HEADER RNA BINDING PROTEIN 14-FEB-18 6FQR
TITLE CRYSTAL STRUCTURE OF IMP3 RRM12 IN COMPLEX WITH RNA (CCCC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 2 MRNA-BINDING PROTEIN 3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IMP-3,IGF-II MRNA-BINDING PROTEIN 3,KH DOMAIN-CONTAINING
COMPND 5 PROTEIN OVEREXPRESSED IN CANCER,HKOC,VICKZ FAMILY MEMBER 3;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: N-TERMINAL LEFT RESIDUES (GGS) DUE TO TEV CLEAVAGE AND
COMPND 8 C-TERMINAL HIS6 TAG;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RNA CCCC;
COMPND 11 CHAIN: C;
COMPND 12 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: IGF2BP3, IMP3, KOC1, VICKZ3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS RNA RECOGNITION MOTIF (RRM), IMP3, IGF2BP3, CRYSTAL STRUCTURE., RNA
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.JIA,H.GUT,A.J.CHAO
REVDAT 3 17-JAN-24 6FQR 1 REMARK
REVDAT 2 28-NOV-18 6FQR 1 JRNL
REVDAT 1 05-SEP-18 6FQR 0
JRNL AUTH M.JIA,H.GUT,J.A.CHAO
JRNL TITL STRUCTURAL BASIS OF IMP3 RRM12 RECOGNITION OF RNA.
JRNL REF RNA V. 24 1659 2018
JRNL REFN ESSN 1469-9001
JRNL PMID 30135093
JRNL DOI 10.1261/RNA.065649.118
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 17881
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 893
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 38.8293 - 3.8151 0.96 2853 150 0.1483 0.1781
REMARK 3 2 3.8151 - 3.0285 0.96 2835 149 0.1473 0.2318
REMARK 3 3 3.0285 - 2.6458 0.96 2870 151 0.1703 0.2438
REMARK 3 4 2.6458 - 2.4039 0.96 2858 149 0.1847 0.2709
REMARK 3 5 2.4039 - 2.2317 0.95 2794 148 0.2044 0.2781
REMARK 3 6 2.2317 - 2.1001 0.94 2778 146 0.2365 0.3165
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2647
REMARK 3 ANGLE : 0.796 3603
REMARK 3 CHIRALITY : 0.052 411
REMARK 3 PLANARITY : 0.006 460
REMARK 3 DIHEDRAL : 12.352 1623
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 6FQR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008768.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-15
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17886
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 95.3
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.54100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER CCP4 7.0.050
REMARK 200 STARTING MODEL: 2E44
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS PH 6.2, 0.2 M MGCL2,
REMARK 280 25% PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -2
REMARK 465 GLY A -1
REMARK 465 MET A 158
REMARK 465 ALA A 159
REMARK 465 ALA A 160
REMARK 465 GLN A 161
REMARK 465 HIS A 162
REMARK 465 HIS A 163
REMARK 465 HIS A 164
REMARK 465 HIS A 165
REMARK 465 HIS A 166
REMARK 465 HIS A 167
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 160
REMARK 465 GLN B 161
REMARK 465 HIS B 162
REMARK 465 HIS B 163
REMARK 465 HIS B 164
