HEADER RNA BINDING PROTEIN/RNA 23-JUN-10 3NNH
TITLE CRYSTAL STRUCTURE OF THE CUGBP1 RRM1 WITH GUUGUUUUGUUU RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUGBP ELAV-LIKE FAMILY MEMBER 1;
COMPND 3 CHAIN: A, C, B, D;
COMPND 4 FRAGMENT: RRM1 DOMAIN (UNP RESIDUES 14-100);
COMPND 5 SYNONYM: CELF-1, CUG-BP- AND ETR-3-LIKE FACTOR 1, BRUNO-LIKE PROTEIN
COMPND 6 2, RNA-BINDING PROTEIN BRUNOL-2, CUG TRIPLET REPEAT RNA-BINDING
COMPND 7 PROTEIN 1, CUG-BP1, DEADENYLATION FACTOR CUG-BP, 50 KDA NUCLEAR
COMPND 8 POLYADENYLATED RNA-BINDING PROTEIN, EMBRYO DEADENYLATION ELEMENT-
COMPND 9 BINDING PROTEIN HOMOLOG, EDEN-BP HOMOLOG;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: RNA (5'-R(*GP*UP*UP*GP*UP*UP*UP*UP*GP*UP*UP*U)-3');
COMPND 13 CHAIN: E, F;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BRUNOL2, CELF1, CUGBP, CUGBP1, NAB50;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS RNA RECOGNITION MOTIF, PRE-MRNA SPLICING, RNA, RNA BINDING PROTEIN-
KEYWDS 2 RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TEPLOVA,J.SONG,H.GAW,A.TEPLOV,D.J.PATEL
REVDAT 3 06-SEP-23 3NNH 1 SEQADV
REVDAT 2 08-OCT-14 3NNH 1 AUTHOR VERSN
REVDAT 1 27-OCT-10 3NNH 0
JRNL AUTH M.TEPLOVA,J.SONG,H.Y.GAW,A.TEPLOV,D.J.PATEL
JRNL TITL STRUCTURAL INSIGHTS INTO RNA RECOGNITION BY THE
JRNL TITL 2 ALTERNATE-SPLICING REGULATOR CUG-BINDING PROTEIN 1.
JRNL REF STRUCTURE V. 18 1364 2010
JRNL REFN ISSN 0969-2126
JRNL PMID 20947024
JRNL DOI 10.1016/J.STR.2010.06.018
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.270
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 11775
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.810
REMARK 3 FREE R VALUE TEST SET COUNT : 1155
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 19.5961 - 5.4652 0.98 1445 154 0.2004 0.2770
REMARK 3 2 5.4652 - 4.3535 0.99 1376 163 0.1553 0.2068
REMARK 3 3 4.3535 - 3.8078 0.99 1364 135 0.1576 0.2428
REMARK 3 4 3.8078 - 3.4617 0.98 1327 140 0.1677 0.2744
REMARK 3 5 3.4617 - 3.2148 0.97 1357 136 0.1793 0.2560
REMARK 3 6 3.2148 - 3.0260 0.95 1279 137 0.1941 0.2651
REMARK 3 7 3.0260 - 2.8749 0.93 1239 146 0.2025 0.3408
REMARK 3 8 2.8749 - 2.7501 0.92 1233 144 0.2032 0.2965
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 : 0.35
REMARK 3 B_SOL : 17.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.51350
REMARK 3 B22 (A**2) : 0.58220
REMARK 3 B33 (A**2) : 0.92860
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3298
REMARK 3 ANGLE : 1.031 4544
REMARK 3 CHIRALITY : 0.062 501
REMARK 3 PLANARITY : 0.004 525
REMARK 3 DIHEDRAL : 20.751 1270
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NNH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000060047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-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 : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
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 : 12357
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.37600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
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 3NMR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM SODIUM TARTRATE, 20%
REMARK 280 PEG 3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 29.59000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.02600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.03700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.02600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.59000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.03700
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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, 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 SER A 13
REMARK 465 GLU A 100
REMARK 465 SER C 13
REMARK 465 SER C 99
REMARK 465 GLU C 100
REMARK 465 G E 1
REMARK 465 SER B 13
REMARK 465 GLU B 100
REMARK 465 SER D 13
REMARK 465 U F 12
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 U E 12 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 U E 12 C1' N1 C2 O2 N3 C4 O4
REMARK 470 U E 12 C5 C6
REMARK 470 G F 1 O5'
REMARK 470 U F 11 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 U F 11 C1' N1 C2 O2 N3 C4 O4
REMARK 470 U F 11 C5 C6
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 GLN A 22 35.15 74.60
REMARK 500 GLN D 22 49.25 70.23
REMARK 500 PRO D 56 109.24 -48.49
REMARK 500 HIS D 80 109.42 -56.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NMR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RRM1-RRM2 DOMAIN COMPLEXED WITH GUUGUUUUGUUU.
