HEADER TRANSCRIPTION 11-NOV-13 4CEK
TITLE CRYSTAL STRUCTURE OF THE SECOND MIF4G DOMAIN OF HUMAN
TITLE 2 NONSENSE MEDIATED DECAY FACTOR UPF2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATOR OF NONSENSE TRANSCRIPTS 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MIF4G2, RESIDUES 455-757;
COMPND 5 SYNONYM: NONSENSE MRNA REDUCING FACTOR 2, UP-FRAMESHIFT SUPPRESSOR
COMPND 6 2 HOMOLOG, HUPF2, UPF2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PPROEXHTB
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CLERICI,A.DENIAUD,V.BOEHM,N.H.GEHRING,C.SCHAFFITZEL,S.CUSACK
REVDAT 2 12-MAR-14 4CEK 1 JRNL
REVDAT 1 11-DEC-13 4CEK 0
JRNL AUTH M.CLERICI,A.DENIAUD,V.BOEHM,N.H.GEHRING,C.SCHAFFITZEL,
JRNL AUTH 2 S.CUSACK
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE THREE MIF4G
JRNL TITL 2 DOMAINS OF NONSENSE-MEDIATED DECAY FACTOR UPF2.
JRNL REF NUCLEIC ACIDS RES. V. 42 2673 2014
JRNL REFN ISSN 0305-1048
JRNL PMID 24271394
JRNL DOI 10.1093/NAR/GKT1197
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0116
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.66
REMARK 3 NUMBER OF REFLECTIONS : 13638
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.20850
REMARK 3 R VALUE (WORKING SET) : 0.20623
REMARK 3 FREE R VALUE : 0.25083
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 723
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.350
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.411
REMARK 3 REFLECTION IN BIN (WORKING SET) : 885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.286
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.348
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1958
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.713
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.09
REMARK 3 B22 (A**2) : -1.30
REMARK 3 B33 (A**2) : -0.78
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.292
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.229
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.177
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.504
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1991 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1394 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2672 ; 1.462 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3385 ; 0.929 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 235 ; 6.151 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;35.692 ;23.542
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 384 ;17.941 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.295 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 302 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2142 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 410 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4CEK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-13.
REMARK 100 THE PDBE ID CODE IS EBI-58936.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MX-225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14361
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.35
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.95
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.09
REMARK 200 R MERGE FOR SHELL (I) : 0.81
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.1
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 19% PEG 3350
REMARK 280 AND AT A PROTEIN CONCENTRATION OF 8 MG/ML
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 20.44000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.11000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.11000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.44000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.30000
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 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 GLY A 451
REMARK 465 ALA A 452
REMARK 465 MET A 453
REMARK 465 GLY A 454
REMARK 465 GLU A 455
REMARK 465 GLY A 456
REMARK 465 ILE A 480A
REMARK 465 LEU A 480B
REMARK 465 PHE A 481
REMARK 465 LYS A 482
REMARK 465 ASP A 483
REMARK 465 ASN A 484
REMARK 465 GLU A 485
REMARK 465 LYS A 486
REMARK 465 SER A 487
REMARK 465 CYS A 488
REMARK 465 GLN A 489
