HEADER TRANSFERASE 20-APR-10 3MMP
TITLE STRUCTURE OF THE QB REPLICASE, AN RNA-DEPENDENT RNA POLYMERASE
TITLE 2 CONSISTING OF VIRAL AND HOST PROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TU 2, ELONGATION FACTOR TS;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: EF-TU 2, P-43, EF-TS;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RNA-DIRECTED RNA POLYMERASE BETA CHAIN;
COMPND 8 CHAIN: G, F;
COMPND 9 SYNONYM: RNA REPLICASE BETA CHAIN;
COMPND 10 EC: 2.7.7.48;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: TUFB, B3980, JW3943, TSF, B0170, JW0165;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAD33;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE QBETA;
SOURCE 13 ORGANISM_COMMON: BACTERIOPHAGE Q-BETA;
SOURCE 14 ORGANISM_TAXID: 39803;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PBAD33
KEYWDS RDRP,HOST-FACTOR COMPLEX, TRANSLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.KIDMOSE,N.N.VASILIEV,A.B.CHETVERIN,C.R.KNUDSEN,G.R.ANDERSEN
REVDAT 3 30-JUN-10 3MMP 1 JRNL
REVDAT 2 23-JUN-10 3MMP 1 JRNL
REVDAT 1 09-JUN-10 3MMP 0
JRNL AUTH R.T.KIDMOSE,N.N.VASILIEV,A.B.CHETVERIN,G.R.ANDERSEN,
JRNL AUTH 2 C.R.KNUDSEN
JRNL TITL STRUCTURE OF THE QBETA REPLICASE, AN RNA-DEPENDENT RNA
JRNL TITL 2 POLYMERASE CONSISTING OF VIRAL AND HOST PROTEINS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 10884 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20534494
JRNL DOI 10.1073/PNAS.1003015107
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 122547
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.630
REMARK 3 FREE R VALUE TEST SET COUNT : 1993
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 47.2917 - 6.0215 0.99 8684 151 0.1717 0.1819
REMARK 3 2 6.0215 - 4.7809 1.00 8677 147 0.1754 0.2049
REMARK 3 3 4.7809 - 4.1770 1.00 8632 148 0.1663 0.1780
REMARK 3 4 4.1770 - 3.7953 1.00 8641 128 0.1888 0.2049
REMARK 3 5 3.7953 - 3.5233 1.00 8591 135 0.2022 0.2335
REMARK 3 6 3.5233 - 3.3157 1.00 8630 142 0.2147 0.2300
REMARK 3 7 3.3157 - 3.1497 1.00 8611 149 0.2337 0.2198
REMARK 3 8 3.1497 - 3.0126 1.00 8592 136 0.2355 0.2752
REMARK 3 9 3.0126 - 2.8966 1.00 8598 140 0.2487 0.2757
REMARK 3 10 2.8966 - 2.7967 1.00 8588 139 0.2515 0.2946
REMARK 3 11 2.7967 - 2.7092 1.00 8639 143 0.2594 0.3210
REMARK 3 12 2.7092 - 2.6318 1.00 8540 149 0.2557 0.2976
REMARK 3 13 2.6318 - 2.5625 1.00 8601 145 0.2661 0.2943
REMARK 3 14 2.5625 - 2.5000 1.00 8530 141 0.2729 0.3353
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 : 0.33
REMARK 3 B_SOL : 46.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.950
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) : 11.95000
REMARK 3 B22 (A**2) : -5.98520
REMARK 3 B33 (A**2) : -5.96480
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.22040
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 : 0.008 18828
REMARK 3 ANGLE : 1.053 25452
REMARK 3 CHIRALITY : 0.075 2888
REMARK 3 PLANARITY : 0.004 3298
REMARK 3 DIHEDRAL : 16.709 6978
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN G AND (RESSEQ 7:113 OR RESSEQ 119:
REMARK 3 519 OR RESSEQ 533:573 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 7:113 OR RESSEQ 119:
REMARK 3 519 OR RESSEQ 533:573 )
REMARK 3 ATOM PAIRS NUMBER : 4318
REMARK 3 RMSD : 0.040
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1009:1041 OR RESSEQ
REMARK 3 1064:1392 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 1009:1041 OR RESSEQ
REMARK 3 1064:1392 )
REMARK 3 ATOM PAIRS NUMBER : 2790
REMARK 3 RMSD : 0.054
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 3:282 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 3:282 )
REMARK 3 ATOM PAIRS NUMBER : 2108
REMARK 3 RMSD : 0.023
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MMP COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058737.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122568
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.60900
REMARK 200 R SYM FOR SHELL (I) : 0.57100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.870
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: PDB ENTRY 1EFU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KCL, 0.05M HEPES PH 7.5, 27%-30%
REMARK 280 V/V PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH), VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
