HEADER TRANSFERASE/DNA 04-NOV-09 3KK3
TITLE HIV-1 REVERSE TRANSCRIPTASE-DNA COMPLEX WITH GS-9148 TERMINATED PRIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REVERSE TRANSCRIPTASE P66 SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P66 RT;
COMPND 5 EC: 2.7.7.49;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: REVERSE TRANSCRIPTASE P51 SUBUNIT;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: P51 RT;
COMPND 12 EC: 2.7.7.49;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: 5'-D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*GP*CP*GP
COMPND 17 *CP*C*(URT))-3';
COMPND 18 CHAIN: P;
COMPND 19 ENGINEERED: YES;
COMPND 20 OTHER_DETAILS: PRIMER DNA;
COMPND 21 MOL_ID: 4;
COMPND 22 MOLECULE: 5'-D(*AP*TP*GP*GP*TP*TP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP
COMPND 23 *GP*GP*GP*AP*CP*TP*GP*TP*G)-3';
COMPND 24 CHAIN: T;
COMPND 25 ENGINEERED: YES;
COMPND 26 OTHER_DETAILS: TEMPLATE DNA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11706;
SOURCE 5 STRAIN: HXB2D;
SOURCE 6 GENE: GAG-POL;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET14B;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1;
SOURCE 14 ORGANISM_COMMON: HIV-1;
SOURCE 15 ORGANISM_TAXID: 11706;
SOURCE 16 STRAIN: HXB2D;
SOURCE 17 GENE: GAG-POL;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET14B;
SOURCE 23 MOL_ID: 3;
SOURCE 24 SYNTHETIC: YES;
SOURCE 25 MOL_ID: 4;
SOURCE 26 SYNTHETIC: YES
KEYWDS HIV, REVERSE TRANSCRIPTASE, PROTEIN-DNA COMPLEX, TRANSFERASE,
KEYWDS 2 TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.B.LANSDON
REVDAT 4 06-SEP-23 3KK3 1 REMARK
REVDAT 3 13-OCT-21 3KK3 1 REMARK SEQADV LINK
REVDAT 2 11-AUG-10 3KK3 1 JRNL
REVDAT 1 23-MAR-10 3KK3 0
JRNL AUTH E.B.LANSDON,D.SAMUEL,L.LAGPACAN,K.M.BRENDZA,K.L.WHITE,
JRNL AUTH 2 M.HUNG,X.LIU,C.G.BOOJAMRA,R.L.MACKMAN,T.CIHLAR,A.S.RAY,
JRNL AUTH 3 M.E.MCGRATH,S.SWAMINATHAN
JRNL TITL VISUALIZING THE MOLECULAR INTERACTIONS OF A NUCLEOTIDE
JRNL TITL 2 ANALOG, GS-9148, WITH HIV-1 REVERSE TRANSCRIPTASE-DNA
JRNL TITL 3 COMPLEX.
JRNL REF J.MOL.BIOL. V. 397 967 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20156454
JRNL DOI 10.1016/J.JMB.2010.02.019
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 104550.120
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.1
REMARK 3 NUMBER OF REFLECTIONS : 27244
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1343
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2810
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2780
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.333
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1439
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0090
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 29088
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3740
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 208
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7875
REMARK 3 NUCLEIC ACID ATOMS : 844
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 22
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 21.00000
REMARK 3 B22 (A**2) : -26.60000
REMARK 3 B33 (A**2) : 5.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.52
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.68
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.940
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.450 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.600 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.870 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.110 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 42.15
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 : PROTEIN_REP.P
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.P
REMARK 3 PARAMETER FILE 3 : WATER_REP.PAR
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : URT.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : URT.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KK3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000056090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, 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 : 31465
