HEADER MRNA PROCESSING 13-JUL-98 4DCG
TITLE VACCINIA METHYLTRANSFERASE VP39 MUTANT D182A COMPLEXED WITH M7G AND S-
TITLE 2 ADENOSYLHOMOCYSTEINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VP39;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POLY(A) POLYMERASE REGULATORY SUBUNIT;
COMPND 5 EC: 2.7.7.19;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS;
SOURCE 3 ORGANISM_TAXID: 10245;
SOURCE 4 STRAIN: BL21 (DE3);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)
KEYWDS METHYLATED GUANOSINE, METHYLTRANSFERASE MUTANT D182A, RNA CAP ANALOG,
KEYWDS 2 POLY(A) POLYMERASE, VACCINIA, MRNA PROCESSING, TRANSCRIPTION,
KEYWDS 3 COMPLEX (TRANSFERASE-RNA CAP ANALOG)
EXPDTA X-RAY DIFFRACTION
AUTHOR G.HU,A.E.HODEL,P.D.GERSHON,F.A.QUIOCHO
REVDAT 6 28-FEB-24 4DCG 1 REMARK
REVDAT 5 03-NOV-21 4DCG 1 REMARK SEQADV
REVDAT 4 24-FEB-09 4DCG 1 VERSN
REVDAT 3 01-APR-03 4DCG 1 JRNL
REVDAT 2 27-OCT-00 4DCG 1 JRNL
REVDAT 1 22-JUL-99 4DCG 0
JRNL AUTH G.HU,P.D.GERSHON,A.E.HODEL,F.A.QUIOCHO
JRNL TITL MRNA CAP RECOGNITION: DOMINANT ROLE OF ENHANCED STACKING
JRNL TITL 2 INTERACTIONS BETWEEN METHYLATED BASES AND PROTEIN AROMATIC
JRNL TITL 3 SIDE CHAINS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 7149 1999
JRNL REFN ISSN 0027-8424
JRNL PMID 10377383
JRNL DOI 10.1073/PNAS.96.13.7149
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 31782
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2399
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 155
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) : 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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4DCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : GOBEL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SMART
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31782
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.20000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5
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 42.16700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.36750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 42.16700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.36750
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: MONOMERIC
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 LYS A 142
REMARK 465 ARG A 143
REMARK 465 GLY A 144
REMARK 465 GLY A 145
REMARK 465 ASN A 146
REMARK 465 GLU A 147
REMARK 465 THR A 298
REMARK 465 THR A 299
REMARK 465 SER A 300
REMARK 465 THR A 301
REMARK 465 GLU A 302
REMARK 465 LYS A 303
REMARK 465 VAL A 304
REMARK 465 SER A 305
REMARK 465 HIS A 306
REMARK 465 GLU A 307
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 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 SER A 141 OG
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 H LYS A 33 HE21 GLN A 37 1.31
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 H HIS A 98 O HOH A 531 4546 1.45
REMARK 500 HH22 ARG A 107 O ARG A 292 2556 1.47
REMARK 500 H2 HOH A 409 O HOH A 545 2556 1.47
REMARK 500 H1 HOH A 411 O HOH A 454 2556 1.49
REMARK 500 HH22 ARG A 76 O HOH A 410 2556 1.52
REMARK 500 H ALA A 31 O PRO A 277 4546 1.52
REMARK 500 HH TYR A 83 O HOH A 542 2556 1.54
REMARK 500 H LYS A 32 O HOH A 475 4546 1.56
REMARK 500 O HOH A 405 H1 HOH A 548 4546 1.58
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 ASP A 2 72.31 -100.83
REMARK 500 PRO A 130 40.10 -102.74
REMARK 500 ILE A 185 -61.56 -120.71
