HEADER LIGASE 14-AUG-11 3TEG
TITLE BACTERIAL AND EUKARYOTIC PHENYLALANYL-TRNA SYNTHETASES CATALYZE
TITLE 2 MISAMINOACYLATION OF TRNAPHE WITH 3,4-DIHYDROXY-L-PHENYLALANINE (L-
TITLE 3 DOPA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLALANYL-TRNA SYNTHETASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHENYLALANINE--TRNA LIGASE, PHERS;
COMPND 5 EC: 6.1.1.20;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FARS1, FARS2, HSPC320;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DOPA, L-DOPA, TRNA, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MOOR,L.KLIPCAN,M.SAFRO
REVDAT 2 13-SEP-23 3TEG 1 REMARK SEQADV
REVDAT 1 23-NOV-11 3TEG 0
JRNL AUTH N.MOOR,L.KLIPCAN,M.G.SAFRO
JRNL TITL BACTERIAL AND EUKARYOTIC PHENYLALANYL-TRNA SYNTHETASES
JRNL TITL 2 CATALYZE MISAMINOACYLATION OF TRNA(PHE) WITH
JRNL TITL 3 3,4-DIHYDROXY-L-PHENYLALANINE.
JRNL REF CHEM.BIOL. V. 18 1221 2011
JRNL REFN ISSN 1074-5521
JRNL PMID 22035791
JRNL DOI 10.1016/J.CHEMBIOL.2011.08.008
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 24066
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1236
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 47.8641 - 4.5842 0.93 2610 136 0.1799 0.2013
REMARK 3 2 4.5842 - 3.6390 0.95 2520 151 0.1288 0.1917
REMARK 3 3 3.6390 - 3.1791 0.97 2573 115 0.1410 0.1761
REMARK 3 4 3.1791 - 2.8885 0.97 2551 132 0.1704 0.2239
REMARK 3 5 2.8885 - 2.6815 0.97 2540 140 0.1775 0.2771
REMARK 3 6 2.6815 - 2.5234 0.98 2523 142 0.1940 0.2819
REMARK 3 7 2.5234 - 2.3970 0.98 2563 129 0.2005 0.2552
REMARK 3 8 2.3970 - 2.2927 0.98 2524 146 0.2046 0.2563
REMARK 3 9 2.2927 - 2.2044 0.95 2426 145 0.2248 0.2886
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 : 0.37
REMARK 3 B_SOL : 68.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.080
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) : 1.65290
REMARK 3 B22 (A**2) : -0.24180
REMARK 3 B33 (A**2) : -1.41110
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 : 0.007 3471
REMARK 3 ANGLE : 0.977 4705
REMARK 3 CHIRALITY : 0.069 493
REMARK 3 PLANARITY : 0.004 605
REMARK 3 DIHEDRAL : 17.790 1261
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5930 25.5924 13.6206
REMARK 3 T TENSOR
REMARK 3 T11: 0.1422 T22: 0.1653
REMARK 3 T33: 0.1215 T12: 0.0127
REMARK 3 T13: 0.0223 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.4984 L22: 1.6483
REMARK 3 L33: 0.5702 L12: -0.0827
REMARK 3 L13: -0.0906 L23: 0.1619
REMARK 3 S TENSOR
REMARK 3 S11: 0.0433 S12: -0.0239 S13: 0.0423
REMARK 3 S21: -0.0093 S22: -0.0666 S23: 0.0736
REMARK 3 S31: -0.0412 S32: -0.0012 S33: 0.0001
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 3TEG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067380.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : ALUMINIUM OR CARBON FOILS
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 : 24066
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 47.853
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