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 127.35500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 127.35500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 69.70000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 5840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 100910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, C, F
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 0
REMARK 465 ALA A 1
REMARK 465 GLU A 2
REMARK 465 HIS A 999
REMARK 465 MET A 1000
REMARK 465 SER A 1001
REMARK 465 LYS A 1002
REMARK 465 GLU A 1003
REMARK 465 LYS A 1004
REMARK 465 PHE A 1005
REMARK 465 GLU A 1006
REMARK 465 ARG A 1007
REMARK 465 THR A 1008
REMARK 465 ALA A 1042
REMARK 465 ALA A 1043
REMARK 465 ARG A 1044
REMARK 465 ALA A 1045
REMARK 465 PHE A 1046
REMARK 465 ASP A 1047
REMARK 465 GLN A 1048
REMARK 465 ILE A 1049
REMARK 465 ASP A 1050
REMARK 465 ASN A 1051
REMARK 465 ALA A 1052
REMARK 465 PRO A 1053
REMARK 465 GLU A 1054
REMARK 465 GLU A 1055
REMARK 465 LYS A 1056
REMARK 465 ALA A 1057
REMARK 465 ARG A 1058
REMARK 465 GLY A 1059
REMARK 465 ILE A 1060
REMARK 465 THR A 1061
REMARK 465 ILE A 1062
REMARK 465 ASN A 1063
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 LYS G 3
REMARK 465 THR G 4
REMARK 465 ALA G 5
REMARK 465 SER G 6
REMARK 465 ASP G 114
REMARK 465 TYR G 115
REMARK 465 SER G 116
REMARK 465 GLU G 117
REMARK 465 ASP G 118
REMARK 465 GLU G 520
REMARK 465 SER G 521
REMARK 465 ASN G 522
REMARK 465 ASP G 523
REMARK 465 GLY G 524
REMARK 465 LEU G 525
REMARK 465 PRO G 526
REMARK 465 LEU G 527
REMARK 465 ARG G 528
REMARK 465 GLY G 529
REMARK 465 PRO G 530
REMARK 465 SER G 531
REMARK 465 GLY G 532
REMARK 465 PRO G 574
REMARK 465 TYR G 575
REMARK 465 GLY G 576
REMARK 465 VAL G 577
REMARK 465 PHE G 578
REMARK 465 GLN G 579
REMARK 465 GLY G 580
REMARK 465 THR G 581
REMARK 465 LYS G 582
REMARK 465 VAL G 583
REMARK 465 ALA G 584
REMARK 465 SER G 585
REMARK 465 LEU G 586
REMARK 465 HIS G 587
REMARK 465 GLU G 588
REMARK 465 ALA G 589
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 GLU C 2
REMARK 465 HIS C 999
REMARK 465 MET C 1000
REMARK 465 SER C 1001
REMARK 465 LYS C 1002
REMARK 465 GLU C 1003
REMARK 465 LYS C 1004
REMARK 465 PHE C 1005
REMARK 465 GLU C 1006
REMARK 465 ARG C 1007
REMARK 465 THR C 1008
REMARK 465 ALA C 1042
REMARK 465 ALA C 1043
REMARK 465 ARG C 1044
REMARK 465 ALA C 1045
REMARK 465 PHE C 1046
REMARK 465 ASP C 1047
REMARK 465 GLN C 1048
REMARK 465 ILE C 1049
REMARK 465 ASP C 1050
REMARK 465 ASN C 1051
REMARK 465 ALA C 1052
REMARK 465 PRO C 1053
REMARK 465 GLU C 1054
REMARK 465 GLU C 1055
REMARK 465 LYS C 1056
REMARK 465 ALA C 1057
REMARK 465 ARG C 1058
REMARK 465 GLY C 1059
REMARK 465 ILE C 1060
REMARK 465 THR C 1061
REMARK 465 ILE C 1062
REMARK 465 ASN C 1063
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 LYS F 3
REMARK 465 THR F 4
REMARK 465 ALA F 5
REMARK 465 SER F 6
REMARK 465 ASP F 114
REMARK 465 TYR F 115
REMARK 465 SER F 116
REMARK 465 GLU F 117
REMARK 465 ASP F 118
REMARK 465 GLU F 520
REMARK 465 SER F 521
REMARK 465 ASN F 522
REMARK 465 ASP F 523
REMARK 465 GLY F 524
REMARK 465 LEU F 525
REMARK 465 PRO F 526
REMARK 465 LEU F 527
REMARK 465 ARG F 528
REMARK 465 GLY F 529
REMARK 465 PRO F 530
REMARK 465 SER F 531
REMARK 465 GLY F 532
REMARK 465 PRO F 574
REMARK 465 TYR F 575
REMARK 465 GLY F 576
REMARK 465 VAL F 577
REMARK 465 PHE F 578
REMARK 465 GLN F 579
REMARK 465 GLY F 580
REMARK 465 THR F 581
REMARK 465 LYS F 582
REMARK 465 VAL F 583
REMARK 465 ALA F 584
REMARK 465 SER F 585
REMARK 465 LEU F 586
REMARK 465 HIS F 587
REMARK 465 GLU F 588
REMARK 465 ALA F 589
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 A1318 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A1318 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG C1318 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG C1318 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG C1318 NE - CZ - NH2 ANGL. DEV. = -8.1 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 ASN A 30 -169.29 53.93
REMARK 500 LYS A 103 45.59 34.56
REMARK 500 ARG A 132 -66.02 -97.41
REMARK 500 SER A 186 94.72 -43.03
REMARK 500 PRO A 207 149.39 -37.41
REMARK 500 GLU A 236 74.40 -167.01
REMARK 500 GLU A 262 122.44 -37.15
REMARK 500 GLU A 265 -80.26 25.28
REMARK 500 LYS A 266 51.55 88.42
REMARK 500 GLN A1097 99.82 -170.33
