HEADER FLAVOPROTEIN, FLUORESCENT PROTEIN 09-DEC-13 4NXF
TITLE CRYSTAL STRUCTURE OF ILOV-I486(2LT) AT PH 8.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOTROPIN-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LOV DOMAIN, UNP RESIDUES 388-496;
COMPND 5 SYNONYM: DEFECTIVE IN CHLOROPLAST AVOIDANCE PROTEIN 1, NON-
COMPND 6 PHOTOTROPIC HYPOCOTYL 1-LIKE PROTEIN 1, ATKIN7, NPH1-LIKE PROTEIN 1;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS, THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: PHOT2, CAV1, KIN7, NPL1, AT5G58140, K21L19.6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS FLAVOPROTEIN, FMN BINDING, FLUORESCENT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG,X.LIU,J.LI
REVDAT 3 08-NOV-23 4NXF 1 REMARK
REVDAT 2 24-AUG-22 4NXF 1 JRNL REMARK SEQADV LINK
REVDAT 1 24-SEP-14 4NXF 0
JRNL AUTH X.LIU,L.JIANG,J.LI,L.WANG,Y.YU,Q.ZHOU,X.LV,W.GONG,Y.LU,
JRNL AUTH 2 J.WANG
JRNL TITL SIGNIFICANT EXPANSION OF FLUORESCENT PROTEIN SENSING ABILITY
JRNL TITL 2 THROUGH THE GENETIC INCORPORATION OF SUPERIOR PHOTO-INDUCED
JRNL TITL 3 ELECTRON-TRANSFER QUENCHERS.
JRNL REF J.AM.CHEM.SOC. V. 136 13094 2014
JRNL REFN ESSN 1520-5126
JRNL PMID 25197956
JRNL DOI 10.1021/JA505219R
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 20782
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) : 0.196
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1053
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 24.2053 - 3.5285 0.72 1941 119 0.2095 0.2219
REMARK 3 2 3.5285 - 2.8020 0.89 2379 131 0.2089 0.2199
REMARK 3 3 2.8020 - 2.4482 0.97 2595 149 0.1945 0.2317
REMARK 3 4 2.4482 - 2.2245 0.98 2630 140 0.1841 0.2385
REMARK 3 5 2.2245 - 2.0652 0.99 2640 127 0.1783 0.2013
REMARK 3 6 2.0652 - 1.9435 0.99 2661 143 0.1793 0.2337
REMARK 3 7 1.9435 - 1.8462 0.99 2643 116 0.1832 0.2522
REMARK 3 8 1.8462 - 1.7659 0.84 2240 128 0.2026 0.2320
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.18
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 1832
REMARK 3 ANGLE : 1.238 2489
REMARK 3 CHIRALITY : 0.086 260
REMARK 3 PLANARITY : 0.006 319
REMARK 3 DIHEDRAL : 18.662 695
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): -3.5914 -2.4953 60.3517
REMARK 3 T TENSOR
REMARK 3 T11: 0.1315 T22: 0.1200
REMARK 3 T33: 0.1587 T12: 0.0021
REMARK 3 T13: 0.0115 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.6643 L22: 0.6375
REMARK 3 L33: 1.7441 L12: 0.0120
REMARK 3 L13: 0.4849 L23: -0.1731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0068 S13: -0.0411
REMARK 3 S21: -0.0075 S22: -0.0192 S23: 0.0145
REMARK 3 S31: 0.0202 S32: 0.0409 S33: 0.0077
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 4NXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21167
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.766
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
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) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
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: MLPHARE
REMARK 200 STARTING MODEL: 4EES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SAMPLE (20-30 MG/ML) IN 20MM
REMARK 280 TRIS, PH 8.0, 50MM NACL, EQUAL VOLUME OF RESERVOIR SOLUTION
REMARK 280 (0.2M AMMONIUM ACETATE, 0.1M TRIS PH 8.0, 16% W/V POLYETHYLENE
REMARK 280 GLYCOL 10000), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.0 K
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 32.44850
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 387
REMARK 465 GLU A 388
REMARK 465 HIS A 495
REMARK 465 VAL A 496
REMARK 465 LEU A 497
REMARK 465 GLU A 498
REMARK 465 HIS A 499
REMARK 465 HIS A 500
REMARK 465 HIS A 501
REMARK 465 HIS A 502
REMARK 465 HIS A 503
REMARK 465 HIS A 504
REMARK 465 MET B 387
REMARK 465 GLU B 388
REMARK 465 SER B 493
REMARK 465 ASP B 494
REMARK 465 HIS B 495
REMARK 465 VAL B 496
REMARK 465 LEU B 497
REMARK 465 GLU B 498
REMARK 465 HIS B 499
REMARK 465 HIS B 500
REMARK 465 HIS B 501
REMARK 465 HIS B 502
REMARK 465 HIS B 503
REMARK 465 HIS B 504
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NXB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT THE SAME PROTEIN AT DIFFERENT PH
REMARK 900 RELATED ID: 4NXE RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT THE SAME PROTEIN AT DIFFERENT PH
REMARK 900 RELATED ID: 4NXG RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT THE SAME PROTEIN AT DIFFERENT PH
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES C426A IS MUTAGENESIS ACCORDING TO DATABASE P93025.