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: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 3CMQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 MM DTT, 100 MM BIS-TRIS PROPANE,1.8
REMARK 280 M NA-ACETATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.59250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.03800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.29350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.03800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.59250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.29350
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ALA A 2
REMARK 465 ALA A 3
REMARK 465 GLU A 4
REMARK 465 CYS A 5
REMARK 465 ALA A 6
REMARK 465 THR A 7
REMARK 465 GLN A 8
REMARK 465 ARG A 9
REMARK 465 ALA A 10
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 ND1 HIS A 60 O HOH A 417 2.16
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 13 -2.28 -143.35
REMARK 500 ASN A 29 22.77 -155.59
REMARK 500 HIS A 47 -1.77 77.14
REMARK 500 PHE A 90 -65.03 -123.05
REMARK 500 ASN A 111 -166.13 -168.62
REMARK 500 ASP A 175 30.36 -91.78
REMARK 500 GLU A 183 -169.86 -161.95
REMARK 500 SER A 185 -147.76 -112.94
REMARK 500 HIS A 236 125.03 -176.77
REMARK 500 ALA A 268 53.06 -106.17
REMARK 500 CYS A 308 80.81 -69.08
REMARK 500 LEU A 335 154.07 -48.90
REMARK 500 SER A 337 86.02 -65.63
REMARK 500 GLU A 338 40.13 77.97
REMARK 500 TYR A 340 133.87 171.76
REMARK 500 HIS A 372 -2.75 79.81
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 DAH A 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CMQ RELATED DB: PDB
REMARK 900 RELATED ID: 3HFV RELATED DB: PDB
REMARK 900 RELATED ID: 3TEH RELATED DB: PDB
DBREF 3TEG A 2 415 UNP O95363 SYFM_HUMAN 38 451
SEQADV 3TEG MET A 1 UNP O95363 EXPRESSION TAG
SEQRES 1 A 415 MET ALA ALA GLU CYS ALA THR GLN ARG ALA PRO GLY SER
SEQRES 2 A 415 VAL VAL GLU LEU LEU GLY LYS SER TYR PRO GLN ASP ASP
SEQRES 3 A 415 HIS SER ASN LEU THR ARG LYS VAL LEU THR ARG VAL GLY
SEQRES 4 A 415 ARG ASN LEU HIS ASN GLN GLN HIS HIS PRO LEU TRP LEU
SEQRES 5 A 415 ILE LYS GLU ARG VAL LYS GLU HIS PHE TYR LYS GLN TYR
SEQRES 6 A 415 VAL GLY ARG PHE GLY THR PRO LEU PHE SER VAL TYR ASP
SEQRES 7 A 415 ASN LEU SER PRO VAL VAL THR THR TRP GLN ASN PHE ASP
SEQRES 8 A 415 SER LEU LEU ILE PRO ALA ASP HIS PRO SER ARG LYS LYS
SEQRES 9 A 415 GLY ASP ASN TYR TYR LEU ASN ARG THR HIS MET LEU ARG
SEQRES 10 A 415 ALA HIS THR SER ALA HIS GLN TRP ASP LEU LEU HIS ALA
SEQRES 11 A 415 GLY LEU ASP ALA PHE LEU VAL VAL GLY ASP VAL TYR ARG
SEQRES 12 A 415 ARG ASP GLN ILE ASP SER GLN HIS TYR PRO ILE PHE HIS
SEQRES 13 A 415 GLN LEU GLU ALA VAL ARG LEU PHE SER LYS HIS GLU LEU
SEQRES 14 A 415 PHE ALA GLY ILE LYS ASP GLY GLU SER LEU GLN LEU PHE
SEQRES 15 A 415 GLU GLN SER SER ARG SER ALA HIS LYS GLN GLU THR HIS
SEQRES 16 A 415 THR MET GLU ALA VAL LYS LEU VAL GLU PHE ASP LEU LYS
SEQRES 17 A 415 GLN THR LEU THR ARG LEU MET ALA HIS LEU PHE GLY ASP
SEQRES 18 A 415 GLU LEU GLU ILE ARG TRP VAL ASP CYS TYR PHE PRO PHE