REMARK 500 PRO A1163 67.39 -69.68
REMARK 500 ARG A1223 -48.79 -134.62
REMARK 500 ILE A1247 -58.66 63.07
REMARK 500 PHE A1323 -159.26 -139.01
REMARK 500 ARG A1333 -61.43 69.42
REMARK 500 LEU A1392 -87.76 -122.89
REMARK 500 ARG G 8 78.97 -151.84
REMARK 500 SER G 83 65.42 -113.75
REMARK 500 LYS G 214 -66.48 -135.82
REMARK 500 SER G 276 81.00 -51.43
REMARK 500 ALA G 277 46.82 39.15
REMARK 500 ASN C 30 -168.66 53.37
REMARK 500 LYS C 103 44.74 36.39
REMARK 500 ARG C 132 -66.94 -96.22
REMARK 500 SER C 186 94.22 -42.67
REMARK 500 PRO C 207 149.35 -36.68
REMARK 500 GLU C 236 74.11 -168.08
REMARK 500 GLU C 262 122.83 -36.24
REMARK 500 GLU C 265 -80.46 25.14
REMARK 500 LYS C 266 51.20 88.75
REMARK 500 GLN C1097 100.19 -170.43
REMARK 500 PRO C1163 65.64 -68.28
REMARK 500 ARG C1223 -49.02 -133.46
REMARK 500 ILE C1247 -56.44 61.43
REMARK 500 ARG C1333 -61.16 67.98
REMARK 500 ARG F 8 78.54 -151.88
REMARK 500 SER F 83 66.74 -114.19
REMARK 500 LYS F 214 -65.68 -134.26
REMARK 500 ASN F 268 14.62 58.82
REMARK 500 SER F 276 80.53 -50.98
REMARK 500 ALA F 277 47.59 39.30
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 LEU A 1392 SER A 1393 -143.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 667 DISTANCE = 5.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PXN A 1394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PXN C 1394
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAINS A AND C ARE A CHIMERA OF UNP ENTRIES P0A6P1 AND P0CE48 WITH
REMARK 999 A SINGLE HIS AS LINKER
DBREF 3MMP A 0 282 UNP P0A6P1 EFTS_ECOLI 1 283
DBREF 3MMP A 1000 1393 UNP P0CE48 EFTU2_ECOLI 1 394
DBREF 3MMP G 1 589 UNP P14647 RDRP_BPQBE 1 589
DBREF 3MMP C 0 282 UNP P0A6P1 EFTS_ECOLI 1 283
DBREF 3MMP C 1000 1393 UNP P0CE48 EFTU2_ECOLI 1 394
DBREF 3MMP F 1 589 UNP P14647 RDRP_BPQBE 1 589
SEQADV 3MMP HIS A 999 UNP P0A6P1 LINKER
SEQADV 3MMP HIS C 999 UNP P0A6P1 LINKER
SEQRES 1 A 678 MET ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG
SEQRES 2 A 678 GLU ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA
SEQRES 3 A 678 LEU THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU
SEQRES 4 A 678 ASN MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS
SEQRES 5 A 678 ALA GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS
SEQRES 6 A 678 ILE ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS
SEQRES 7 A 678 GLN THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA
SEQRES 8 A 678 PHE ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS
SEQRES 9 A 678 ILE THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU
SEQRES 10 A 678 GLU ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE
SEQRES 11 A 678 ASN ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU
SEQRES 12 A 678 GLY SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL
SEQRES 13 A 678 ALA ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE
SEQRES 14 A 678 ALA MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS
SEQRES 15 A 678 PRO GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR
SEQRES 16 A 678 GLN VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO
SEQRES 17 A 678 LYS GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS
SEQRES 18 A 678 LYS PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE
SEQRES 19 A 678 VAL MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS
SEQRES 20 A 678 GLU HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU
SEQRES 21 A 678 VAL GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA
SEQRES 22 A 678 ALA GLU VAL ALA ALA MET SER LYS GLN SER HIS MET SER
SEQRES 23 A 678 LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN VAL
SEQRES 24 A 678 GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR LEU
SEQRES 25 A 678 THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR GLY
SEQRES 26 A 678 GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA PRO
SEQRES 27 A 678 GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER HIS
SEQRES 28 A 678 VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS VAL
SEQRES 29 A 678 ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET ILE
SEQRES 30 A 678 THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL VAL
SEQRES 31 A 678 ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU HIS
SEQRES 32 A 678 ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE ILE
