HEADER DNA BINDING PROTEIN 23-JUL-12 4G94
TITLE G1 ORF67 / STAPHYLOCCUS AUREUS SIGMAA DOMAIN 4 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA POLYMERASE SIGMA FACTOR RPOD;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ORF067;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;
SOURCE 3 ORGANISM_TAXID: 93061;
SOURCE 4 STRAIN: NCTC 8325;
SOURCE 5 GENE: PLAC, RPOD, SAOUHSC_01662, SIGA, SIGMAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS PHAGE G1;
SOURCE 10 ORGANISM_TAXID: 292029;
SOURCE 11 GENE: ORF67;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RNA POLYMERASE BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.A.DARST,J.S.OSMUNDSON,C.M.MONTERO-DIAZ,A.HOCHSCHILD
REVDAT 2 28-FEB-24 4G94 1 SEQADV
REVDAT 1 23-JAN-13 4G94 0
JRNL AUTH J.OSMUNDSON,C.MONTERO-DIEZ,L.F.WESTBLADE,A.HOCHSCHILD,
JRNL AUTH 2 S.A.DARST
JRNL TITL PROMOTER-SPECIFIC TRANSCRIPTION INHIBITION IN STAPHYLOCOCCUS
JRNL TITL 2 AUREUS BY A PHAGE PROTEIN.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 151 1005 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 23178120
JRNL DOI 10.1016/J.CELL.2012.10.034
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 18678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 935
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 26.3524 - 3.8169 0.90 2475 131 0.1804 0.2051
REMARK 3 2 3.8169 - 3.0310 1.00 2609 137 0.1928 0.2431
REMARK 3 3 3.0310 - 2.6483 1.00 2572 136 0.2112 0.2426
REMARK 3 4 2.6483 - 2.4063 1.00 2531 133 0.2241 0.2996
REMARK 3 5 2.4063 - 2.2340 0.99 2551 135 0.2385 0.2586
REMARK 3 6 2.2340 - 2.1023 0.99 2524 133 0.2746 0.3076
REMARK 3 7 2.1023 - 1.9971 0.98 2481 130 0.3322 0.3846
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.120
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 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 : 0.011 2130
REMARK 3 ANGLE : 1.431 2881
REMARK 3 CHIRALITY : 0.106 329
REMARK 3 PLANARITY : 0.007 373
REMARK 3 DIHEDRAL : 14.906 812
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND RESSEQ 92:198
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1898 -11.1416 14.7924
REMARK 3 T TENSOR
REMARK 3 T11: 0.4204 T22: 0.3242
REMARK 3 T33: 0.5440 T12: 0.0136
REMARK 3 T13: -0.0724 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 2.8767 L22: 5.4423
REMARK 3 L33: 3.2963 L12: -0.0810
REMARK 3 L13: 0.5392 L23: 0.6109
REMARK 3 S TENSOR
REMARK 3 S11: 0.1004 S12: 0.0011 S13: -0.4375
REMARK 3 S21: -0.0959 S22: 0.2118 S23: -0.9005
REMARK 3 S31: 0.7016 S32: 0.1125 S33: -0.2907
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND RESSEQ 1:91
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3051 6.7495 27.1013
REMARK 3 T TENSOR
REMARK 3 T11: 0.4814 T22: 0.4426
REMARK 3 T33: 0.4719 T12: -0.0347
REMARK 3 T13: 0.0318 T23: -0.1365
REMARK 3 L TENSOR
REMARK 3 L11: 2.9488 L22: 7.3490
REMARK 3 L33: 5.8790 L12: -1.4534
REMARK 3 L13: -0.5170 L23: 1.3844
REMARK 3 S TENSOR
REMARK 3 S11: -0.1021 S12: -0.4062 S13: 0.5474
REMARK 3 S21: 1.2323 S22: 0.0300 S23: 0.4663
REMARK 3 S31: -0.2377 S32: -0.3929 S33: 0.0224
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND RESSEQ 296:357
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1447 -1.4046 6.9925
REMARK 3 T TENSOR
REMARK 3 T11: 0.4998 T22: 0.5013
REMARK 3 T33: 0.4169 T12: -0.0314
REMARK 3 T13: -0.0929 T23: -0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 0.9814 L22: 2.1533
REMARK 3 L33: 4.4420 L12: -0.6070
REMARK 3 L13: 0.0203 L23: -2.2465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.4738 S13: -0.0594
REMARK 3 S21: -0.7918 S22: -0.0707 S23: 0.3517
REMARK 3 S31: 0.0909 S32: -0.3695 S33: 0.0203
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 4G94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000073893.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 70
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .97918
REMARK 200 MONOCHROMATOR : SI(111)
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 : 18679
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.997
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.750