DBREF 4NXF A 388 496 UNP P93025 PHOT2_ARATH 388 496
DBREF 4NXF B 388 496 UNP P93025 PHOT2_ARATH 388 496
SEQADV 4NXF MET A 387 UNP P93025 EXPRESSION TAG
SEQADV 4NXF THR A 394 UNP P93025 SER 394 ENGINEERED MUTATION
SEQADV 4NXF GLY A 409 UNP P93025 SER 409 ENGINEERED MUTATION
SEQADV 4NXF ALA A 426 UNP P93025 CYS 426 SEE REMARK 999
SEQADV 4NXF THR A 452 UNP P93025 ILE 452 ENGINEERED MUTATION
SEQADV 4NXF LEU A 470 UNP P93025 PHE 470 ENGINEERED MUTATION
SEQADV 4NXF VAL A 475 UNP P93025 MET 475 ENGINEERED MUTATION
SEQADV 4NXF 2LT A 486 UNP P93025 ILE 486 ENGINEERED MUTATION
SEQADV 4NXF LEU A 497 UNP P93025 EXPRESSION TAG
SEQADV 4NXF GLU A 498 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS A 499 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS A 500 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS A 501 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS A 502 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS A 503 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS A 504 UNP P93025 EXPRESSION TAG
SEQADV 4NXF MET B 387 UNP P93025 EXPRESSION TAG
SEQADV 4NXF THR B 394 UNP P93025 SER 394 ENGINEERED MUTATION
SEQADV 4NXF GLY B 409 UNP P93025 SER 409 ENGINEERED MUTATION
SEQADV 4NXF ALA B 426 UNP P93025 CYS 426 SEE REMARK 999
SEQADV 4NXF THR B 452 UNP P93025 ILE 452 ENGINEERED MUTATION
SEQADV 4NXF LEU B 470 UNP P93025 PHE 470 ENGINEERED MUTATION
SEQADV 4NXF VAL B 475 UNP P93025 MET 475 ENGINEERED MUTATION
SEQADV 4NXF 2LT B 486 UNP P93025 ILE 486 ENGINEERED MUTATION
SEQADV 4NXF LEU B 497 UNP P93025 EXPRESSION TAG
SEQADV 4NXF GLU B 498 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS B 499 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS B 500 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS B 501 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS B 502 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS B 503 UNP P93025 EXPRESSION TAG
SEQADV 4NXF HIS B 504 UNP P93025 EXPRESSION TAG
SEQRES 1 A 118 MET GLU LYS ASN PHE VAL ILE THR ASP PRO ARG LEU PRO
SEQRES 2 A 118 ASP ASN PRO ILE ILE PHE ALA SER ASP GLY PHE LEU GLU
SEQRES 3 A 118 LEU THR GLU TYR SER ARG GLU GLU ILE LEU GLY ARG ASN
SEQRES 4 A 118 ALA ARG PHE LEU GLN GLY PRO GLU THR ASP GLN ALA THR
SEQRES 5 A 118 VAL GLN LYS ILE ARG ASP ALA ILE ARG ASP GLN ARG GLU
SEQRES 6 A 118 THR THR VAL GLN LEU ILE ASN TYR THR LYS SER GLY LYS
SEQRES 7 A 118 LYS PHE TRP ASN LEU LEU HIS LEU GLN PRO VAL ARG ASP
SEQRES 8 A 118 GLN LYS GLY GLU LEU GLN TYR PHE 2LT GLY VAL GLN LEU
SEQRES 9 A 118 ASP GLY SER ASP HIS VAL LEU GLU HIS HIS HIS HIS HIS
SEQRES 10 A 118 HIS
SEQRES 1 B 118 MET GLU LYS ASN PHE VAL ILE THR ASP PRO ARG LEU PRO
SEQRES 2 B 118 ASP ASN PRO ILE ILE PHE ALA SER ASP GLY PHE LEU GLU