SEQRES 33 A 678 VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU GLU
SEQRES 34 A 678 LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU LEU
SEQRES 35 A 678 SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE VAL
SEQRES 36 A 678 ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA GLU
SEQRES 37 A 678 TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU ASP
SEQRES 38 A 678 SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS PRO
SEQRES 39 A 678 PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER GLY
SEQRES 40 A 678 ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY ILE
SEQRES 41 A 678 ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE LYS
SEQRES 42 A 678 GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET PHE
SEQRES 43 A 678 ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN VAL
SEQRES 44 A 678 GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE GLU
SEQRES 45 A 678 ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS PRO
SEQRES 46 A 678 HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER LYS
SEQRES 47 A 678 ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY TYR
SEQRES 48 A 678 ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY
SEQRES 49 A 678 THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET PRO
SEQRES 50 A 678 GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS PRO
SEQRES 51 A 678 ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG GLU
SEQRES 52 A 678 GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS VAL
SEQRES 53 A 678 LEU SER
SEQRES 1 G 589 MET SER LYS THR ALA SER SER ARG ASN SER LEU SER ALA
SEQRES 2 G 589 GLN LEU ARG ARG ALA ALA ASN THR ARG ILE GLU VAL GLU
SEQRES 3 G 589 GLY ASN LEU ALA LEU SER ILE ALA ASN ASP LEU LEU LEU
SEQRES 4 G 589 ALA TYR GLY GLN SER PRO PHE ASN SER GLU ALA GLU CYS
SEQRES 5 G 589 ILE SER PHE SER PRO ARG PHE ASP GLY THR PRO ASP ASP
SEQRES 6 G 589 PHE ARG ILE ASN TYR LEU LYS ALA GLU ILE MET SER LYS
SEQRES 7 G 589 TYR ASP ASP PHE SER LEU GLY ILE ASP THR GLU ALA VAL
SEQRES 8 G 589 ALA TRP GLU LYS PHE LEU ALA ALA GLU ALA GLU CYS ALA
SEQRES 9 G 589 LEU THR ASN ALA ARG LEU TYR ARG PRO ASP TYR SER GLU
SEQRES 10 G 589 ASP PHE ASN PHE SER LEU GLY GLU SER CYS ILE HIS MET
SEQRES 11 G 589 ALA ARG ARG LYS ILE ALA LYS LEU ILE GLY ASP VAL PRO
SEQRES 12 G 589 SER VAL GLU GLY MET LEU ARG HIS CYS ARG PHE SER GLY
SEQRES 13 G 589 GLY ALA THR THR THR ASN ASN ARG SER TYR GLY HIS PRO
SEQRES 14 G 589 SER PHE LYS PHE ALA LEU PRO GLN ALA CYS THR PRO ARG
SEQRES 15 G 589 ALA LEU LYS TYR VAL LEU ALA LEU ARG ALA SER THR HIS
SEQRES 16 G 589 PHE ASP THR ARG ILE SER ASP ILE SER PRO PHE ASN LYS
SEQRES 17 G 589 ALA VAL THR VAL PRO LYS ASN SER LYS THR ASP ARG CYS
SEQRES 18 G 589 ILE ALA ILE GLU PRO GLY TRP ASN MET PHE PHE GLN LEU
SEQRES 19 G 589 GLY ILE GLY GLY ILE LEU ARG ASP ARG LEU ARG CYS TRP
SEQRES 20 G 589 GLY ILE ASP LEU ASN ASP GLN THR ILE ASN GLN ARG ARG
SEQRES 21 G 589 ALA HIS GLU GLY SER VAL THR ASN ASN LEU ALA THR VAL
SEQRES 22 G 589 ASP LEU SER ALA ALA SER ASP SER ILE SER LEU ALA LEU
SEQRES 23 G 589 CYS GLU LEU LEU LEU PRO PRO GLY TRP PHE GLU VAL LEU
SEQRES 24 G 589 MET ASP LEU ARG SER PRO LYS GLY ARG LEU PRO ASP GLY
SEQRES 25 G 589 SER VAL VAL THR TYR GLU LYS ILE SER SER MET GLY ASN
SEQRES 26 G 589 GLY TYR THR PHE GLU LEU GLU SER LEU ILE PHE ALA SER
SEQRES 27 G 589 LEU ALA ARG SER VAL CYS GLU ILE LEU ASP LEU ASP SER
SEQRES 28 G 589 SER GLU VAL THR VAL TYR GLY ASP ASP ILE ILE LEU PRO
SEQRES 29 G 589 SER CYS ALA VAL PRO ALA LEU ARG GLU VAL PHE LYS TYR
SEQRES 30 G 589 VAL GLY PHE THR THR ASN THR LYS LYS THR PHE SER GLU
SEQRES 31 G 589 GLY PRO PHE ARG GLU SER CYS GLY LYS HIS TYR TYR SER
SEQRES 32 G 589 GLY VAL ASP VAL THR PRO PHE TYR ILE ARG HIS ARG ILE
SEQRES 33 G 589 VAL SER PRO ALA ASP LEU ILE LEU VAL LEU ASN ASN LEU
SEQRES 34 G 589 TYR ARG TRP ALA THR ILE ASP GLY VAL TRP ASP PRO ARG
SEQRES 35 G 589 ALA HIS SER VAL TYR LEU LYS TYR ARG LYS LEU LEU PRO
SEQRES 36 G 589 LYS GLN LEU GLN ARG ASN THR ILE PRO ASP GLY TYR GLY
SEQRES 37 G 589 ASP GLY ALA LEU VAL GLY SER VAL LEU ILE ASN PRO PHE
SEQRES 38 G 589 ALA LYS ASN ARG GLY TRP ILE ARG TYR VAL PRO VAL ILE
SEQRES 39 G 589 THR ASP HIS THR ARG ASP ARG GLU ARG ALA GLU LEU GLY
SEQRES 40 G 589 SER TYR LEU TYR ASP LEU PHE SER ARG CYS LEU SER GLU
SEQRES 41 G 589 SER ASN ASP GLY LEU PRO LEU ARG GLY PRO SER GLY CYS
