HEADER TRANSLATION/RNA 11-NOV-04 1WSU
TITLE C-TERMINAL DOMAIN OF ELONGATION FACTOR SELB COMPLEXED WITH SECIS RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-R(*GP*GP*CP*GP*UP*UP*GP*CP*CP*GP*GP*UP*CP*U*GP*GP*CP*AP*
COMPND 3 AP*CP*GP*CP*C)-3';
COMPND 4 CHAIN: E, F, G;
COMPND 5 SYNONYM: SECIS RNA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR;
COMPND 9 CHAIN: A, B, C, D;
COMPND 10 FRAGMENT: SECIS BINDING DOMAIN;
COMPND 11 SYNONYM: SELB TRANSLATION FACTOR;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SELENOCYSTEIN INCORPORATED SEQUENCE OF RNA. THE FIRST
SOURCE 4 3 AND LAST 3 RESIDUES ARE CLONING ARTIFACTS.;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MOORELLA THERMOACETICA;
SOURCE 7 ORGANISM_TAXID: 1525;
SOURCE 8 GENE: SELB;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS WINGED-HELIX, TRANSLATION-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.YOSHIZAWA,L.RASUBALA,T.OSE,D.KOHDA,D.FOURMY,K.MAENAKA
REVDAT 5 25-OCT-23 1WSU 1 SEQADV
REVDAT 4 24-FEB-09 1WSU 1 VERSN
REVDAT 3 05-APR-05 1WSU 1 SOURCE
REVDAT 2 08-MAR-05 1WSU 1 JRNL
REVDAT 1 25-JAN-05 1WSU 0
JRNL AUTH S.YOSHIZAWA,L.RASUBALA,T.OSE,D.KOHDA,D.FOURMY,K.MAENAKA
JRNL TITL STRUCTURAL BASIS FOR MRNA RECOGNITION BY ELONGATION FACTOR
JRNL TITL 2 SELB
JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 198 2005
JRNL REFN ISSN 1545-9993
JRNL PMID 15665870
JRNL DOI 10.1038/NSMB890
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 41657
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 SET) : 0.224
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4099
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 0.73
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 316
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 : 3836
REMARK 3 NUCLEIC ACID ATOMS : 1375
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.83100
REMARK 3 B22 (A**2) : -13.21100
REMARK 3 B33 (A**2) : -0.62000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.37
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.152
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.76
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.104
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000023959.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-03
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 : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41948
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.20800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1LVA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI-SODIUM CITRATE DIHYDRATE, HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 40.93250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.90700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.93250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.90700
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: HEPTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, 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 U E 26
REMARK 465 U F 26
REMARK 465 C G 25
REMARK 465 U G 26
REMARK 465 GLY B 633
REMARK 465 ASN B 634
REMARK 465 GLY C 511
REMARK 465 SER C 512
REMARK 465 GLU C 513
REMARK 465 THR C 514
REMARK 465 GLN C 515
REMARK 465 LYS C 516
REMARK 465 GLY C 541
REMARK 465 SER C 542
REMARK 465 PHE C 543
REMARK 465 ASN C 544
REMARK 465 LEU C 545