REMARK 900 RELATED ID: 3NNA RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RRM1-RRM2 DOMAIN COMPLEXED WITH GUUGUUUUUGUU.
REMARK 900 RELATED ID: 3NNC RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RRM1-RRM2 DOMAIN COMPLEXED WITH UGUGUGUUGUGUG.
DBREF 3NNH A 14 100 UNP Q92879 CELF1_HUMAN 14 100
DBREF 3NNH C 14 100 UNP Q92879 CELF1_HUMAN 14 100
DBREF 3NNH E 1 12 PDB 3NNH 3NNH 1 12
DBREF 3NNH B 14 100 UNP Q92879 CELF1_HUMAN 14 100
DBREF 3NNH D 14 100 UNP Q92879 CELF1_HUMAN 14 100
DBREF 3NNH F 1 12 PDB 3NNH 3NNH 1 12
SEQADV 3NNH SER A 13 UNP Q92879 EXPRESSION TAG
SEQADV 3NNH SER C 13 UNP Q92879 EXPRESSION TAG
SEQADV 3NNH SER B 13 UNP Q92879 EXPRESSION TAG
SEQADV 3NNH SER D 13 UNP Q92879 EXPRESSION TAG
SEQRES 1 A 88 SER ASP ALA ILE LYS MET PHE VAL GLY GLN VAL PRO ARG
SEQRES 2 A 88 THR TRP SER GLU LYS ASP LEU ARG GLU LEU PHE GLU GLN
SEQRES 3 A 88 TYR GLY ALA VAL TYR GLU ILE ASN VAL LEU ARG ASP ARG
SEQRES 4 A 88 SER GLN ASN PRO PRO GLN SER LYS GLY CYS CYS PHE VAL
SEQRES 5 A 88 THR PHE TYR THR ARG LYS ALA ALA LEU GLU ALA GLN ASN
SEQRES 6 A 88 ALA LEU HIS ASN MET LYS VAL LEU PRO GLY MET HIS HIS
SEQRES 7 A 88 PRO ILE GLN MET LYS PRO ALA ASP SER GLU
SEQRES 1 C 88 SER ASP ALA ILE LYS MET PHE VAL GLY GLN VAL PRO ARG
SEQRES 2 C 88 THR TRP SER GLU LYS ASP LEU ARG GLU LEU PHE GLU GLN
SEQRES 3 C 88 TYR GLY ALA VAL TYR GLU ILE ASN VAL LEU ARG ASP ARG
SEQRES 4 C 88 SER GLN ASN PRO PRO GLN SER LYS GLY CYS CYS PHE VAL
SEQRES 5 C 88 THR PHE TYR THR ARG LYS ALA ALA LEU GLU ALA GLN ASN
SEQRES 6 C 88 ALA LEU HIS ASN MET LYS VAL LEU PRO GLY MET HIS HIS
SEQRES 7 C 88 PRO ILE GLN MET LYS PRO ALA ASP SER GLU
SEQRES 1 E 12 G U U G U U U U G U U U
SEQRES 1 B 88 SER ASP ALA ILE LYS MET PHE VAL GLY GLN VAL PRO ARG
SEQRES 2 B 88 THR TRP SER GLU LYS ASP LEU ARG GLU LEU PHE GLU GLN
SEQRES 3 B 88 TYR GLY ALA VAL TYR GLU ILE ASN VAL LEU ARG ASP ARG
SEQRES 4 B 88 SER GLN ASN PRO PRO GLN SER LYS GLY CYS CYS PHE VAL
SEQRES 5 B 88 THR PHE TYR THR ARG LYS ALA ALA LEU GLU ALA GLN ASN
SEQRES 6 B 88 ALA LEU HIS ASN MET LYS VAL LEU PRO GLY MET HIS HIS