SEQRES 42 G 589 ASP SER ALA ASP LEU PHE ALA ILE ASP GLN LEU ILE CYS
SEQRES 43 G 589 ARG SER ASN PRO THR LYS ILE SER ARG SER THR GLY LYS
SEQRES 44 G 589 PHE ASP ILE GLN TYR ILE ALA CYS SER SER ARG VAL LEU
SEQRES 45 G 589 ALA PRO TYR GLY VAL PHE GLN GLY THR LYS VAL ALA SER
SEQRES 46 G 589 LEU HIS GLU ALA
SEQRES 1 C 678 MET ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG
SEQRES 2 C 678 GLU ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA
SEQRES 3 C 678 LEU THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU
SEQRES 4 C 678 ASN MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS
SEQRES 5 C 678 ALA GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS
SEQRES 6 C 678 ILE ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS
SEQRES 7 C 678 GLN THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA
SEQRES 8 C 678 PHE ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS
SEQRES 9 C 678 ILE THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU
SEQRES 10 C 678 GLU ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE
SEQRES 11 C 678 ASN ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU
SEQRES 12 C 678 GLY SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL
SEQRES 13 C 678 ALA ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE
SEQRES 14 C 678 ALA MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS
SEQRES 15 C 678 PRO GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR
SEQRES 16 C 678 GLN VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO
SEQRES 17 C 678 LYS GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS
SEQRES 18 C 678 LYS PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE
SEQRES 19 C 678 VAL MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS
SEQRES 20 C 678 GLU HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU
SEQRES 21 C 678 VAL GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA
SEQRES 22 C 678 ALA GLU VAL ALA ALA MET SER LYS GLN SER HIS MET SER
SEQRES 23 C 678 LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN VAL
SEQRES 24 C 678 GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR LEU
SEQRES 25 C 678 THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR GLY
SEQRES 26 C 678 GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA PRO
SEQRES 27 C 678 GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER HIS
SEQRES 28 C 678 VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS VAL
SEQRES 29 C 678 ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET ILE
SEQRES 30 C 678 THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL VAL
SEQRES 31 C 678 ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU HIS
SEQRES 32 C 678 ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE ILE
SEQRES 33 C 678 VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU GLU
SEQRES 34 C 678 LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU LEU
SEQRES 35 C 678 SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE VAL
SEQRES 36 C 678 ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA GLU
SEQRES 37 C 678 TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU ASP
SEQRES 38 C 678 SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS PRO
SEQRES 39 C 678 PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER GLY
SEQRES 40 C 678 ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY ILE
SEQRES 41 C 678 ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE LYS
SEQRES 42 C 678 GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET PHE
SEQRES 43 C 678 ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN VAL
SEQRES 44 C 678 GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE GLU
SEQRES 45 C 678 ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS PRO
SEQRES 46 C 678 HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER LYS
SEQRES 47 C 678 ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY TYR
SEQRES 48 C 678 ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY
SEQRES 49 C 678 THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET PRO
SEQRES 50 C 678 GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS PRO
SEQRES 51 C 678 ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG GLU
SEQRES 52 C 678 GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS VAL
SEQRES 53 C 678 LEU SER
SEQRES 1 F 589 MET SER LYS THR ALA SER SER ARG ASN SER LEU SER ALA