REMARK 500 ILE A 242 -63.18 -96.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG7 A 401
DBREF 4DCG A 1 307 UNP P07617 PAP2_VACCV 1 307
SEQADV 4DCG ALA A 182 UNP P07617 ASP 182 ENGINEERED MUTATION
SEQRES 1 A 307 MET ASP VAL VAL SER LEU ASP LYS PRO PHE MET TYR PHE
SEQRES 2 A 307 GLU GLU ILE ASP ASN GLU LEU ASP TYR GLU PRO GLU SER
SEQRES 3 A 307 ALA ASN GLU VAL ALA LYS LYS LEU PRO TYR GLN GLY GLN
SEQRES 4 A 307 LEU LYS LEU LEU LEU GLY GLU LEU PHE PHE LEU SER LYS
SEQRES 5 A 307 LEU GLN ARG HIS GLY ILE LEU ASP GLY ALA THR VAL VAL
SEQRES 6 A 307 TYR ILE GLY SER ALA PRO GLY THR HIS ILE ARG TYR LEU
SEQRES 7 A 307 ARG ASP HIS PHE TYR ASN LEU GLY VAL ILE ILE LYS TRP
SEQRES 8 A 307 MET LEU ILE ASP GLY ARG HIS HIS ASP PRO ILE LEU ASN
SEQRES 9 A 307 GLY LEU ARG ASP VAL THR LEU VAL THR ARG PHE VAL ASP
SEQRES 10 A 307 GLU GLU TYR LEU ARG SER ILE LYS LYS GLN LEU HIS PRO
SEQRES 11 A 307 SER LYS ILE ILE LEU ILE SER ASP VAL ARG SER LYS ARG
SEQRES 12 A 307 GLY GLY ASN GLU PRO SER THR ALA ASP LEU LEU SER ASN
SEQRES 13 A 307 TYR ALA LEU GLN ASN VAL MET ILE SER ILE LEU ASN PRO
SEQRES 14 A 307 VAL ALA SER SER LEU LYS TRP ARG CYS PRO PHE PRO ALA
SEQRES 15 A 307 GLN TRP ILE LYS ASP PHE TYR ILE PRO HIS GLY ASN LYS
SEQRES 16 A 307 MET LEU GLN PRO PHE ALA PRO SER TYR SER ALA GLU MET
SEQRES 17 A 307 ARG LEU LEU SER ILE TYR THR GLY GLU ASN MET ARG LEU
SEQRES 18 A 307 THR ARG VAL THR LYS SER ASP ALA VAL ASN TYR GLU LYS
SEQRES 19 A 307 LYS MET TYR TYR LEU ASN LYS ILE VAL ARG ASN LYS VAL
SEQRES 20 A 307 VAL VAL ASN PHE ASP TYR PRO ASN GLN GLU TYR ASP TYR
SEQRES 21 A 307 PHE HIS MET TYR PHE MET LEU ARG THR VAL TYR CYS ASN
SEQRES 22 A 307 LYS THR PHE PRO THR THR LYS ALA LYS VAL LEU PHE LEU
SEQRES 23 A 307 GLN GLN SER ILE PHE ARG PHE LEU ASN ILE PRO THR THR
SEQRES 24 A 307 SER THR GLU LYS VAL SER HIS GLU
HET SAH A 400 30
HET MG7 A 401 21
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM MG7 7-METHYLGUANOSINE
FORMUL 2 SAH C14 H20 N6 O5 S
FORMUL 3 MG7 C11 H16 N5 O5 1+
FORMUL 4 HOH *155(H2 O)
HELIX 1 1 PHE A 13 GLU A 15 5 3
HELIX 2 2 PRO A 24 ASN A 28 5 5
HELIX 3 3 GLN A 37 ARG A 55 1 19
HELIX 4 4 THR A 73 LEU A 85 1 13
HELIX 5 5 PRO A 101 LEU A 103 5 3
HELIX 6 6 GLU A 118 LEU A 128 1 11
HELIX 7 7 THR A 150 LEU A 167 1 18
HELIX 8 8 PRO A 181 GLN A 183 5 3
HELIX 9 9 LYS A 226 LYS A 241 1 16
HELIX 10 10 TYR A 258 THR A 269 1 12
HELIX 11 11 THR A 279 LEU A 294 1 16
SHEET 1 A 7 ASN A 194 MET A 196 0
SHEET 2 A 7 MET A 208 ILE A 213 -1 N LEU A 211 O ASN A 194
SHEET 3 A 7 ALA A 171 TRP A 176 -1 N TRP A 176 O MET A 208
SHEET 4 A 7 ILE A 133 SER A 137 1 N LEU A 135 O ALA A 171
SHEET 5 A 7 THR A 63 ILE A 67 1 N THR A 63 O ILE A 134
SHEET 6 A 7 LYS A 90 ASP A 95 1 N LYS A 90 O VAL A 64
SHEET 7 A 7 VAL A 109 THR A 113 1 N THR A 110 O TRP A 91
SHEET 1 B 2 PHE A 188 PRO A 191 0
SHEET 2 B 2 LEU A 221 VAL A 224 -1 N VAL A 224 O PHE A 188
CISPEP 1 ALA A 70 PRO A 71 0 0.16
CISPEP 2 HIS A 129 PRO A 130 0 0.45
SITE 1 AC1 18 GLN A 39 LEU A 42 TYR A 66 ILE A 67
SITE 2 AC1 18 GLY A 68 SER A 69 ALA A 70 PRO A 71
SITE 3 AC1 18 GLY A 72 HIS A 74 ASP A 95 ARG A 97
SITE 4 AC1 18 PHE A 115 VAL A 116 ASP A 138 VAL A 139
SITE 5 AC1 18 ARG A 140 HOH A 493
SITE 1 AC2 8 TYR A 22 PRO A 24 ALA A 27 PHE A 180
SITE 2 AC2 8 TYR A 204 GLU A 233 HOH A 414 HOH A 488
CRYST1 84.334 66.735 79.392 90.00 117.21 90.00 C 1 2 1 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 0.011858 0.000000 0.006097 0.00000
SCALE2 0.000000 0.014985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