REMARK 465 ASP C 546
REMARK 465 PRO C 547
REMARK 465 SER C 548
REMARK 465 GLU C 549
REMARK 465 LEU C 550
REMARK 465 ARG C 624
REMARK 465 VAL C 625
REMARK 465 GLY C 626
REMARK 465 ASP C 627
REMARK 465 GLY C 633
REMARK 465 ASN C 634
REMARK 465 GLY D 511
REMARK 465 SER D 589
REMARK 465 THR D 590
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 G E 27 P OP1 OP2
REMARK 470 G F 27 P OP1 OP2
REMARK 470 G G 27 P OP1 OP2
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 512 -96.13 -127.40
REMARK 500 GLU A 513 -8.42 -144.82
REMARK 500 ARG A 530 -103.43 51.38
REMARK 500 SER A 604 -148.02 -102.06
REMARK 500 ARG B 530 -98.50 45.24
REMARK 500 SER B 604 -148.41 -112.89
REMARK 500 ARG C 530 -119.82 59.09
REMARK 500 GLU C 569 -77.24 -69.30
REMARK 500 THR C 590 41.36 -94.62
REMARK 500 PRO C 592 -175.61 -59.04
REMARK 500 PHE C 593 134.87 -172.48
REMARK 500 SER C 604 -133.30 -100.75
REMARK 500 VAL C 619 4.15 -60.87
REMARK 500 THR D 514 27.23 -76.03
REMARK 500 ARG D 530 -109.82 46.97
REMARK 500 GLN D 532 54.88 -117.20
REMARK 500 ASN D 544 82.16 69.80
REMARK 500 ASP D 546 166.68 -47.57
REMARK 500 PRO D 547 -102.44 -57.37
REMARK 500 SER D 548 16.38 -65.92
REMARK 500 SER D 604 -169.11 -124.54
REMARK 500 VAL D 631 98.41 -57.34
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WSU A 512 634 UNP Q46455 SELB_MOOTH 512 634
DBREF 1WSU B 512 634 UNP Q46455 SELB_MOOTH 512 634
DBREF 1WSU C 512 634 UNP Q46455 SELB_MOOTH 512 634
DBREF 1WSU D 512 634 UNP Q46455 SELB_MOOTH 512 634
DBREF 1WSU E 13 35 PDB 1WSU 1WSU 13 35
DBREF 1WSU F 13 35 PDB 1WSU 1WSU 13 35
DBREF 1WSU G 13 35 PDB 1WSU 1WSU 13 35
SEQADV 1WSU GLY A 511 UNP Q46455 CLONING ARTIFACT
SEQADV 1WSU GLY B 511 UNP Q46455 CLONING ARTIFACT
SEQADV 1WSU GLY C 511 UNP Q46455 CLONING ARTIFACT
SEQADV 1WSU GLY D 511 UNP Q46455 CLONING ARTIFACT
SEQRES 1 E 23 G G C G U U G C C G G U C
SEQRES 2 E 23 U G G C A A C G C C
SEQRES 1 F 23 G G C G U U G C C G G U C
SEQRES 2 F 23 U G G C A A C G C C
SEQRES 1 G 23 G G C G U U G C C G G U C
SEQRES 2 G 23 U G G C A A C G C C
SEQRES 1 A 124 GLY SER GLU THR GLN LYS LYS LEU LEU LYS ASP LEU GLU
SEQRES 2 A 124 ASP LYS TYR ARG VAL SER ARG TRP GLN PRO PRO SER PHE
SEQRES 3 A 124 LYS GLU VAL ALA GLY SER PHE ASN LEU ASP PRO SER GLU
SEQRES 4 A 124 LEU GLU GLU LEU LEU HIS TYR LEU VAL ARG GLU GLY VAL
SEQRES 5 A 124 LEU VAL LYS ILE ASN ASP GLU PHE TYR TRP HIS ARG GLN
SEQRES 6 A 124 ALA LEU GLY GLU ALA ARG GLU VAL ILE LYS ASN LEU ALA
SEQRES 7 A 124 SER THR GLY PRO PHE GLY LEU ALA GLU ALA ARG ASP ALA
SEQRES 8 A 124 LEU GLY SER SER ARG LYS TYR VAL LEU PRO LEU LEU GLU
SEQRES 9 A 124 TYR LEU ASP GLN VAL LYS PHE THR ARG ARG VAL GLY ASP
SEQRES 10 A 124 LYS ARG VAL VAL VAL GLY ASN
SEQRES 1 B 124 GLY SER GLU THR GLN LYS LYS LEU LEU LYS ASP LEU GLU
SEQRES 2 B 124 ASP LYS TYR ARG VAL SER ARG TRP GLN PRO PRO SER PHE
SEQRES 3 B 124 LYS GLU VAL ALA GLY SER PHE ASN LEU ASP PRO SER GLU
SEQRES 4 B 124 LEU GLU GLU LEU LEU HIS TYR LEU VAL ARG GLU GLY VAL
SEQRES 5 B 124 LEU VAL LYS ILE ASN ASP GLU PHE TYR TRP HIS ARG GLN
SEQRES 6 B 124 ALA LEU GLY GLU ALA ARG GLU VAL ILE LYS ASN LEU ALA
SEQRES 7 B 124 SER THR GLY PRO PHE GLY LEU ALA GLU ALA ARG ASP ALA
SEQRES 8 B 124 LEU GLY SER SER ARG LYS TYR VAL LEU PRO LEU LEU GLU
SEQRES 9 B 124 TYR LEU ASP GLN VAL LYS PHE THR ARG ARG VAL GLY ASP
SEQRES 10 B 124 LYS ARG VAL VAL VAL GLY ASN