SEQRES 3 B 118 LEU THR GLU TYR SER ARG GLU GLU ILE LEU GLY ARG ASN
SEQRES 4 B 118 ALA ARG PHE LEU GLN GLY PRO GLU THR ASP GLN ALA THR
SEQRES 5 B 118 VAL GLN LYS ILE ARG ASP ALA ILE ARG ASP GLN ARG GLU
SEQRES 6 B 118 THR THR VAL GLN LEU ILE ASN TYR THR LYS SER GLY LYS
SEQRES 7 B 118 LYS PHE TRP ASN LEU LEU HIS LEU GLN PRO VAL ARG ASP
SEQRES 8 B 118 GLN LYS GLY GLU LEU GLN TYR PHE 2LT GLY VAL GLN LEU
SEQRES 9 B 118 ASP GLY SER ASP HIS VAL LEU GLU HIS HIS HIS HIS HIS
SEQRES 10 B 118 HIS
MODRES 4NXF 2LT A 486 TYR 3,5-DICHLORO-L-TYROSINE
MODRES 4NXF 2LT B 486 TYR 3,5-DICHLORO-L-TYROSINE
HET 2LT A 486 14
HET 2LT B 486 14
HET FMN A1001 31
HET FMN B1001 31
HETNAM 2LT 3,5-DICHLORO-L-TYROSINE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 1 2LT 2(C9 H9 CL2 N O3)
FORMUL 3 FMN 2(C17 H21 N4 O9 P)
FORMUL 5 HOH *108(H2 O)
HELIX 1 1 SER A 407 GLU A 415 1 9
HELIX 2 2 SER A 417 LEU A 422 1 6
HELIX 3 3 ASN A 425 GLN A 430 5 6
HELIX 4 4 ASP A 435 GLN A 449 1 15
HELIX 5 5 SER B 407 GLU B 415 1 9
HELIX 6 6 SER B 417 LEU B 422 1 6
HELIX 7 7 ASN B 425 GLN B 430 5 6
HELIX 8 8 ASP B 435 GLN B 449 1 15
SHEET 1 A 5 ILE A 403 ALA A 406 0
SHEET 2 A 5 PHE A 391 THR A 394 -1 N ILE A 393 O ILE A 404
SHEET 3 A 5 LEU A 482 ASP A 491 -1 O PHE A 485 N THR A 394
SHEET 4 A 5 LYS A 465 ARG A 476 -1 N LEU A 469 O LEU A 490
SHEET 5 A 5 THR A 452 TYR A 459 -1 N LEU A 456 O ASN A 468
SHEET 1 B 5 ILE B 403 ALA B 406 0
SHEET 2 B 5 PHE B 391 THR B 394 -1 N ILE B 393 O ILE B 404
SHEET 3 B 5 LEU B 482 ASP B 491 -1 O PHE B 485 N THR B 394
SHEET 4 B 5 LYS B 465 ARG B 476 -1 N VAL B 475 O TYR B 484
SHEET 5 B 5 THR B 452 TYR B 459 -1 N LEU B 456 O ASN B 468
LINK C PHE A 485 N 2LT A 486 1555 1555 1.33
LINK C 2LT A 486 N GLY A 487 1555 1555 1.33
LINK C PHE B 485 N 2LT B 486 1555 1555 1.33
LINK C 2LT B 486 N GLY B 487 1555 1555 1.32
SITE 1 AC1 24 VAL A 392 THR A 394 ASN A 401 ASN A 425
SITE 2 AC1 24 ALA A 426 ARG A 427 LEU A 429 GLN A 430
SITE 3 AC1 24 ARG A 443 ILE A 446 LEU A 456 ASN A 458
SITE 4 AC1 24 ASN A 468 LEU A 470 LEU A 472 PHE A 485
SITE 5 AC1 24 2LT A 486 GLY A 487 GLN A 489 HOH A1103
SITE 6 AC1 24 HOH A1107 HOH A1128 HOH A1133 HOH A1136
SITE 1 AC2 24 VAL B 392 THR B 394 ASN B 401 ASN B 425
SITE 2 AC2 24 ALA B 426 ARG B 427 LEU B 429 GLN B 430
SITE 3 AC2 24 ILE B 442 ARG B 443 ILE B 446 LEU B 456
SITE 4 AC2 24 ASN B 458 ASN B 468 LEU B 470 LEU B 472
SITE 5 AC2 24 PHE B 485 2LT B 486 GLY B 487 GLN B 489
SITE 6 AC2 24 HOH B1106 HOH B1107 HOH B1139 HOH B1140
CRYST1 37.233 64.897 49.362 90.00 102.59 90.00 P 1 21 1 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 0.026858 0.000000 0.006000 0.00000
SCALE2 0.000000 0.015409 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020758 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