SEQRES 19 A 415 THR HIS PRO SER PHE GLU MET GLU ILE ASN PHE HIS GLY
SEQRES 20 A 415 GLU TRP LEU GLU VAL LEU GLY CYS GLY VAL MET GLU GLN
SEQRES 21 A 415 GLN LEU VAL ASN SER ALA GLY ALA GLN ASP ARG ILE GLY
SEQRES 22 A 415 TRP ALA PHE GLY LEU GLY LEU GLU ARG LEU ALA MET ILE
SEQRES 23 A 415 LEU TYR ASP ILE PRO ASP ILE ARG LEU PHE TRP CYS GLU
SEQRES 24 A 415 ASP GLU ARG PHE LEU LYS GLN PHE CYS VAL SER ASN ILE
SEQRES 25 A 415 ASN GLN LYS VAL LYS PHE GLN PRO LEU SER LYS TYR PRO
SEQRES 26 A 415 ALA VAL ILE ASN ASP ILE SER PHE TRP LEU PRO SER GLU
SEQRES 27 A 415 ASN TYR ALA GLU ASN ASP PHE TYR ASP LEU VAL ARG THR
SEQRES 28 A 415 ILE GLY GLY ASP LEU VAL GLU LYS VAL ASP LEU ILE ASP
SEQRES 29 A 415 LYS PHE VAL HIS PRO LYS THR HIS LYS THR SER HIS CYS
SEQRES 30 A 415 TYR ARG ILE THR TYR ARG HIS MET GLU ARG THR LEU SER
SEQRES 31 A 415 GLN ARG GLU VAL ARG HIS ILE HIS GLN ALA LEU GLN GLU
SEQRES 32 A 415 ALA ALA VAL GLN LEU LEU GLY VAL GLU GLY ARG PHE
HET DAH A 416 25
HETNAM DAH 3,4-DIHYDROXYPHENYLALANINE
HETSYN DAH L-DOPA
FORMUL 2 DAH C9 H11 N O4
FORMUL 3 HOH *311(H2 O)
HELIX 1 1 THR A 31 THR A 36 1 6
HELIX 2 2 ASN A 41 GLN A 45 5 5
HELIX 3 3 HIS A 48 ARG A 68 1 21
HELIX 4 4 THR A 86 PHE A 90 1 5
HELIX 5 5 ASP A 91 LEU A 94 5 4
HELIX 6 6 HIS A 99 ASN A 107 5 9
HELIX 7 7 HIS A 119 ALA A 122 5 4
HELIX 8 8 HIS A 123 ALA A 130 1 8
HELIX 9 9 SER A 165 PHE A 170 1 6
HELIX 10 10 ASP A 175 LEU A 179 5 5
HELIX 11 11 THR A 196 GLY A 220 1 25
HELIX 12 12 GLU A 259 ALA A 266 1 8
HELIX 13 13 LEU A 280 ASP A 289 1 10
HELIX 14 14 ASP A 292 TRP A 297 5 6
HELIX 15 15 ASP A 300 LYS A 305 1 6
HELIX 16 16 GLN A 306 CYS A 308 5 3
HELIX 17 17 ALA A 341 GLY A 354 1 14
HELIX 18 18 SER A 390 GLY A 410 1 21
SHEET 1 A 2 VAL A 14 LEU A 17 0
SHEET 2 A 2 LYS A 20 PRO A 23 -1 O LYS A 20 N LEU A 17
SHEET 1 B 7 SER A 75 TYR A 77 0
SHEET 2 B 7 ALA A 134 TYR A 142 1 O VAL A 138 N TYR A 77
SHEET 3 B 7 ILE A 154 PHE A 164 -1 O GLU A 159 N VAL A 137
SHEET 4 B 7 ILE A 272 GLY A 279 -1 O ILE A 272 N PHE A 164
SHEET 5 B 7 GLU A 248 MET A 258 -1 N GLY A 254 O GLY A 277
SHEET 6 B 7 THR A 235 PHE A 245 -1 N PHE A 245 O GLU A 248
SHEET 7 B 7 ILE A 225 PHE A 232 -1 N VAL A 228 O GLU A 240
SHEET 1 C 2 VAL A 83 THR A 85 0
SHEET 2 C 2 HIS A 114 LEU A 116 -1 O MET A 115 N VAL A 84
SHEET 1 D 4 VAL A 357 VAL A 367 0
SHEET 2 D 4 THR A 374 TYR A 382 -1 O ARG A 379 N ASP A 361
SHEET 3 D 4 VAL A 327 TRP A 334 -1 N VAL A 327 O TYR A 382
SHEET 4 D 4 GLU A 412 GLY A 413 -1 O GLU A 412 N TRP A 334
CISPEP 1 HIS A 236 PRO A 237 0 -1.08
SITE 1 AC1 16 HIS A 119 SER A 121 GLN A 124 ARG A 143
SITE 2 AC1 16 GLN A 157 GLU A 159 PHE A 232 PHE A 234
SITE 3 AC1 16 THR A 235 GLY A 254 CYS A 255 GLY A 256
SITE 4 AC1 16 ALA A 275 PHE A 276 GLY A 277 HOH A 500
CRYST1 55.185 90.587 96.076 90.00 90.00 90.00 P 21 21 21 4
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 0.018121 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011039 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010408 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