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.61400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: 3KJV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% PEG4000, 0.05M MES PH 6.0, 5MM
REMARK 280 MAGNESIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 48.19900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.19900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 83.49900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.53500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 83.49900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.53500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.19900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 83.49900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 84.53500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.19900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 83.49900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 84.53500
REMARK 290 SMTRY3 8 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P, T
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 ILE A 556
REMARK 465 ARG A 557
REMARK 465 LYS A 558
REMARK 465 VAL A 559
REMARK 465 LEU A 560
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 SER B -1
REMARK 465 SER B 0
REMARK 465 PRO B 1
REMARK 465 ILE B 2
REMARK 465 SER B 3
REMARK 465 THR B 215
REMARK 465 THR B 216
REMARK 465 PRO B 217
REMARK 465 ASP B 218
REMARK 465 LYS B 219
REMARK 465 LYS B 220
REMARK 465 HIS B 221
REMARK 465 GLN B 222
REMARK 465 LYS B 223
REMARK 465 GLU B 224
REMARK 465 PRO B 225
REMARK 465 PRO B 226
REMARK 465 PHE B 227
REMARK 465 LEU B 228
REMARK 465 TRP B 229
REMARK 465 MET B 230
REMARK 465 GLY B 231
REMARK 465 GLY B 359
REMARK 465 ALA B 360
REMARK 465 HIS B 361
REMARK 465 LYS B 431
REMARK 465 GLU B 432
REMARK 465 PRO B 433
REMARK 465 ILE B 434
REMARK 465 VAL B 435
REMARK 465 GLY B 436
REMARK 465 ALA B 437
REMARK 465 GLU B 438
REMARK 465 THR B 439
REMARK 465 PHE B 440
REMARK 465 DA P 802
REMARK 465 DC P 803
REMARK 465 DA P 804
REMARK 465 DA T 701
REMARK 465 DT T 702
REMARK 465 DT T 726
REMARK 465 DG T 727
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 ASP B 86 CG OD1 OD2
REMARK 470 ARG B 358 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 430 CG CD OE1 OE2
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 TYR B 56 NH2 ARG B 143 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 NZ LYS B 173 NZ LYS B 173 3656 2.01
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 PRO B 19 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO B 392 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 DC P 809 O4' - C1' - N1 ANGL. DEV. = 2.2 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 SER A 3 129.13 -38.85
REMARK 500 PRO A 4 3.31 -66.70
REMARK 500 LYS A 66 76.09 52.30
REMARK 500 ASP A 67 5.44 59.17
REMARK 500 LYS A 73 157.00 -46.45
REMARK 500 LEU A 74 119.42 -173.00
REMARK 500 ILE A 135 -6.62 -54.54
REMARK 500 ASN A 136 -145.77 -168.87
REMARK 500 GLU A 138 -71.24 -40.03
REMARK 500 VAL A 148 -163.55 -114.11
REMARK 500 LYS A 154 -40.13 -16.08
REMARK 500 MET A 184 -122.30 45.12
REMARK 500 ASP A 192 51.90 -97.25
REMARK 500 PRO A 217 -167.42 -53.63
REMARK 500 LYS A 223 64.49 19.10
REMARK 500 GLU A 224 54.68 -148.56
REMARK 500 SER A 280 40.62 -80.98
REMARK 500 ARG A 284 62.24 -64.03
REMARK 500 GLU A 291 144.32 -28.55
REMARK 500 GLN A 334 97.26 -68.49
REMARK 500 THR A 351 -159.72 -139.40
REMARK 500 ALA A 355 44.32 -162.77
REMARK 500 PRO A 392 46.16 -77.26
REMARK 500 PRO A 412 -165.26 -75.73
REMARK 500 GLU A 413 113.63 -28.29
REMARK 500 THR A 472 -163.98 -119.87
REMARK 500 ILE B 5 -92.38 -171.25
REMARK 500 LYS B 13 134.96 -39.46
REMARK 500 PRO B 14 90.33 -53.90
REMARK 500 PHE B 61 -164.31 -129.26
REMARK 500 LYS B 66 -143.73 -159.06
REMARK 500 ASP B 76 71.40 -66.49
REMARK 500 GLN B 85 152.42 -49.66
REMARK 500 PHE B 87 12.08 -166.04
REMARK 500 PRO B 97 99.18 -59.74
