HEADER TRANSCRIPTION/DNA 06-JUL-90 3CRO
TITLE THE PHAGE 434 CRO/OR1 COMPLEX AT 2.5 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*AP*AP*GP*TP*AP*CP*AP*AP*AP*CP*TP*TP*TP*CP*TP*TP*G P*TP*AP*T)-3');
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-
COMPND 8 D(*TP*AP*TP*AP*CP*AP*AP*GP*AP*AP*AP*GP*TP*TP*TP*GP*T P*AP*CP*T)-3');
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PROTEIN (434 CRO);
COMPND 13 CHAIN: L, R
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: PHAGE 434;
SOURCE 7 ORGANISM_TAXID: 10712
KEYWDS PROTEIN-DNA COMPLEX, DOUBLE HELIX, TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MONDRAGON,S.C.HARRISON
REVDAT 5 21-FEB-24 3CRO 1 REMARK
REVDAT 4 24-FEB-09 3CRO 1 VERSN
REVDAT 3 01-APR-03 3CRO 1 JRNL
REVDAT 2 10-AUG-93 3CRO 1
REVDAT 1 15-OCT-91 3CRO 0
JRNL AUTH A.MONDRAGON,S.C.HARRISON
JRNL TITL THE PHAGE 434 CRO/OR1 COMPLEX AT 2.5 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 219 321 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 2038059
JRNL DOI 10.1016/0022-2836(91)90568-Q
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.MONDRAGON,C.WOLBERGER,S.C.HARRISON
REMARK 1 TITL STRUCTURE OF PHAGE 434 CRO PROTEIN AT 2.35 ANGSTROMS
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 205 179 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.K.AGGARWAL,D.W.RODGERS,M.DROTTAR,M.PTASHNE,S.C.HARRISON
REMARK 1 TITL RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE 434.
REMARK 1 TITL 2 A VIEW AT HIGH RESOLUTION
REMARK 1 REF SCIENCE V. 242 899 1988
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.E.ANDERSON,M.PTASHNE,S.C.HARRISON
REMARK 1 TITL STRUCTURE OF THE REPRESSOR-OPERATOR COMPLEX OF BACTERIOPHAGE
REMARK 1 TITL 2 434
REMARK 1 REF NATURE V. 326 846 1987
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 5351
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1042
REMARK 3 NUCLEIC ACID ATOMS : 814
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 25
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.010 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.300 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : 0.010 ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DENSITY FOR THE LAST SIX CARBOXY TERMINAL RESIDUES (64 -
REMARK 3 70) WAS NOT OBSERVED IN THE MAP AT ANY STAGE OF THE
REMARK 3 REFINEMENT AND THESE RESIDUES ARE PROBABLY DISORDERED.
REMARK 4
REMARK 4 3CRO 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_1000178923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 277.00
REMARK 200 PH : 6.20
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-13
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XENTRONICS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7232
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.20, TEMPERATURE 277.00K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.80000
REMARK 290 SMTRY3 2 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 300 REMARK: THE TWO PROTEIN DOMAINS HAVE BEEN ASSIGNED CHAIN INDICATORS
REMARK 300 *L* AND *R*. THE TWO DNA CHAINS HAVE BEEN ASSIGNED CHAIN
REMARK 300 INDICATORS *A* AND *B*. THE UNIT CELL CONTAINS TWO
REMARK 300 COMPLEXES EACH OF WHICH CONSISTS OF A PROTEIN DIMER AND
REMARK 300 TWO DIFFERENT STRANDS OF DNA.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, R
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 ARG L 65
REMARK 465 GLY L 66
REMARK 465 LYS L 67
REMARK 465 ALA L 68
REMARK 465 ALA L 69
REMARK 465 THR R 63
REMARK 465 LYS R 64
REMARK 465 ARG R 65
REMARK 465 GLY R 66
REMARK 465 LYS R 67
REMARK 465 ALA R 68
REMARK 465 ALA R 69
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 DT A 15 O3' DT A 15 C3' -0.071
REMARK 500 GLU L 19 CD GLU L 19 OE2 0.067
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 DA A 7 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT A 13 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC A 14 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DT A 15 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DT A 15 C3' - O3' - P ANGL. DEV. = -11.2 DEGREES
REMARK 500 DG A 17 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT A 18 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC B 5 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DA B 7 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DG B 12 O5' - P - OP1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 DT B 15 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG B 16 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 GLU L 19 N - CA - CB ANGL. DEV. = 11.8 DEGREES