REMARK 465 HIS B 165
REMARK 465 HIS B 166
REMARK 465 HIS B 167
REMARK 465 C C 4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 327 O HOH A 341 2.16
REMARK 500 O HOH B 277 O HOH B 299 2.16
REMARK 500 O HOH A 242 O HOH A 289 2.18
REMARK 500 OG SER A 128 O HOH A 201 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 328 O HOH A 330 1655 2.14
REMARK 500 O HOH B 211 O HOH B 297 1455 2.17
REMARK 500 O PRO B 90 NH2 ARG B 133 1455 2.17
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 LYS A 36 -142.32 -106.41
REMARK 500 ILE A 80 -86.96 -124.70
REMARK 500 LYS B 36 -131.35 -98.02
REMARK 500 ILE B 80 -95.95 -132.22
REMARK 500 ASP B 156 74.80 -108.22
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 B 329 DISTANCE = 6.42 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FQ1 RELATED DB: PDB
REMARK 900 IMP3 RRM12
DBREF 6FQR A 1 161 UNP O00425 IF2B3_HUMAN 1 161
DBREF 6FQR B 1 161 UNP O00425 IF2B3_HUMAN 1 161
DBREF 6FQR C 1 4 PDB 6FQR 6FQR 1 4
SEQADV 6FQR GLY A -2 UNP O00425 EXPRESSION TAG
SEQADV 6FQR GLY A -1 UNP O00425 EXPRESSION TAG
SEQADV 6FQR SER A 0 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS A 162 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS A 163 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS A 164 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS A 165 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS A 166 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS A 167 UNP O00425 EXPRESSION TAG
SEQADV 6FQR GLY B -2 UNP O00425 EXPRESSION TAG
SEQADV 6FQR GLY B -1 UNP O00425 EXPRESSION TAG
SEQADV 6FQR SER B 0 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS B 162 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS B 163 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS B 164 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS B 165 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS B 166 UNP O00425 EXPRESSION TAG
SEQADV 6FQR HIS B 167 UNP O00425 EXPRESSION TAG
SEQRES 1 A 170 GLY GLY SER MET ASN LYS LEU TYR ILE GLY ASN LEU SER
SEQRES 2 A 170 GLU ASN ALA ALA PRO SER ASP LEU GLU SER ILE PHE LYS
SEQRES 3 A 170 ASP ALA LYS ILE PRO VAL SER GLY PRO PHE LEU VAL LYS
SEQRES 4 A 170 THR GLY TYR ALA PHE VAL ASP CYS PRO ASP GLU SER TRP
SEQRES 5 A 170 ALA LEU LYS ALA ILE GLU ALA LEU SER GLY LYS ILE GLU
SEQRES 6 A 170 LEU HIS GLY LYS PRO ILE GLU VAL GLU HIS SER VAL PRO
SEQRES 7 A 170 LYS ARG GLN ARG ILE ARG LYS LEU GLN ILE ARG ASN ILE
SEQRES 8 A 170 PRO PRO HIS LEU GLN TRP GLU VAL LEU ASP SER LEU LEU
SEQRES 9 A 170 VAL GLN TYR GLY VAL VAL GLU SER CYS GLU GLN VAL ASN
SEQRES 10 A 170 THR ASP SER GLU THR ALA VAL VAL ASN VAL THR TYR SER
SEQRES 11 A 170 SER LYS ASP GLN ALA ARG GLN ALA LEU ASP LYS LEU ASN
SEQRES 12 A 170 GLY PHE GLN LEU GLU ASN PHE THR LEU LYS VAL ALA TYR
SEQRES 13 A 170 ILE PRO ASP GLU MET ALA ALA GLN HIS HIS HIS HIS HIS
