 107
SHEET 1 AB8 5 VAL B 204 LEU B 206 0
SHEET 2 AB8 5 VAL B 275 MET B 279 1 O VAL B 277 N GLU B 205
SHEET 3 AB8 5 LEU B 301 ALA B 304 -1 O VAL B 302 N ARG B 278
SHEET 4 AB8 5 ALA B 309 ILE B 312 -1 O LEU B 310 N ILE B 303
SHEET 5 AB8 5 MET B 316 GLY B 317 -1 O MET B 316 N ILE B 312
SHEET 1 AB9 4 HIS B 264 ASP B 267 0
SHEET 2 AB9 4 LEU B 330 PHE B 336 -1 O GLU B 333 N HIS B 264
SHEET 3 AB9 4 ARG B 214 ARG B 221 -1 N ILE B 220 O LEU B 330
SHEET 4 AB9 4 GLU B 386 VAL B 394 -1 O VAL B 391 N GLY B 217
SHEET 1 AC1 2 LYS B 285 VAL B 287 0
SHEET 2 AC1 2 GLU B 293 THR B 295 -1 O ILE B 294 N LEU B 286
SHEET 1 AC2 3 ILE B 405 ARG B 408 0
SHEET 2 AC2 3 GLN B 443 GLY B 447 -1 O VAL B 446 N ILE B 405
SHEET 3 AC2 3 THR B 435 ALA B 438 -1 N VAL B 437 O SER B 445
SHEET 1 AC3 7 GLN B 508 GLU B 509 0
SHEET 2 AC3 7 VAL B 567 VAL B 577 1 O ARG B 568 N GLN B 508
SHEET 3 AC3 7 LYS B 584 CYS B 594 -1 O ALA B 590 N GLU B 571
SHEET 4 AC3 7 VAL B 676 LEU B 682 -1 O LEU B 681 N LEU B 589
SHEET 5 AC3 7 ARG B 654 LEU B 662 -1 N LEU B 662 O VAL B 676
SHEET 6 AC3 7 LEU B 641 ARG B 651 -1 N ALA B 647 O LEU B 659
SHEET 7 AC3 7 PHE B 631 PRO B 635 -1 N VAL B 634 O ARG B 648
SHEET 1 AC4 3 PHE B 515 ILE B 516 0
SHEET 2 AC4 3 ALA B 543 MET B 544 -1 O ALA B 543 N ILE B 516
SHEET 3 AC4 3 LEU B 531 THR B 532 -1 N LEU B 531 O MET B 544
SHEET 1 AC5 4 LEU B 732 TYR B 741 0
SHEET 2 AC5 4 ARG B 750 TRP B 759 -1 O GLY B 756 N ARG B 736
SHEET 3 AC5 4 VAL B 703 ASP B 712 -1 N ARG B 705 O LEU B 757
SHEET 4 AC5 4 THR B 789 LEU B 790 -1 O THR B 789 N LEU B 710
SHEET 1 AC6 7 GLU C 47 VAL C 48 0
SHEET 2 AC6 7 ILE C 106 TYR C 115 1 O ARG C 107 N GLU C 47
SHEET 3 AC6 7 MET C 126 ASP C 136 -1 O GLU C 131 N CYS C 110
SHEET 4 AC6 7 GLN C 223 GLY C 230 -1 O PHE C 227 N GLY C 132
SHEET 5 AC6 7 LEU C 199 VAL C 207 -1 N GLY C 203 O GLY C 228
SHEET 6 AC6 7 THR C 172 ILE C 180 -1 N VAL C 178 O MET C 202
SHEET 7 AC6 7 VAL C 162 PHE C 169 -1 N ARG C 165 O GLU C 177
SHEET 1 AC7 2 VAL C 54 ASP C 56 0
SHEET 2 AC7 2 MET C 85 LEU C 87 -1 O LEU C 86 N GLU C 55
SHEET 1 AC8 7 GLU D 47 VAL D 48 0
SHEET 2 AC8 7 ILE D 106 TYR D 115 1 O ARG D 107 N GLU D 47
SHEET 3 AC8 7 MET D 126 ASP D 136 -1 O GLU D 131 N CYS D 110
SHEET 4 AC8 7 GLN D 223 GLY D 230 -1 O PHE D 227 N GLY D 132
SHEET 5 AC8 7 TRP D 198 VAL D 207 -1 N GLY D 203 O GLY D 228
SHEET 6 AC8 7 THR D 172 GLN D 181 -1 N VAL D 178 O MET D 202
SHEET 7 AC8 7 VAL D 162 PHE D 169 -1 N ARG D 163 O ASP D 179
SHEET 1 AC9 2 VAL D 54 ASP D 56 0
SHEET 2 AC9 2 MET D 85 LEU D 87 -1 O LEU D 86 N GLU D 55
CISPEP 1 PRO C 104 PRO C 105 0 2.95
CISPEP 2 GLU C 173 PRO C 174 0 -7.35
CISPEP 3 PRO D 104 PRO D 105 0 3.54
CISPEP 4 GLU D 173 PRO D 174 0 -4.56
SITE 1 AC1 11 LEU C 64 SER C 92 GLN C 95 GLU C 131
SITE 2 AC1 11 PHE C 169 PHE C 171 THR C 172 GLY C 203
SITE 3 AC1 11 CYS C 204 ALA C 226 GLY C 228
SITE 1 AC2 12 LEU D 64 GLN D 95 MET D 99 GLN D 129
SITE 2 AC2 12 GLU D 131 PHE D 171 THR D 172 GLY D 203
SITE 3 AC2 12 CYS D 204 ALA D 226 GLY D 228 MET D 229
CRYST1 113.300 218.830 107.630 90.00 101.94 90.00 C 1 2 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 0.008826 0.000000 0.001866 0.00000
SCALE2 0.000000 0.004570 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009497 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