REMARK 500 ASP L 55 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP L 55 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TYR L 61 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 PHE R 44 N - CA - CB ANGL. DEV. = 10.8 DEGREES
REMARK 500 ALA R 49 CB - CA - C ANGL. DEV. = -10.9 DEGREES
REMARK 500 ASP R 55 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP R 55 CB - CG - OD2 ANGL. DEV. = -6.7 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 GLN R 0 -130.87 101.31
REMARK 500 THR R 1 161.07 -40.83
REMARK 500 LYS R 7 -83.39 -60.34
REMARK 500 LYS R 8 -63.18 -14.67
REMARK 500 LYS R 14 75.10 63.69
REMARK 500 GLN R 17 -77.23 -43.27
REMARK 500 LEU R 20 -73.94 -62.90
REMARK 500 ALA R 21 -32.24 -35.33
REMARK 500 VAL R 26 -158.16 -122.61
REMARK 500 ARG R 41 65.48 -160.97
REMARK 500 PRO R 42 156.86 -34.13
REMARK 500 ILE R 48 -82.96 -53.77
REMARK 500 ALA R 49 -21.12 -31.74
REMARK 500 ASN R 53 66.30 72.24
REMARK 500 CYS R 54 -145.47 -152.48
REMARK 500 TYR R 61 -135.05 -121.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DNA CHAINS ARE ALIGNED AS FOLLOWS
REMARK 999
REMARK 999 *B* 5(PRIME) T-A-T-A-C-A-A-G-A-A-A-G-T-T-T-G-T-A-C-T
REMARK 999 *A* 3(PRIME) T-A-T-G-T-T-C-T-T-T-C-A-A-A-C-A-T-G-A-A
REMARK 999
REMARK 999 THE DNA CHAINS ARE NUMBERED SEQUENTIALLY. THE FOLLOWING
REMARK 999 TABLE PRESENTS THE RELATIONSHIP BETWEEN THE SEQUENTIAL
REMARK 999 DNA NUMBERING AND THAT USED IN THE PAPER CITED ON THE
REMARK 999 *JRNL* RECORDS ABOVE:
REMARK 999
REMARK 999 PDB ENTRY PUBLISHED
REMARK 999 --------- ---------
REMARK 999 A A 1 -4R
REMARK 999 A A 2 -3R
REMARK 999 G A 3 -2R
REMARK 999 T A 4 -1R
REMARK 999 A A 5 1R
REMARK 999 C A 6 2R
REMARK 999 A A 7 3R
REMARK 999 A A 8 4R
REMARK 999 A A 9 5R
REMARK 999 C A 10 6R
REMARK 999 T A 11 7R
REMARK 999 T A 12 7'L
REMARK 999 T A 13 6'L
REMARK 999 C A 14 5'L
REMARK 999 T A 15 4'L
REMARK 999 T A 16 3'L
REMARK 999 G A 17 2'L
REMARK 999 T A 18 1'L
REMARK 999 A A 19 -1'L
REMARK 999 T A 20 -2'L
REMARK 999 T B 1 -3L
REMARK 999 A B 2 -2L
REMARK 999 T B 3 -1L
REMARK 999 A B 4 1L
REMARK 999 C B 5 2L
REMARK 999 A B 6 3L
REMARK 999 A B 7 4L
REMARK 999 G B 8 5L
REMARK 999 A B 9 6L
REMARK 999 A B 10 7L
REMARK 999 A B 11 7'R
REMARK 999 G B 12 6'R
REMARK 999 T B 13 5'R
REMARK 999 T B 14 4'R
REMARK 999 T B 15 3'R
REMARK 999 G B 16 2'R
REMARK 999 T B 17 1'R
REMARK 999 A B 18 -1'R
REMARK 999 C B 19 -2'R
REMARK 999 T B 20 -3'R
DBREF 3CRO L -1 69 UNP P03036 RCRO_BP434 1 71
DBREF 3CRO R -1 69 UNP P03036 RCRO_BP434 1 71
DBREF 3CRO A 1 20 PDB 3CRO 3CRO 1 20
DBREF 3CRO B 1 20 PDB 3CRO 3CRO 1 20
SEQRES 1 A 20 DA DA DG DT DA DC DA DA DA DC DT DT DT
SEQRES 2 A 20 DC DT DT DG DT DA DT
SEQRES 1 B 20 DT DA DT DA DC DA DA DG DA DA DA DG DT
SEQRES 2 B 20 DT DT DG DT DA DC DT
SEQRES 1 L 71 MET GLN THR LEU SER GLU ARG LEU LYS LYS ARG ARG ILE
SEQRES 2 L 71 ALA LEU LYS MET THR GLN THR GLU LEU ALA THR LYS ALA
SEQRES 3 L 71 GLY VAL LYS GLN GLN SER ILE GLN LEU ILE GLU ALA GLY
SEQRES 4 L 71 VAL THR LYS ARG PRO ARG PHE LEU PHE GLU ILE ALA MET
SEQRES 5 L 71 ALA LEU ASN CYS ASP PRO VAL TRP LEU GLN TYR GLY THR
SEQRES 6 L 71 LYS ARG GLY LYS ALA ALA
SEQRES 1 R 71 MET GLN THR LEU SER GLU ARG LEU LYS LYS ARG ARG ILE
SEQRES 2 R 71 ALA LEU LYS MET THR GLN THR GLU LEU ALA THR LYS ALA
SEQRES 3 R 71 GLY VAL LYS GLN GLN SER ILE GLN LEU ILE GLU ALA GLY
SEQRES 4 R 71 VAL THR LYS ARG PRO ARG PHE LEU PHE GLU ILE ALA MET
SEQRES 5 R 71 ALA LEU ASN CYS ASP PRO VAL TRP LEU GLN TYR GLY THR
SEQRES 6 R 71 LYS ARG GLY LYS ALA ALA
FORMUL 5 HOH *25(H2 O)
HELIX 1 H1L THR L 1 ALA L 12 1 12
HELIX 2 H2L THR L 16 THR L 22 1 7
HELIX 3 H3L GLN L 28 ALA L 36 1 9
HELIX 4 H4L LEU L 45 ALA L 51 1 7
HELIX 5 H5L PRO L 56 TYR L 61 1 6
HELIX 6 H1R THR R 1 ALA R 12 1 12
HELIX 7 H2R THR R 16 THR R 22 1 7
HELIX 8 H3R GLN R 28 ALA R 36 1 9
HELIX 9 H4R LEU R 45 ALA R 51 1 7
HELIX 10 H5R PRO R 56 TYR R 61 1 6
CRYST1 49.200 47.600 61.700 90.00 109.50 90.00 P 1 21 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 0.020325 0.000000 0.007198 0.00000
SCALE2 0.000000 0.021008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017194 0.00000
(ATOM LINES ARE NOT SHOWN.)
END