REMARK 465 ASN A 490
REMARK 465 LYS A 491
REMARK 465 GLU A 492
REMARK 465 SER A 493
REMARK 465 ASN A 494
REMARK 465 LYS A 495
REMARK 465 ASP A 496
REMARK 465 ASP A 497
REMARK 465 THR A 498
REMARK 465 LYS A 499
REMARK 465 GLU A 500
REMARK 465 ALA A 501
REMARK 465 LYS A 502
REMARK 465 GLU A 503
REMARK 465 SER A 504
REMARK 465 LYS A 505
REMARK 465 GLU A 506
REMARK 465 ASN A 507
REMARK 465 LYS A 508
REMARK 465 GLU A 509
REMARK 465 VAL A 510
REMARK 465 SER A 511
REMARK 465 SER A 512
REMARK 465 PRO A 513
REMARK 465 ASP A 514
REMARK 465 ASP A 515
REMARK 465 LEU A 516
REMARK 465 GLU A 517
REMARK 465 LEU A 518
REMARK 465 GLU A 519
REMARK 465 LEU A 520
REMARK 465 GLU A 521
REMARK 465 ASN A 522
REMARK 465 LEU A 523
REMARK 465 GLU A 524
REMARK 465 ILE A 525
REMARK 465 ASN A 526
REMARK 465 ASP A 527
REMARK 465 ASP A 528
REMARK 465 GLU A 533
REMARK 465 GLY A 533A
REMARK 465 GLU A 549
REMARK 465 GLN A 550
REMARK 465 GLU A 551
REMARK 465 ASP A 552
REMARK 465 GLU A 553
REMARK 465 GLU A 554
REMARK 465 ALA A 555
REMARK 465 ASP A 656
REMARK 465 GLN A 657
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 PRO A 479 99.28 -64.73
REMARK 500 GLU A 547 87.70 -67.19
REMARK 500 THR A 597 125.85 -173.28
REMARK 500 VAL A 611 129.24 -39.32
REMARK 500 MET A 633 68.72 -162.62
REMARK 500 HIS A 739 70.07 35.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CEM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST MIF4G DOMAIN OF HUMAN
REMARK 900 NONSENSE MEDIATED DECAY FACTOR UPF2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL GAMG LEFT AFTER HIS-TAG CLEAVAGE
DBREF 4CEK A 455 757 UNP Q9HAU5 RENT2_HUMAN 455 757
SEQADV 4CEK GLY A 451 UNP Q9HAU5 EXPRESSION TAG
SEQADV 4CEK ALA A 452 UNP Q9HAU5 EXPRESSION TAG
SEQADV 4CEK MET A 453 UNP Q9HAU5 EXPRESSION TAG
SEQADV 4CEK GLY A 454 UNP Q9HAU5 EXPRESSION TAG
SEQRES 1 A 307 GLY ALA MET GLY GLU GLY GLY ILE TRP GLU ASP GLU ASP
SEQRES 2 A 307 ALA ARG ASN PHE TYR GLU ASN LEU ILE ASP LEU LYS ALA
SEQRES 3 A 307 PHE VAL PRO ALA ILE LEU PHE LYS ASP ASN GLU LYS SER
SEQRES 4 A 307 CYS GLN ASN LYS GLU SER ASN LYS ASP ASP THR LYS GLU
SEQRES 5 A 307 ALA LYS GLU SER LYS GLU ASN LYS GLU VAL SER SER PRO
SEQRES 6 A 307 ASP ASP LEU GLU LEU GLU LEU GLU ASN LEU GLU ILE ASN
SEQRES 7 A 307 ASP ASP THR LEU GLU LEU GLU GLY GLY ASP GLU ALA GLU
SEQRES 8 A 307 ASP LEU THR LYS LYS LEU LEU ASP GLU GLN GLU GLN GLU
SEQRES 9 A 307 ASP GLU GLU ALA SER THR GLY SER HIS LEU LYS LEU ILE
SEQRES 10 A 307 VAL ASP ALA PHE LEU GLN GLN LEU PRO ASN CYS VAL ASN
SEQRES 11 A 307 ARG ASP LEU ILE ASP LYS ALA ALA MET ASP PHE CYS MET
SEQRES 12 A 307 ASN MET ASN THR LYS ALA ASN ARG LYS LYS LEU VAL ARG
SEQRES 13 A 307 ALA LEU PHE ILE VAL PRO ARG GLN ARG LEU ASP LEU LEU
SEQRES 14 A 307 PRO PHE TYR ALA ARG LEU VAL ALA THR LEU HIS PRO CYS
SEQRES 15 A 307 MET SER ASP VAL ALA GLU ASP LEU CYS SER MET LEU ARG
SEQRES 16 A 307 GLY ASP PHE ARG PHE HIS VAL ARG LYS LYS ASP GLN ILE
SEQRES 17 A 307 ASN ILE GLU THR LYS ASN LYS THR VAL ARG PHE ILE GLY
SEQRES 18 A 307 GLU LEU THR LYS PHE LYS MET PHE THR LYS ASN ASP THR
SEQRES 19 A 307 LEU HIS CYS LEU LYS MET LEU LEU SER ASP PHE SER HIS
SEQRES 20 A 307 HIS HIS ILE GLU MET ALA CYS THR LEU LEU GLU THR CYS
SEQRES 21 A 307 GLY ARG PHE LEU PHE ARG SER PRO GLU SER HIS LEU ARG
SEQRES 22 A 307 THR SER VAL LEU LEU GLU GLN MET MET ARG LYS LYS GLN
SEQRES 23 A 307 ALA MET HIS LEU ASP ALA ARG TYR VAL THR MET VAL GLU
SEQRES 24 A 307 ASN ALA TYR TYR TYR CYS ASN PRO
FORMUL 2 HOH *32(H2 O)
HELIX 1 1 GLU A 462 ASN A 470 1 9
HELIX 2 2 ASP A 473 PHE A 477 5 5
HELIX 3 3 ASP A 535 GLU A 547 1 13
HELIX 4 4 SER A 559 LEU A 575 1 17
HELIX 5 5 PRO A 576 CYS A 578 5 3
HELIX 6 6 ASN A 580 MET A 595 1 16
HELIX 7 7 THR A 597 ILE A 610 1 14
HELIX 8 8 PRO A 612 ASP A 617 5 6
HELIX 9 9 LEU A 618 HIS A 630 1 13
HELIX 10 10 SER A 634 LYS A 654 1 21
HELIX 11 11 ASN A 659 PHE A 676 1 18
HELIX 12 12 THR A 680 ASP A 694 1 15
HELIX 13 13 SER A 696 MET A 738 1 43
HELIX 14 14 ASP A 741 ASN A 756 1 16
CRYST1 40.880 56.600 142.220 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 0.024462 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007031 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