SEQRES 1 C 124 GLY SER GLU THR GLN LYS LYS LEU LEU LYS ASP LEU GLU
SEQRES 2 C 124 ASP LYS TYR ARG VAL SER ARG TRP GLN PRO PRO SER PHE
SEQRES 3 C 124 LYS GLU VAL ALA GLY SER PHE ASN LEU ASP PRO SER GLU
SEQRES 4 C 124 LEU GLU GLU LEU LEU HIS TYR LEU VAL ARG GLU GLY VAL
SEQRES 5 C 124 LEU VAL LYS ILE ASN ASP GLU PHE TYR TRP HIS ARG GLN
SEQRES 6 C 124 ALA LEU GLY GLU ALA ARG GLU VAL ILE LYS ASN LEU ALA
SEQRES 7 C 124 SER THR GLY PRO PHE GLY LEU ALA GLU ALA ARG ASP ALA
SEQRES 8 C 124 LEU GLY SER SER ARG LYS TYR VAL LEU PRO LEU LEU GLU
SEQRES 9 C 124 TYR LEU ASP GLN VAL LYS PHE THR ARG ARG VAL GLY ASP
SEQRES 10 C 124 LYS ARG VAL VAL VAL GLY ASN
SEQRES 1 D 124 GLY SER GLU THR GLN LYS LYS LEU LEU LYS ASP LEU GLU
SEQRES 2 D 124 ASP LYS TYR ARG VAL SER ARG TRP GLN PRO PRO SER PHE
SEQRES 3 D 124 LYS GLU VAL ALA GLY SER PHE ASN LEU ASP PRO SER GLU
SEQRES 4 D 124 LEU GLU GLU LEU LEU HIS TYR LEU VAL ARG GLU GLY VAL
SEQRES 5 D 124 LEU VAL LYS ILE ASN ASP GLU PHE TYR TRP HIS ARG GLN
SEQRES 6 D 124 ALA LEU GLY GLU ALA ARG GLU VAL ILE LYS ASN LEU ALA
SEQRES 7 D 124 SER THR GLY PRO PHE GLY LEU ALA GLU ALA ARG ASP ALA
SEQRES 8 D 124 LEU GLY SER SER ARG LYS TYR VAL LEU PRO LEU LEU GLU
SEQRES 9 D 124 TYR LEU ASP GLN VAL LYS PHE THR ARG ARG VAL GLY ASP
SEQRES 10 D 124 LYS ARG VAL VAL VAL GLY ASN
FORMUL 8 HOH *273(H2 O)
HELIX 1 1 THR A 514 ARG A 530 1 17
HELIX 2 2 SER A 535 ASN A 544 1 10
HELIX 3 3 ASP A 546 GLU A 560 1 15
HELIX 4 4 ARG A 574 ALA A 588 1 15
HELIX 5 5 SER A 589 GLY A 591 5 3
HELIX 6 6 GLY A 594 GLY A 603 1 10
HELIX 7 7 SER A 605 VAL A 619 1 15
HELIX 8 8 GLY B 511 ARG B 530 1 20
HELIX 9 9 SER B 535 ASN B 544 1 10
HELIX 10 10 ASP B 546 GLU B 560 1 15
HELIX 11 11 ARG B 574 SER B 589 1 16
HELIX 12 12 GLY B 594 GLY B 603 1 10
HELIX 13 13 SER B 605 VAL B 619 1 15
HELIX 14 14 LYS C 517 ARG C 530 1 14
HELIX 15 15 SER C 535 ALA C 540 1 6
HELIX 16 16 LEU C 553 GLU C 560 1 8
HELIX 17 17 ARG C 574 ALA C 588 1 15
HELIX 18 18 SER C 589 GLY C 591 5 3
HELIX 19 19 GLY C 594 GLY C 603 1 10
HELIX 20 20 SER C 605 VAL C 619 1 15
HELIX 21 21 SER D 512 LYS D 517 1 6
HELIX 22 22 LEU D 518 ARG D 530 1 13
HELIX 23 23 SER D 535 ASN D 544 1 10
HELIX 24 24 ASP D 546 GLU D 560 1 15
HELIX 25 25 ARG D 574 LEU D 587 1 14
HELIX 26 26 GLY D 594 LEU D 602 1 9
HELIX 27 27 SER D 605 VAL D 619 1 15
SHEET 1 A 2 LEU A 563 LYS A 565 0
SHEET 2 A 2 TYR A 571 HIS A 573 -1 O TRP A 572 N VAL A 564
SHEET 1 B 2 THR A 622 VAL A 625 0
SHEET 2 B 2 LYS A 628 VAL A 631 -1 O VAL A 630 N ARG A 623
SHEET 1 C 2 LEU B 563 LYS B 565 0
SHEET 2 C 2 TYR B 571 HIS B 573 -1 O TRP B 572 N VAL B 564
SHEET 1 D 2 THR B 622 VAL B 625 0
SHEET 2 D 2 LYS B 628 VAL B 631 -1 O LYS B 628 N VAL B 625
SHEET 1 E 2 LEU C 563 LYS C 565 0
SHEET 2 E 2 TYR C 571 HIS C 573 -1 O TRP C 572 N VAL C 564
SHEET 1 F 2 THR C 622 ARG C 623 0
SHEET 2 F 2 VAL C 630 VAL C 631 -1 O VAL C 630 N ARG C 623
SHEET 1 G 2 LEU D 563 LYS D 565 0
SHEET 2 G 2 TYR D 571 HIS D 573 -1 O TRP D 572 N VAL D 564
SHEET 1 H 2 THR D 622 ARG D 623 0
SHEET 2 H 2 VAL D 630 VAL D 631 -1 O VAL D 630 N ARG D 623
CRYST1 81.865 169.814 71.827 90.00 90.00 90.00 P 21 21 2 16
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 0.012215 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005889 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013922 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