SEQRES 14 A 170 HIS
SEQRES 1 B 170 GLY GLY SER MET ASN LYS LEU TYR ILE GLY ASN LEU SER
SEQRES 2 B 170 GLU ASN ALA ALA PRO SER ASP LEU GLU SER ILE PHE LYS
SEQRES 3 B 170 ASP ALA LYS ILE PRO VAL SER GLY PRO PHE LEU VAL LYS
SEQRES 4 B 170 THR GLY TYR ALA PHE VAL ASP CYS PRO ASP GLU SER TRP
SEQRES 5 B 170 ALA LEU LYS ALA ILE GLU ALA LEU SER GLY LYS ILE GLU
SEQRES 6 B 170 LEU HIS GLY LYS PRO ILE GLU VAL GLU HIS SER VAL PRO
SEQRES 7 B 170 LYS ARG GLN ARG ILE ARG LYS LEU GLN ILE ARG ASN ILE
SEQRES 8 B 170 PRO PRO HIS LEU GLN TRP GLU VAL LEU ASP SER LEU LEU
SEQRES 9 B 170 VAL GLN TYR GLY VAL VAL GLU SER CYS GLU GLN VAL ASN
SEQRES 10 B 170 THR ASP SER GLU THR ALA VAL VAL ASN VAL THR TYR SER
SEQRES 11 B 170 SER LYS ASP GLN ALA ARG GLN ALA LEU ASP LYS LEU ASN
SEQRES 12 B 170 GLY PHE GLN LEU GLU ASN PHE THR LEU LYS VAL ALA TYR
SEQRES 13 B 170 ILE PRO ASP GLU MET ALA ALA GLN HIS HIS HIS HIS HIS
SEQRES 14 B 170 HIS
SEQRES 1 C 4 C C C C
FORMUL 4 HOH *298(H2 O)
HELIX 1 AA1 ALA A 14 ALA A 25 1 12
HELIX 2 AA2 ASP A 46 SER A 58 1 13
HELIX 3 AA3 PRO A 75 ARG A 79 5 5
HELIX 4 AA4 GLN A 93 VAL A 102 1 10
HELIX 5 AA5 SER A 128 ASN A 140 1 13
HELIX 6 AA6 ALA B 14 ALA B 25 1 12
HELIX 7 AA7 ASP B 46 SER B 58 1 13
HELIX 8 AA8 PRO B 75 ARG B 79 5 5
HELIX 9 AA9 GLN B 93 VAL B 102 1 10
HELIX 10 AB1 SER B 128 ASN B 140 1 13
SHEET 1 AA1 4 LEU A 34 VAL A 35 0
SHEET 2 AA1 4 ALA A 40 ASP A 43 -1 O PHE A 41 N LEU A 34
SHEET 3 AA1 4 LYS A 3 GLY A 7 -1 N LEU A 4 O VAL A 42
SHEET 4 AA1 4 GLU A 69 HIS A 72 -1 O GLU A 71 N TYR A 5
SHEET 1 AA2 2 GLU A 62 LEU A 63 0
SHEET 2 AA2 2 LYS A 66 PRO A 67 -1 O LYS A 66 N LEU A 63
SHEET 1 AA3 4 VAL A 107 VAL A 113 0
SHEET 2 AA3 4 ALA A 120 TYR A 126 -1 O VAL A 121 N VAL A 113
SHEET 3 AA3 4 LYS A 82 ILE A 88 -1 N LEU A 83 O VAL A 124
SHEET 4 AA3 4 LYS A 150 TYR A 153 -1 O LYS A 150 N ARG A 86
SHEET 1 AA4 2 GLN A 143 LEU A 144 0
SHEET 2 AA4 2 PHE A 147 THR A 148 -1 O PHE A 147 N LEU A 144
SHEET 1 AA5 4 LEU B 34 VAL B 35 0
SHEET 2 AA5 4 TYR B 39 ASP B 43 -1 O PHE B 41 N LEU B 34
SHEET 3 AA5 4 LYS B 3 GLY B 7 -1 N LEU B 4 O VAL B 42
SHEET 4 AA5 4 GLU B 69 HIS B 72 -1 O GLU B 71 N TYR B 5
SHEET 1 AA6 2 GLU B 62 LEU B 63 0
SHEET 2 AA6 2 LYS B 66 PRO B 67 -1 O LYS B 66 N LEU B 63
SHEET 1 AA7 4 VAL B 107 GLN B 112 0
SHEET 2 AA7 4 ALA B 120 TYR B 126 -1 O THR B 125 N SER B 109
SHEET 3 AA7 4 LYS B 82 ILE B 88 -1 N LEU B 83 O VAL B 124
SHEET 4 AA7 4 LYS B 150 TYR B 153 -1 O LYS B 150 N ARG B 86
SHEET 1 AA8 2 GLN B 143 LEU B 144 0
SHEET 2 AA8 2 PHE B 147 THR B 148 -1 O PHE B 147 N LEU B 144
CRYST1 30.060 41.190 72.270 92.14 100.40 108.65 P 1 2
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 0.033267 0.011230 0.007290 0.00000
SCALE2 0.000000 0.025624 0.002627 0.00000
SCALE3 0.000000 0.000000 0.014142 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