SEQRES 2 F 589 GLN LEU ARG ARG ALA ALA ASN THR ARG ILE GLU VAL GLU
SEQRES 3 F 589 GLY ASN LEU ALA LEU SER ILE ALA ASN ASP LEU LEU LEU
SEQRES 4 F 589 ALA TYR GLY GLN SER PRO PHE ASN SER GLU ALA GLU CYS
SEQRES 5 F 589 ILE SER PHE SER PRO ARG PHE ASP GLY THR PRO ASP ASP
SEQRES 6 F 589 PHE ARG ILE ASN TYR LEU LYS ALA GLU ILE MET SER LYS
SEQRES 7 F 589 TYR ASP ASP PHE SER LEU GLY ILE ASP THR GLU ALA VAL
SEQRES 8 F 589 ALA TRP GLU LYS PHE LEU ALA ALA GLU ALA GLU CYS ALA
SEQRES 9 F 589 LEU THR ASN ALA ARG LEU TYR ARG PRO ASP TYR SER GLU
SEQRES 10 F 589 ASP PHE ASN PHE SER LEU GLY GLU SER CYS ILE HIS MET
SEQRES 11 F 589 ALA ARG ARG LYS ILE ALA LYS LEU ILE GLY ASP VAL PRO
SEQRES 12 F 589 SER VAL GLU GLY MET LEU ARG HIS CYS ARG PHE SER GLY
SEQRES 13 F 589 GLY ALA THR THR THR ASN ASN ARG SER TYR GLY HIS PRO
SEQRES 14 F 589 SER PHE LYS PHE ALA LEU PRO GLN ALA CYS THR PRO ARG
SEQRES 15 F 589 ALA LEU LYS TYR VAL LEU ALA LEU ARG ALA SER THR HIS
SEQRES 16 F 589 PHE ASP THR ARG ILE SER ASP ILE SER PRO PHE ASN LYS
SEQRES 17 F 589 ALA VAL THR VAL PRO LYS ASN SER LYS THR ASP ARG CYS
SEQRES 18 F 589 ILE ALA ILE GLU PRO GLY TRP ASN MET PHE PHE GLN LEU
SEQRES 19 F 589 GLY ILE GLY GLY ILE LEU ARG ASP ARG LEU ARG CYS TRP
SEQRES 20 F 589 GLY ILE ASP LEU ASN ASP GLN THR ILE ASN GLN ARG ARG
SEQRES 21 F 589 ALA HIS GLU GLY SER VAL THR ASN ASN LEU ALA THR VAL
SEQRES 22 F 589 ASP LEU SER ALA ALA SER ASP SER ILE SER LEU ALA LEU
SEQRES 23 F 589 CYS GLU LEU LEU LEU PRO PRO GLY TRP PHE GLU VAL LEU
SEQRES 24 F 589 MET ASP LEU ARG SER PRO LYS GLY ARG LEU PRO ASP GLY
SEQRES 25 F 589 SER VAL VAL THR TYR GLU LYS ILE SER SER MET GLY ASN
SEQRES 26 F 589 GLY TYR THR PHE GLU LEU GLU SER LEU ILE PHE ALA SER
SEQRES 27 F 589 LEU ALA ARG SER VAL CYS GLU ILE LEU ASP LEU ASP SER
SEQRES 28 F 589 SER GLU VAL THR VAL TYR GLY ASP ASP ILE ILE LEU PRO
SEQRES 29 F 589 SER CYS ALA VAL PRO ALA LEU ARG GLU VAL PHE LYS TYR
SEQRES 30 F 589 VAL GLY PHE THR THR ASN THR LYS LYS THR PHE SER GLU
SEQRES 31 F 589 GLY PRO PHE ARG GLU SER CYS GLY LYS HIS TYR TYR SER
SEQRES 32 F 589 GLY VAL ASP VAL THR PRO PHE TYR ILE ARG HIS ARG ILE
SEQRES 33 F 589 VAL SER PRO ALA ASP LEU ILE LEU VAL LEU ASN ASN LEU
SEQRES 34 F 589 TYR ARG TRP ALA THR ILE ASP GLY VAL TRP ASP PRO ARG
SEQRES 35 F 589 ALA HIS SER VAL TYR LEU LYS TYR ARG LYS LEU LEU PRO
SEQRES 36 F 589 LYS GLN LEU GLN ARG ASN THR ILE PRO ASP GLY TYR GLY
SEQRES 37 F 589 ASP GLY ALA LEU VAL GLY SER VAL LEU ILE ASN PRO PHE
SEQRES 38 F 589 ALA LYS ASN ARG GLY TRP ILE ARG TYR VAL PRO VAL ILE
SEQRES 39 F 589 THR ASP HIS THR ARG ASP ARG GLU ARG ALA GLU LEU GLY
SEQRES 40 F 589 SER TYR LEU TYR ASP LEU PHE SER ARG CYS LEU SER GLU
SEQRES 41 F 589 SER ASN ASP GLY LEU PRO LEU ARG GLY PRO SER GLY CYS
SEQRES 42 F 589 ASP SER ALA ASP LEU PHE ALA ILE ASP GLN LEU ILE CYS
SEQRES 43 F 589 ARG SER ASN PRO THR LYS ILE SER ARG SER THR GLY LYS
SEQRES 44 F 589 PHE ASP ILE GLN TYR ILE ALA CYS SER SER ARG VAL LEU
SEQRES 45 F 589 ALA PRO TYR GLY VAL PHE GLN GLY THR LYS VAL ALA SER
SEQRES 46 F 589 LEU HIS GLU ALA
HET PXN A1394 25
HET PXN C1394 25
HETNAM PXN (2S)-1-[3-{[(2R)-2-HYDROXYPROPYL]OXY}-2,2-BIS({[(2R)-2-
HETNAM 2 PXN HYDROXYPROPYL]OXY}METHYL)PROPOXY]PROPAN-2-OL
HETSYN PXN PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH)
FORMUL 5 PXN 2(C17 H36 O8)
FORMUL 7 HOH *925(H2 O)
HELIX 1 1 THR A 4 GLY A 16 1 13
HELIX 2 2 GLY A 18 LEU A 26 1 9
HELIX 3 3 ASP A 32 ALA A 52 1 21
HELIX 4 4 THR A 79 ASP A 85 1 7
HELIX 5 5 ASP A 85 GLY A 102 1 18
HELIX 6 6 ASP A 106 GLY A 126 1 21
HELIX 7 7 ASP A 161 LYS A 176 1 16
HELIX 8 8 LYS A 181 VAL A 185 5 5
HELIX 9 9 LYS A 192 MET A 202 1 11
HELIX 10 10 PRO A 207 VAL A 226 1 20
HELIX 11 11 SER A 227 GLY A 230 5 4
HELIX 12 12 VAL A 241 HIS A 248 1 8
HELIX 13 13 ASP A 270 SER A 282 1 13
HELIX 14 14 GLY A 1023 GLY A 1040 1 18
HELIX 15 15 GLY A 1083 THR A 1093 1 11
HELIX 16 16 GLN A 1114 VAL A 1125 1 12
HELIX 17 17 LYS A 1136 VAL A 1140 5 5
HELIX 18 18 ASP A 1142 TYR A 1160 1 19
HELIX 19 19 PRO A 1163 THR A 1167 5 5
HELIX 20 20 SER A 1173 GLY A 1180 1 8
HELIX 21 21 ASP A 1181 ILE A 1199 1 19
HELIX 22 22 ARG A 1204 LYS A 1208 5 5
HELIX 23 23 LYS A 1282 ILE A 1286 5 5
HELIX 24 24 SER G 10 ASN G 20 1 11
HELIX 25 25 ASN G 28 TYR G 41 1 14
HELIX 26 26 SER G 48 SER G 54 1 7
HELIX 27 27 THR G 62 MET G 76 1 15
HELIX 28 28 ASP G 87 TYR G 111 1 25