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 12% 1-PROPANOL, 10%
REMARK 280 PEG5000 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 19.19050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.36050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.36200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.36050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.19050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.36200
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 MET A 296 CG SD CE
REMARK 470 LYS A 297 CG CD CE NZ
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 GLN A 299 CG CD OE1 NE2
REMARK 470 GLU A 301 CG CD OE1 OE2
REMARK 470 ASP A 302 CG OD1 OD2
REMARK 470 ARG A 352 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 356 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 8 CG CD CE NZ
REMARK 470 ARG B 49 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 148 CG CD CE NZ
REMARK 470 GLU B 151 CG CD OE1 OE2
REMARK 470 GLU B 152 CG CD OE1 OE2
REMARK 470 ARG B 154 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 170 CG CD CE NZ
REMARK 470 ASP B 173 CG OD1 OD2
REMARK 470 LYS B 198 CG CD CE NZ
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 GLU B 146 OG1 THR B 149 2.04
REMARK 500 O HOH B 238 O HOH B 240 2.17
REMARK 500 NZ LYS B 159 OE1 GLU B 167 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY B 147 N - CA - C ANGL. DEV. = 15.0 DEGREES
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 ASN B 19 -120.47 50.84
REMARK 500 TRP B 36 -52.90 -134.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G8X RELATED DB: PDB
DBREF 4G94 A 296 357 UNP P0A0J0 RPOD_STAA8 296 357
DBREF 4G94 B 1 198 UNP Q4Z9Y5 Q4Z9Y5_9CAUD 1 198
SEQADV 4G94 MET A 296 UNP P0A0J0 LEU 296 CONFLICT
SEQRES 1 A 62 MET LYS GLU GLN LEU GLU ASP VAL LEU ASP THR LEU THR
SEQRES 2 A 62 ASP ARG GLU GLU ASN VAL LEU ARG LEU ARG PHE GLY LEU
SEQRES 3 A 62 ASP ASP GLY ARG THR ARG THR LEU GLU GLU VAL GLY LYS
SEQRES 4 A 62 VAL PHE GLY VAL THR ARG GLU ARG ILE ARG GLN ILE GLU
SEQRES 5 A 62 ALA LYS ALA LEU ARG LYS LEU ARG HIS PRO
SEQRES 1 B 198 MET LYS LEU LYS ILE LEU ASP LYS ASP ASN ALA THR LEU
SEQRES 2 B 198 ASN VAL PHE HIS ARG ASN LYS GLU HIS LYS THR ILE ASP
SEQRES 3 B 198 ASN VAL PRO THR ALA ASN LEU VAL ASP TRP TYR PRO LEU
SEQRES 4 B 198 SER ASN ALA TYR GLU TYR LYS LEU SER ARG ASN GLY GLU
SEQRES 5 B 198 TYR LEU GLU LEU LYS ARG LEU ARG SER THR LEU PRO SER
SEQRES 6 B 198 SER TYR GLY LEU ASP ASP ASN ASN GLN ASP ILE ILE ARG
SEQRES 7 B 198 ASP ASN ASN HIS ARG CYS LYS ILE GLY TYR TRP TYR ASN
SEQRES 8 B 198 PRO ALA VAL ARG LYS ASP ASN LEU LYS ILE ILE GLU LYS
SEQRES 9 B 198 ALA LYS GLN TYR GLY LEU PRO ILE ILE THR GLU GLU TYR
SEQRES 10 B 198 ASP ALA ASN THR VAL GLU GLN GLY PHE ARG ASP ILE GLY
SEQRES 11 B 198 VAL ILE PHE GLN SER LEU LYS THR ILE VAL VAL THR ARG
SEQRES 12 B 198 TYR LEU GLU GLY LYS THR GLU GLU GLU LEU ARG ILE PHE
SEQRES 13 B 198 ASN MET LYS SER GLU GLU SER GLN LEU ASN GLU ALA LEU
SEQRES 14 B 198 LYS GLU SER ASP PHE SER VAL ASP LEU THR TYR SER ASP
SEQRES 15 B 198 LEU GLY GLN ILE TYR ASN MET LEU LEU LEU MET LYS LYS
SEQRES 16 B 198 ILE SER LYS
FORMUL 3 HOH *54(H2 O)
HELIX 1 1 MET A 296 THR A 306 1 11
HELIX 2 2 THR A 308 GLY A 320 1 13
HELIX 3 3 THR A 328 GLY A 337 1 10
HELIX 4 4 THR A 339 HIS A 356 1 18
HELIX 5 5 ASN B 32 TRP B 36 5 5
HELIX 6 6 ASN B 73 ARG B 78 1 6
HELIX 7 7 ASP B 79 ARG B 83 5 5
HELIX 8 8 ASN B 91 TYR B 108 1 18
HELIX 9 9 ASP B 118 GLY B 147 1 30
HELIX 10 10 GLU B 152 ASN B 157 1 6
HELIX 11 11 SER B 160 GLU B 171 1 12
HELIX 12 12 ASP B 173 LYS B 198 1 26
SHEET 1 A 3 LYS B 2 ILE B 5 0
SHEET 2 A 3 ASN B 10 ARG B 18 -1 O THR B 12 N LYS B 4
SHEET 3 A 3 GLU B 21 PRO B 29 -1 O VAL B 28 N ALA B 11
SHEET 1 B 3 TYR B 43 LEU B 47 0
SHEET 2 B 3 TYR B 53 ARG B 58 -1 O GLU B 55 N LYS B 46
SHEET 3 B 3 CYS B 84 LYS B 85 -1 O CYS B 84 N LEU B 54
CISPEP 1 GLY B 147 LYS B 148 0 12.95
CRYST1 38.381 64.724 108.721 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 0.026055 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015450 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