REMARK 500 ALA B 98 -18.78 -49.67
REMARK 500 VAL B 111 21.82 -147.51
REMARK 500 ASP B 113 5.95 -63.30
REMARK 500 ASP B 121 139.47 -36.90
REMARK 500 PHE B 160 23.95 -76.05
REMARK 500 ILE B 167 -17.04 -48.32
REMARK 500 PRO B 170 -76.30 -56.20
REMARK 500 ASN B 175 63.54 -153.65
REMARK 500 PRO B 176 -6.53 -56.13
REMARK 500 MET B 184 -147.14 53.65
REMARK 500 LEU B 193 164.57 -39.08
REMARK 500 LEU B 209 -72.30 -96.50
REMARK 500 TRP B 212 -74.81 -84.22
REMARK 500 LEU B 234 110.29 -178.98
REMARK 500 ASP B 237 31.43 -71.45
REMARK 500
REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 218 LYS A 219 128.04
REMARK 500 THR A 286 LYS A 287 -128.86
REMARK 500 LYS A 287 ALA A 288 142.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DC P 820 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 443 OD2
REMARK 620 2 ASP A 443 OD1 55.7
REMARK 620 3 GLU A 478 OE2 81.6 133.0
REMARK 620 4 ASP A 498 OD1 78.1 74.4 118.7
REMARK 620 5 ASP A 498 OD2 60.7 104.0 64.1 55.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 P 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 T 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KJV RELATED DB: PDB
REMARK 900 RELATED ID: 3KK2 RELATED DB: PDB
REMARK 900 RELATED ID: 3KK3 RELATED DB: PDB
DBREF 3KK3 A 1 560 UNP P04585 POL_HV1H2 588 1147
DBREF 3KK3 B 1 440 UNP P04585 POL_HV1H2 588 1027
DBREF 3KK3 P 802 822 PDB 3KK3 3KK3 802 822
DBREF 3KK3 T 701 727 PDB 3KK3 3KK3 701 727
SEQADV 3KK3 CYS A 258 UNP P04585 GLN 845 ENGINEERED MUTATION
SEQADV 3KK3 SER A 280 UNP P04585 CYS 867 ENGINEERED MUTATION
SEQADV 3KK3 MET B -11 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 GLY B -10 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 SER B -9 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 SER B -8 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 HIS B -7 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 HIS B -6 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 HIS B -5 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 HIS B -4 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 HIS B -3 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 HIS B -2 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 SER B -1 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 SER B 0 UNP P04585 EXPRESSION TAG
SEQADV 3KK3 SER B 280 UNP P04585 CYS 867 ENGINEERED MUTATION
SEQRES 1 A 560 PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS
SEQRES 2 A 560 PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU
SEQRES 3 A 560 THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR
SEQRES 4 A 560 GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO
SEQRES 5 A 560 GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS
SEQRES 6 A 560 LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG
SEQRES 7 A 560 GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN
SEQRES 8 A 560 LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS
SEQRES 9 A 560 SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER
SEQRES 10 A 560 VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE
SEQRES 11 A 560 THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG
SEQRES 12 A 560 TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER
SEQRES 13 A 560 PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU
SEQRES 14 A 560 PRO PHE ARG LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN
SEQRES 15 A 560 TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE
SEQRES 16 A 560 GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS
SEQRES 17 A 560 LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS
SEQRES 18 A 560 GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU
SEQRES 19 A 560 HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO
SEQRES 20 A 560 GLU LYS ASP SER TRP THR VAL ASN ASP ILE CYS LYS LEU
SEQRES 21 A 560 VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY
SEQRES 22 A 560 ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR
SEQRES 23 A 560 LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA
SEQRES 24 A 560 GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU
SEQRES 25 A 560 PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU
SEQRES 26 A 560 ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR
SEQRES 27 A 560 TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR
SEQRES 28 A 560 GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP
SEQRES 29 A 560 VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR
SEQRES 30 A 560 GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS
SEQRES 31 A 560 LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR
SEQRES 32 A 560 GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE
SEQRES 33 A 560 VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU
SEQRES 34 A 560 GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL
SEQRES 35 A 560 ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA
SEQRES 36 A 560 GLY TYR VAL THR ASN ARG GLY ARG GLN LYS VAL VAL THR
SEQRES 37 A 560 LEU THR ASP THR THR ASN GLN LYS THR GLU LEU GLN ALA
SEQRES 38 A 560 ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN
SEQRES 39 A 560 ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN
SEQRES 40 A 560 ALA GLN PRO ASP GLN SER GLU SER GLU LEU VAL ASN GLN
SEQRES 41 A 560 ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU
SEQRES 42 A 560 ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU
SEQRES 43 A 560 GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS VAL
SEQRES 44 A 560 LEU
SEQRES 1 B 452 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER PRO
SEQRES 2 B 452 ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS PRO
SEQRES 3 B 452 GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU THR
SEQRES 4 B 452 GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR GLU
SEQRES 5 B 452 MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO GLU
SEQRES 6 B 452 ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS LYS
SEQRES 7 B 452 ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG GLU
SEQRES 8 B 452 LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN LEU
SEQRES 9 B 452 GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS SER
SEQRES 10 B 452 VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER VAL
SEQRES 11 B 452 PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE THR
SEQRES 12 B 452 ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG TYR
SEQRES 13 B 452 GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER PRO
SEQRES 14 B 452 ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU PRO
SEQRES 15 B 452 PHE ARG LYS GLN ASN PRO ASP ILE VAL ILE TYR GLN TYR
SEQRES 16 B 452 MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE GLY
SEQRES 17 B 452 GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS LEU
SEQRES 18 B 452 LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS GLN
SEQRES 19 B 452 LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU HIS
SEQRES 20 B 452 PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO GLU
SEQRES 21 B 452 LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU VAL
SEQRES 22 B 452 GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY ILE
SEQRES 23 B 452 LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR LYS
SEQRES 24 B 452 ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA GLU
SEQRES 25 B 452 LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU PRO
SEQRES 26 B 452 VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU ILE
SEQRES 27 B 452 ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR TYR
SEQRES 28 B 452 GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR GLY
SEQRES 29 B 452 LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP VAL
SEQRES 30 B 452 LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR GLU
SEQRES 31 B 452 SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS LEU
SEQRES 32 B 452 PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR GLU
SEQRES 33 B 452 TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE VAL
SEQRES 34 B 452 ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU GLU