HELIX 29 29 SER G 122 GLY G 140 1 19
HELIX 30 30 SER G 144 CYS G 152 1 9
HELIX 31 31 ASN G 163 GLY G 167 5 5
HELIX 32 32 HIS G 168 LEU G 175 1 8
HELIX 33 33 THR G 180 ARG G 182 5 3
HELIX 34 34 ALA G 183 SER G 193 1 11
HELIX 35 35 PRO G 226 ARG G 245 1 20
HELIX 36 36 CYS G 246 GLY G 248 5 3
HELIX 37 37 GLN G 254 ASN G 268 1 15
HELIX 38 38 ALA G 277 SER G 281 5 5
HELIX 39 39 SER G 283 LEU G 291 1 9
HELIX 40 40 PRO G 292 ARG G 303 1 12
HELIX 41 41 TYR G 327 ASP G 348 1 22
HELIX 42 42 ASP G 350 VAL G 354 5 5
HELIX 43 43 ALA G 367 VAL G 378 1 12
HELIX 44 44 ASN G 383 THR G 387 5 5
HELIX 45 45 SER G 418 ALA G 433 1 16
HELIX 46 46 ASP G 440 LYS G 452 1 13
HELIX 47 47 PRO G 455 ASN G 461 1 7
HELIX 48 48 SER G 475 ASN G 479 5 5
HELIX 49 49 ALA G 504 LEU G 518 1 15
HELIX 50 50 SER G 535 GLN G 543 1 9
HELIX 51 51 THR C 4 GLY C 16 1 13
HELIX 52 52 GLY C 18 LEU C 26 1 9
HELIX 53 53 ASP C 32 ALA C 52 1 21
HELIX 54 54 THR C 79 ASP C 85 1 7
HELIX 55 55 ASP C 85 GLY C 102 1 18
HELIX 56 56 ASP C 106 GLY C 126 1 21
HELIX 57 57 ASP C 161 LYS C 176 1 16
HELIX 58 58 LYS C 181 VAL C 185 5 5
HELIX 59 59 LYS C 192 MET C 202 1 11
HELIX 60 60 PRO C 207 VAL C 226 1 20
HELIX 61 61 VAL C 241 HIS C 248 1 8
HELIX 62 62 ASP C 270 SER C 282 1 13
HELIX 63 63 GLY C 1023 GLY C 1040 1 18
HELIX 64 64 GLY C 1083 THR C 1093 1 11
HELIX 65 65 GLN C 1114 VAL C 1125 1 12
HELIX 66 66 LYS C 1136 VAL C 1140 5 5
HELIX 67 67 ASP C 1142 TYR C 1160 1 19
HELIX 68 68 PRO C 1163 THR C 1167 5 5
HELIX 69 69 SER C 1173 GLY C 1180 1 8
HELIX 70 70 ASP C 1181 ILE C 1199 1 19
HELIX 71 71 ARG C 1204 LYS C 1208 5 5
HELIX 72 72 LYS C 1282 ILE C 1286 5 5
HELIX 73 73 SER F 10 ASN F 20 1 11
HELIX 74 74 ASN F 28 TYR F 41 1 14
HELIX 75 75 SER F 48 SER F 54 1 7
HELIX 76 76 THR F 62 ILE F 75 1 14
HELIX 77 77 ASP F 87 TYR F 111 1 25
HELIX 78 78 SER F 122 GLY F 140 1 19
HELIX 79 79 SER F 144 CYS F 152 1 9
HELIX 80 80 ASN F 163 GLY F 167 5 5
HELIX 81 81 HIS F 168 LEU F 175 1 8
HELIX 82 82 ALA F 183 SER F 193 1 11
HELIX 83 83 PRO F 226 ARG F 245 1 20
HELIX 84 84 CYS F 246 GLY F 248 5 3
HELIX 85 85 GLN F 254 ASN F 268 1 15
HELIX 86 86 ALA F 277 SER F 281 5 5
HELIX 87 87 SER F 283 LEU F 291 1 9
HELIX 88 88 PRO F 292 ARG F 303 1 12
HELIX 89 89 TYR F 327 ASP F 348 1 22
HELIX 90 90 ASP F 350 VAL F 354 5 5
HELIX 91 91 ALA F 367 VAL F 378 1 12
HELIX 92 92 ASN F 383 THR F 387 5 5
HELIX 93 93 SER F 418 ALA F 433 1 16
HELIX 94 94 ASP F 440 LYS F 452 1 13
HELIX 95 95 PRO F 455 ASN F 461 1 7
HELIX 96 96 SER F 475 ASN F 479 5 5
HELIX 97 97 ALA F 504 LEU F 518 1 15
HELIX 98 98 SER F 535 GLN F 543 1 9
SHEET 1 A 3 ASP A 58 ASP A 66 0
SHEET 2 A 3 TYR A 69 CYS A 77 -1 O LEU A 73 N LYS A 62
SHEET 3 A 3 ASN A 130 GLU A 138 -1 O ASN A 130 N ASN A 76
SHEET 1 B 3 VAL A 141 HIS A 147 0
SHEET 2 B 3 ILE A 151 LYS A 158 -1 O ILE A 151 N HIS A 147
SHEET 3 B 3 GLU A 251 GLU A 259 -1 O PHE A 258 N GLY A 152
SHEET 1 C 2 PRO A 232 PHE A 233 0
SHEET 2 C 2 GLU A 236 THR A 240 -1 O LYS A 239 N PHE A 233
SHEET 1 D 6 VAL A1067 ASP A1070 0
SHEET 2 D 6 HIS A1075 ASP A1080 -1 O HIS A1078 N VAL A1067
SHEET 3 D 6 HIS A1011 GLY A1018 1 N VAL A1014 O ALA A1077
SHEET 4 D 6 GLY A1100 ALA A1106 1 O ILE A1102 N GLY A1015
SHEET 5 D 6 ILE A1130 ASN A1135 1 O ILE A1131 N ALA A1101
SHEET 6 D 6 ILE A1169 ARG A1171 1 O VAL A1170 N LEU A1134
SHEET 1 E 7 LEU A1211 PRO A1213 0
SHEET 2 E 7 VAL A1291 ALA A1293 -1 O LEU A1292 N LEU A1212
SHEET 3 E 7 GLU A1241 VAL A1245 -1 N GLU A1243 O ALA A1293
SHEET 4 E 7 GLN A1251 GLU A1259 -1 O GLN A1251 N ILE A1244
SHEET 5 E 7 ASN A1273 LEU A1278 -1 O GLY A1275 N GLU A1259
SHEET 6 E 7 GLY A1224 ARG A1230 -1 N VAL A1227 O VAL A1276
SHEET 7 E 7 ASP A1216 ILE A1220 -1 N ILE A1220 O GLY A1224
SHEET 1 F 5 LEU A1211 PRO A1213 0
SHEET 2 F 5 VAL A1291 ALA A1293 -1 O LEU A1292 N LEU A1212
SHEET 3 F 5 GLU A1241 VAL A1245 -1 N GLU A1243 O ALA A1293
SHEET 4 F 5 GLN A1251 GLU A1259 -1 O GLN A1251 N ILE A1244
SHEET 5 F 5 LEU A1264 LEU A1265 -1 O LEU A1265 N VAL A1258
SHEET 1 G 2 ILE A1235 LYS A1237 0
SHEET 2 G 2 GLU A1267 ARG A1269 -1 O GLY A1268 N ILE A1236
SHEET 1 H 7 PRO A1300 ILE A1310 0
SHEET 2 H 7 ASN A1355 ALA A1367 -1 O LEU A1362 N THR A1302
SHEET 3 H 7 THR A1335 GLU A1342 -1 N THR A1338 O ILE A1363
SHEET 4 H 7 GLN A1329 PHE A1332 -1 N PHE A1330 O VAL A1337
SHEET 5 H 7 ARG A1373 GLU A1378 -1 O ARG A1377 N GLN A1329
