HEADER DNA BINDING PROTEIN 28-JUN-19 6KCQ
TITLE CRYSTAL STRUCTURE OF YEDK WITH SSDNA CONTAINING AN ABASIC SITE
CAVEAT 6KCQ RESIDUES DA A 3 AND DA A 4 ARE NOT PROPERLY LINKED: DISTANCE
CAVEAT 2 6KCQ BETWEEN O3' AND P IS 1.39. IT IS BECAUSE OF THE POOR
CAVEAT 3 6KCQ ELECTRIC DENSITY.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOS RESPONSE-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: YEDK;
COMPND 5 EC: 3.4.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(P*AP*AP*AP*(PED)P*AP*A)-3');
COMPND 9 CHAIN: A;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: YEDK, C4J69_22885, ECTO6_01993, EFV06_12905, EFV16_12155,
SOURCE 5 SAMEA3472108_01185, SAMEA3752559_04370;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 11 ORGANISM_TAXID: 562
KEYWDS DNA REPAIR, ABASIC SITE, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.WANG,H.BAO,H.HUANG
REVDAT 3 22-NOV-23 6KCQ 1 REMARK
REVDAT 2 22-JAN-20 6KCQ 1 JRNL
REVDAT 1 10-JUL-19 6KCQ 0
JRNL AUTH N.WANG,H.BAO,L.CHEN,Y.LIU,Y.LI,B.WU,H.HUANG
JRNL TITL MOLECULAR BASIS OF ABASIC SITE SENSING IN SINGLE-STRANDED
JRNL TITL 2 DNA BY THE SRAP DOMAIN OF E. COLI YEDK.
JRNL REF NUCLEIC ACIDS RES. V. 47 10388 2019
JRNL REFN ESSN 1362-4962
JRNL PMID 31504793
JRNL DOI 10.1093/NAR/GKZ744
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.520
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 22607
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.730
REMARK 3 FREE R VALUE TEST SET COUNT : 1070
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 37.6190 - 3.4010 1.00 2967 151 0.1442 0.1746
REMARK 3 2 3.4010 - 2.6997 1.00 2889 152 0.1471 0.2049
REMARK 3 3 2.6997 - 2.3585 1.00 2865 169 0.1569 0.2009
REMARK 3 4 2.3585 - 2.1429 1.00 2870 132 0.1509 0.1954
REMARK 3 5 2.1429 - 1.9893 1.00 2912 120 0.1660 0.2362
REMARK 3 6 1.9893 - 1.8720 0.99 2853 149 0.1845 0.2269
REMARK 3 7 1.8720 - 1.7783 0.89 2495 126 0.2067 0.2455
REMARK 3 8 1.7783 - 1.7008 0.58 1686 71 0.2181 0.2513
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.920
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 : 0.007 1941
REMARK 3 ANGLE : 0.885 2652
REMARK 3 CHIRALITY : 0.054 273
REMARK 3 PLANARITY : 0.005 333
REMARK 3 DIHEDRAL : 14.808 1122
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1299 60.7069 -5.7480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0205 T22: 0.0530
REMARK 3 T33: 0.0676 T12: 0.0038
REMARK 3 T13: -0.0087 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 1.1341 L22: 2.3436
REMARK 3 L33: 1.5143 L12: 0.5885
REMARK 3 L13: -0.0975 L23: -0.4004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0189 S12: -0.0227 S13: 0.0777
REMARK 3 S21: 0.0006 S22: 0.0763 S23: 0.3540
REMARK 3 S31: -0.0012 S32: -0.1993 S33: -0.0119
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 6KCQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1300012742.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24080
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.40900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 6KBS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M CALCIUM CHLORIDE DIHYDRATE 0.1M
REMARK 280 BIS-TRIS PH6.5 30% MPEG550, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 22.21150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.31725
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 11.10575
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MET B 1
REMARK 465 LEU B 223
REMARK 465 GLU B 224
REMARK 465 VAL B 225
REMARK 465 LEU B 226
REMARK 465 PHE B 227
REMARK 465 GLN B 228
REMARK 465 DA A -3
REMARK 465 DA A -2
REMARK 465 DA A 5
REMARK 465 DA A 6
REMARK 465 DA A 7
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 NE2 GLN B 154 O HOH B 301 1.75
REMARK 500 O HOH B 455 O HOH B 476 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DA A 3 O3' DA A 4 P -0.219
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 CYS B 2 CA - CB - SG ANGL. DEV. = -11.3 DEGREES
REMARK 500 PED A 2 O3' - P - O5' ANGL. DEV. = -11.9 DEGREES