SEQRES 7 B 88 PRO ILE GLN MET LYS PRO ALA ASP SER GLU
SEQRES 1 D 88 SER ASP ALA ILE LYS MET PHE VAL GLY GLN VAL PRO ARG
SEQRES 2 D 88 THR TRP SER GLU LYS ASP LEU ARG GLU LEU PHE GLU GLN
SEQRES 3 D 88 TYR GLY ALA VAL TYR GLU ILE ASN VAL LEU ARG ASP ARG
SEQRES 4 D 88 SER GLN ASN PRO PRO GLN SER LYS GLY CYS CYS PHE VAL
SEQRES 5 D 88 THR PHE TYR THR ARG LYS ALA ALA LEU GLU ALA GLN ASN
SEQRES 6 D 88 ALA LEU HIS ASN MET LYS VAL LEU PRO GLY MET HIS HIS
SEQRES 7 D 88 PRO ILE GLN MET LYS PRO ALA ASP SER GLU
SEQRES 1 F 12 G U U G U U U U G U U U
FORMUL 7 HOH *29(H2 O)
HELIX 1 1 SER A 28 GLU A 37 1 10
HELIX 2 2 THR A 68 HIS A 80 1 13
HELIX 3 3 SER C 28 GLU C 37 1 10
HELIX 4 4 THR C 68 HIS C 80 1 13
HELIX 5 5 SER B 28 GLU B 37 1 10
HELIX 6 6 THR B 68 HIS B 80 1 13
HELIX 7 7 SER D 28 GLU D 37 1 10
HELIX 8 8 GLN D 38 GLY D 40 5 3
HELIX 9 9 THR D 68 HIS D 80 1 13
SHEET 1 A 4 VAL A 42 ASP A 50 0
SHEET 2 A 4 GLN A 57 PHE A 66 -1 O PHE A 63 N ASN A 46
SHEET 3 A 4 ILE A 16 GLY A 21 -1 N MET A 18 O VAL A 64
SHEET 4 A 4 GLN A 93 PRO A 96 -1 O LYS A 95 N PHE A 19
SHEET 1 B 4 VAL C 42 ASP C 50 0
SHEET 2 B 4 GLN C 57 PHE C 66 -1 O GLN C 57 N ASP C 50
SHEET 3 B 4 ILE C 16 GLY C 21 -1 N MET C 18 O VAL C 64
SHEET 4 B 4 GLN C 93 PRO C 96 -1 O LYS C 95 N PHE C 19
SHEET 1 C 4 VAL B 42 ASP B 50 0
SHEET 2 C 4 GLN B 57 PHE B 66 -1 O PHE B 63 N ASN B 46
SHEET 3 C 4 LYS B 17 GLY B 21 -1 N VAL B 20 O CYS B 62
SHEET 4 C 4 GLN B 93 PRO B 96 -1 O LYS B 95 N PHE B 19
SHEET 1 D 4 VAL D 42 ASP D 50 0
SHEET 2 D 4 GLN D 57 PHE D 66 -1 O PHE D 63 N ASN D 46
SHEET 3 D 4 LYS D 17 GLY D 21 -1 N MET D 18 O VAL D 64
SHEET 4 D 4 GLN D 93 PRO D 96 -1 O LYS D 95 N PHE D 19
CISPEP 1 ASN A 54 PRO A 55 0 -9.73
CISPEP 2 ASN C 54 PRO C 55 0 -1.81
CISPEP 3 ASN B 54 PRO B 55 0 -1.89
CISPEP 4 ASN D 54 PRO D 55 0 0.27
CRYST1 59.180 62.074 122.052 90.00 90.00 90.00 P 21 21 21 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 0.016898 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016110 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008193 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