SHEET 6 H 7 ARG A1381 VAL A1391 -1 O GLY A1386 N PHE A1374
SHEET 7 H 7 PRO A1300 ILE A1310 -1 N GLU A1305 O LYS A1390
SHEET 1 I 2 GLN G 177 CYS G 179 0
SHEET 2 I 2 ILE G 200 ILE G 203 1 O ASP G 202 N CYS G 179
SHEET 1 J 4 ARG G 220 ILE G 224 0
SHEET 2 J 4 PHE G 206 VAL G 212 -1 N VAL G 212 O ARG G 220
SHEET 3 J 4 LYS G 306 ARG G 308 1 O ARG G 308 N ALA G 209
SHEET 4 J 4 VAL G 314 THR G 316 -1 O VAL G 315 N GLY G 307
SHEET 1 K 3 LEU G 270 ASP G 274 0
SHEET 2 K 3 ASP G 360 PRO G 364 -1 O LEU G 363 N ALA G 271
SHEET 3 K 3 THR G 355 TYR G 357 -1 N THR G 355 O ILE G 362
SHEET 1 L 3 PHE G 393 SER G 396 0
SHEET 2 L 3 LYS G 399 TYR G 402 -1 O TYR G 401 N ARG G 394
SHEET 3 L 3 VAL G 405 ASP G 406 -1 O VAL G 405 N TYR G 402
SHEET 1 M 2 THR G 434 ILE G 435 0
SHEET 2 M 2 VAL G 438 TRP G 439 -1 O VAL G 438 N ILE G 435
SHEET 1 N 2 THR G 462 ILE G 463 0
SHEET 2 N 2 LEU G 472 VAL G 473 1 O LEU G 472 N ILE G 463
SHEET 1 O 3 LYS G 483 ARG G 485 0
SHEET 2 O 3 ILE G 488 ARG G 501 -1 O ILE G 488 N ARG G 485
SHEET 3 O 3 ILE G 553 CYS G 567 -1 O ASP G 561 N THR G 495
SHEET 1 P 3 ASP C 58 ASP C 66 0
SHEET 2 P 3 TYR C 69 CYS C 77 -1 O LEU C 73 N LYS C 62
SHEET 3 P 3 ASN C 130 GLU C 138 -1 O ASN C 130 N ASN C 76
SHEET 1 Q 3 VAL C 141 HIS C 147 0
SHEET 2 Q 3 ILE C 151 LYS C 158 -1 O VAL C 155 N GLY C 143
SHEET 3 Q 3 GLU C 251 GLU C 259 -1 O PHE C 258 N GLY C 152
SHEET 1 R 2 PRO C 232 PHE C 233 0
SHEET 2 R 2 GLU C 236 THR C 240 -1 O LYS C 239 N PHE C 233
SHEET 1 S 6 VAL C1067 ASP C1070 0
SHEET 2 S 6 HIS C1075 ASP C1080 -1 O HIS C1078 N VAL C1067
SHEET 3 S 6 HIS C1011 GLY C1018 1 N VAL C1014 O ALA C1077
SHEET 4 S 6 GLY C1100 ALA C1106 1 O ILE C1102 N GLY C1015
SHEET 5 S 6 ILE C1130 ASN C1135 1 O ILE C1131 N ALA C1101
SHEET 6 S 6 ILE C1169 ARG C1171 1 O VAL C1170 N LEU C1134
SHEET 1 T 7 LEU C1211 PRO C1213 0
SHEET 2 T 7 VAL C1291 ALA C1293 -1 O LEU C1292 N LEU C1212
SHEET 3 T 7 GLU C1241 VAL C1245 -1 N GLU C1243 O ALA C1293
SHEET 4 T 7 GLN C1251 GLU C1259 -1 O GLN C1251 N ILE C1244
SHEET 5 T 7 ASN C1273 LEU C1278 -1 O GLY C1275 N GLU C1259
SHEET 6 T 7 GLY C1224 ARG C1230 -1 N VAL C1227 O VAL C1276
SHEET 7 T 7 ASP C1216 ILE C1220 -1 N ILE C1220 O GLY C1224
SHEET 1 U 5 LEU C1211 PRO C1213 0
SHEET 2 U 5 VAL C1291 ALA C1293 -1 O LEU C1292 N LEU C1212
SHEET 3 U 5 GLU C1241 VAL C1245 -1 N GLU C1243 O ALA C1293
SHEET 4 U 5 GLN C1251 GLU C1259 -1 O GLN C1251 N ILE C1244
SHEET 5 U 5 LEU C1264 LEU C1265 -1 O LEU C1265 N VAL C1258
SHEET 1 V 2 ILE C1235 LYS C1237 0
SHEET 2 V 2 GLU C1267 ARG C1269 -1 O GLY C1268 N ILE C1236
SHEET 1 W 7 PRO C1300 ILE C1310 0
SHEET 2 W 7 ASN C1355 ALA C1367 -1 O LEU C1362 N THR C1302
SHEET 3 W 7 THR C1335 GLU C1342 -1 N THR C1338 O ILE C1363
SHEET 4 W 7 GLN C1329 PHE C1332 -1 N PHE C1330 O VAL C1337
SHEET 5 W 7 ARG C1373 GLU C1378 -1 O ARG C1377 N GLN C1329
SHEET 6 W 7 ARG C1381 VAL C1391 -1 O GLY C1386 N PHE C1374
SHEET 7 W 7 PRO C1300 ILE C1310 -1 N TYR C1309 O ALA C1385
SHEET 1 X 2 GLN F 177 CYS F 179 0
SHEET 2 X 2 ILE F 200 ILE F 203 1 O SER F 201 N GLN F 177
SHEET 1 Y 4 ARG F 220 ILE F 224 0
SHEET 2 Y 4 PHE F 206 VAL F 212 -1 N VAL F 212 O ARG F 220
SHEET 3 Y 4 LYS F 306 ARG F 308 1 O ARG F 308 N ALA F 209
SHEET 4 Y 4 VAL F 314 THR F 316 -1 O VAL F 315 N GLY F 307
SHEET 1 Z 3 LEU F 270 ASP F 274 0
SHEET 2 Z 3 ASP F 360 PRO F 364 -1 O LEU F 363 N ALA F 271
SHEET 3 Z 3 THR F 355 TYR F 357 -1 N THR F 355 O ILE F 362
SHEET 1 AA 3 PHE F 393 SER F 396 0
SHEET 2 AA 3 LYS F 399 TYR F 402 -1 O TYR F 401 N ARG F 394
SHEET 3 AA 3 VAL F 405 ASP F 406 -1 O VAL F 405 N TYR F 402
SHEET 1 AB 2 THR F 434 ILE F 435 0
SHEET 2 AB 2 VAL F 438 TRP F 439 -1 O VAL F 438 N ILE F 435
SHEET 1 AC 2 THR F 462 ILE F 463 0
SHEET 2 AC 2 LEU F 472 VAL F 473 1 O LEU F 472 N ILE F 463
SHEET 1 AD 3 LYS F 483 ARG F 485 0
SHEET 2 AD 3 ILE F 488 ARG F 501 -1 O ILE F 488 N ARG F 485
SHEET 3 AD 3 ILE F 553 CYS F 567 -1 O ASP F 561 N THR F 495
SITE 1 AC1 7 HOH A 741 HOH A 887 ARG A1262 PRO G 143
SITE 2 AC1 7 MET G 148 TYR G 186 ALA G 189
SITE 1 AC2 4 ARG C1262 PRO F 143 MET F 148 TYR F 186
CRYST1 254.710 139.400 101.870 90.00 92.06 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 0.003926 0.000000 0.000141 0.00000
SCALE2 0.000000 0.007174 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009823 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