REMARK 500 PED A 2 C3' - O3' - P ANGL. DEV. = -10.0 DEGREES
REMARK 500 DA A 3 O3' - P - O5' ANGL. DEV. = 30.2 DEGREES
REMARK 500 DA A 3 C3' - O3' - P ANGL. DEV. = -7.6 DEGREES
REMARK 500 DA A 4 O5' - P - OP1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 DA A 4 O5' - P - OP2 ANGL. DEV. = -11.8 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 ALA B 142 -39.76 -134.46
REMARK 500 GLN B 154 -113.25 23.01
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 506 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B 507 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH B 508 DISTANCE = 7.42 ANGSTROMS
DBREF1 6KCQ B 1 222 UNP A0A2S5ZH06_ECOLX
DBREF2 6KCQ B A0A2S5ZH06 1 222
DBREF 6KCQ A -3 7 PDB 6KCQ 6KCQ -3 7
SEQADV 6KCQ LEU B 223 UNP A0A2S5ZH0 EXPRESSION TAG
SEQADV 6KCQ GLU B 224 UNP A0A2S5ZH0 EXPRESSION TAG
SEQADV 6KCQ VAL B 225 UNP A0A2S5ZH0 EXPRESSION TAG
SEQADV 6KCQ LEU B 226 UNP A0A2S5ZH0 EXPRESSION TAG
SEQADV 6KCQ PHE B 227 UNP A0A2S5ZH0 EXPRESSION TAG
SEQADV 6KCQ GLN B 228 UNP A0A2S5ZH0 EXPRESSION TAG
SEQRES 1 B 228 MET CYS GLY ARG PHE ALA GLN SER GLN THR ARG GLU ASP
SEQRES 2 B 228 TYR LEU ALA LEU LEU ALA GLU ASP ILE GLU ARG ASP ILE
SEQRES 3 B 228 PRO TYR ASP PRO GLU PRO ILE GLY ARG TYR ASN VAL ALA
SEQRES 4 B 228 PRO GLY THR LYS VAL LEU LEU LEU SER GLU ARG ASP GLU
SEQRES 5 B 228 HIS LEU HIS LEU ASP PRO VAL PHE TRP GLY TYR ALA PRO
SEQRES 6 B 228 GLY TRP TRP ASP LYS PRO PRO LEU ILE ASN ALA ARG VAL
SEQRES 7 B 228 GLU THR ALA ALA THR SER ARG MET PHE LYS PRO LEU TRP
SEQRES 8 B 228 GLN HIS GLY ARG ALA ILE CYS PHE ALA ASP GLY TRP PHE
SEQRES 9 B 228 GLU TRP LYS LYS GLU GLY ASP LYS LYS GLN PRO PHE PHE
SEQRES 10 B 228 ILE TYR ARG ALA ASP GLY GLN PRO ILE PHE MET ALA ALA
SEQRES 11 B 228 ILE GLY SER THR PRO PHE GLU ARG GLY ASP GLU ALA GLU
SEQRES 12 B 228 GLY PHE LEU ILE VAL THR ALA ALA ALA ASP GLN GLY LEU
SEQRES 13 B 228 VAL ASP ILE HIS ASP ARG ARG PRO LEU VAL LEU SER PRO
SEQRES 14 B 228 GLU ALA ALA ARG GLU TRP MET ARG GLN GLU ILE SER GLY
SEQRES 15 B 228 LYS GLU ALA SER GLU ILE ALA ALA SER GLY CYS VAL PRO
SEQRES 16 B 228 ALA ASN GLN PHE SER TRP HIS PRO VAL SER ARG ALA VAL
SEQRES 17 B 228 GLY ASN VAL LYS ASN GLN GLY ALA GLU LEU ILE GLN PRO
SEQRES 18 B 228 VAL LEU GLU VAL LEU PHE GLN
SEQRES 1 A 11 DA DA DA DA DA PED DA DA DA DA DA
HET PED A 2 11
HETNAM PED PENTANE-3,4-DIOL-5-PHOSPHATE
HETSYN PED OPEN FORM OF 1'-2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
FORMUL 2 PED C5 H13 O6 P
FORMUL 3 HOH *218(H2 O)
HELIX 1 AA1 THR B 10 ALA B 16 1 7
HELIX 2 AA2 GLU B 20 ARG B 24 5 5
HELIX 3 AA3 PHE B 87 GLY B 94 1 8
HELIX 4 AA4 PRO B 135 GLY B 139 5 5
HELIX 5 AA5 ASP B 153 ILE B 159 5 7
HELIX 6 AA6 SER B 168 ARG B 177 1 10
HELIX 7 AA7 SER B 181 CYS B 193 1 13
HELIX 8 AA8 PRO B 195 ASN B 197 5 3
HELIX 9 AA9 SER B 205 ASN B 210 5 6
HELIX 10 AB1 GLY B 215 GLN B 220 5 6
SHEET 1 AA1 5 ARG B 35 VAL B 38 0
SHEET 2 AA1 5 PHE B 5 GLN B 7 -1 N PHE B 5 O VAL B 38
SHEET 3 AA1 5 GLY B 102 GLU B 109 -1 O GLY B 102 N ALA B 6
SHEET 4 AA1 5 LYS B 112 ARG B 120 -1 O LYS B 112 N GLU B 109
SHEET 5 AA1 5 PHE B 199 PRO B 203 -1 O SER B 200 N TYR B 119
SHEET 1 AA2 2 LYS B 43 ARG B 50 0
SHEET 2 AA2 2 HIS B 53 PHE B 60 -1 O HIS B 55 N SER B 48
SHEET 1 AA3 4 ASN B 75 ARG B 77 0
SHEET 2 AA3 4 PHE B 145 ALA B 151 1 O THR B 149 N ALA B 76
SHEET 3 AA3 4 ILE B 126 GLY B 132 -1 N ILE B 131 O LEU B 146
SHEET 4 AA3 4 ARG B 162 PRO B 164 0
SHEET 1 AA4 4 ARG B 95 ALA B 100 0
SHEET 2 AA4 4 ILE B 126 GLY B 132 -1 O ILE B 126 N ALA B 100
SHEET 3 AA4 4 PHE B 145 ALA B 151 -1 O LEU B 146 N ILE B 131
SHEET 4 AA4 4 VAL B 166 LEU B 167 0
LINK N CYS B 2 C1' PED A 2 1555 1555 1.48
LINK SG CYS B 2 C1' PED A 2 1555 1555 1.77
LINK O3' DA A 1 P PED A 2 1555 1555 1.56
LINK O3' PED A 2 P DA A 3 1555 1555 1.60
CISPEP 1 THR B 134 PRO B 135 0 -0.75
CRYST1 70.671 70.671 44.423 90.00 90.00 90.00 P 43 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 0.014150 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022511 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