SEQRES 35 B 452 LYS GLU PRO ILE VAL GLY ALA GLU THR PHE
SEQRES 1 P 21 DA DC DA DG DT DC DC DC DT DG DT DT DC
SEQRES 2 P 21 DG DG DG DC DG DC DC URT
SEQRES 1 T 27 DA DT DG DG DT DT DG DG DC DG DC DC DC
SEQRES 2 T 27 DG DA DA DC DA DG DG DG DA DC DT DG DT
SEQRES 3 T 27 DG
HET URT P 822 21
HET MG A 601 1
HET SO4 P 3 5
HET SO4 T 2 5
HETNAM URT ({[(2R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-FLUORO-2,5-
HETNAM 2 URT DIHYDROFURAN-2-YL]OXY}METHYL)PHOSPHONIC ACID
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
FORMUL 3 URT C10 H11 F N5 O5 P
FORMUL 5 MG MG 2+
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 8 HOH *22(H2 O)
HELIX 1 1 THR A 27 GLU A 44 1 18
HELIX 2 2 PHE A 77 THR A 84 1 8
HELIX 3 3 HIS A 96 LEU A 100 5 5
HELIX 4 4 ALA A 114 VAL A 118 5 5
HELIX 5 5 PHE A 124 ALA A 129 5 6
HELIX 6 6 GLY A 155 ASN A 175 1 21
HELIX 7 7 GLU A 194 ARG A 211 1 18
HELIX 8 8 THR A 253 SER A 268 1 16
HELIX 9 9 THR A 296 LEU A 310 1 15
HELIX 10 10 ASN A 363 TRP A 383 1 21
HELIX 11 11 GLN A 394 TYR A 405 1 12
HELIX 12 12 THR A 473 SER A 489 1 17
HELIX 13 13 SER A 499 ALA A 508 1 10
HELIX 14 14 SER A 515 LYS A 528 1 14
HELIX 15 15 GLU A 546 SER A 553 1 8
HELIX 16 16 THR B 27 GLU B 44 1 18
HELIX 17 17 PHE B 77 THR B 84 1 8
HELIX 18 18 PRO B 97 LYS B 102 5 6
HELIX 19 19 GLY B 112 TYR B 115 5 4
HELIX 20 20 PHE B 124 ALA B 129 5 6
HELIX 21 21 SER B 134 GLU B 138 5 5
HELIX 22 22 PHE B 160 LEU B 168 1 9
HELIX 23 23 LEU B 168 GLN B 174 1 7
HELIX 24 24 GLU B 194 ARG B 211 1 18
HELIX 25 25 HIS B 235 TRP B 239 5 5
HELIX 26 26 VAL B 254 SER B 268 1 15
HELIX 27 27 THR B 296 LEU B 310 1 15
HELIX 28 28 ASN B 363 GLY B 384 1 22
HELIX 29 29 GLN B 394 TRP B 402 1 9
HELIX 30 30 THR B 403 TYR B 405 5 3
HELIX 31 31 LEU B 422 TRP B 426 5 5
SHEET 1 A 3 ILE A 47 LYS A 49 0
SHEET 2 A 3 ILE A 142 TYR A 146 -1 O GLN A 145 N SER A 48
SHEET 3 A 3 PHE A 130 ILE A 132 -1 N PHE A 130 O TYR A 144
SHEET 1 B 2 VAL A 60 LYS A 64 0
SHEET 2 B 2 TRP A 71 VAL A 75 -1 O ARG A 72 N ILE A 63
SHEET 1 C 4 VAL A 179 TYR A 183 0
SHEET 2 C 4 ASP A 186 SER A 191 -1 O ASP A 186 N TYR A 183
SHEET 3 C 4 SER A 105 ASP A 110 -1 N SER A 105 O SER A 191
SHEET 4 C 4 LYS A 220 HIS A 221 -1 O HIS A 221 N VAL A 108
SHEET 1 D 3 PHE A 227 TRP A 229 0
SHEET 2 D 3 TYR A 232 LEU A 234 -1 O TYR A 232 N TRP A 229
SHEET 3 D 3 TRP A 239 VAL A 241 -1 O THR A 240 N GLU A 233
SHEET 1 E 5 ASN A 348 TYR A 354 0
SHEET 2 E 5 TRP A 337 TYR A 342 -1 N TRP A 337 O TYR A 354
SHEET 3 E 5 ILE A 326 LYS A 331 -1 N ILE A 326 O TYR A 342
SHEET 4 E 5 LYS A 388 LEU A 391 1 O LYS A 388 N ALA A 327
SHEET 5 E 5 TRP A 414 PHE A 416 1 O GLU A 415 N PHE A 389
SHEET 1 F 2 HIS A 361 THR A 362 0
SHEET 2 F 2 GLN A 512 SER A 513 -1 O GLN A 512 N THR A 362
SHEET 1 G 5 GLN A 464 LEU A 469 0
SHEET 2 G 5 GLY A 453 THR A 459 -1 N ALA A 455 O VAL A 467
SHEET 3 G 5 GLU A 438 ALA A 445 -1 N ALA A 445 O LYS A 454
SHEET 4 G 5 GLU A 492 THR A 497 1 O ASN A 494 N PHE A 440
SHEET 5 G 5 LYS A 530 TRP A 535 1 O TYR A 532 N ILE A 495
SHEET 1 H 3 ILE B 47 ILE B 50 0
SHEET 2 H 3 ILE B 142 TYR B 146 -1 O ARG B 143 N ILE B 50
SHEET 3 H 3 PHE B 130 ILE B 132 -1 N PHE B 130 O TYR B 144
SHEET 1 I 2 VAL B 60 LYS B 64 0
SHEET 2 I 2 TRP B 71 VAL B 75 -1 O ARG B 72 N ILE B 63
SHEET 1 J 3 THR B 107 ASP B 110 0
SHEET 2 J 3 ASP B 186 GLY B 190 -1 O LEU B 187 N LEU B 109
SHEET 3 J 3 VAL B 179 TYR B 183 -1 N TYR B 181 O TYR B 188
SHEET 1 K 2 TRP B 252 THR B 253 0
SHEET 2 K 2 VAL B 292 ILE B 293 -1 O ILE B 293 N TRP B 252
SHEET 1 L 5 ASN B 348 ALA B 355 0
SHEET 2 L 5 GLN B 336 TYR B 342 -1 N TRP B 337 O TYR B 354
SHEET 3 L 5 ILE B 326 GLY B 333 -1 N GLN B 330 O THR B 338
SHEET 4 L 5 LYS B 388 LEU B 391 1 O LYS B 390 N ILE B 329
SHEET 5 L 5 GLU B 413 PHE B 416 1 O GLU B 415 N LEU B 391
LINK O3' DC P 821 P1 URT P 822 1555 1555 1.63
LINK OD2 ASP A 443 MG MG A 601 1555 1555 2.29
LINK OD1 ASP A 443 MG MG A 601 1555 1555 2.44
LINK OE2 GLU A 478 MG MG A 601 1555 1555 2.37
LINK OD1 ASP A 498 MG MG A 601 1555 1555 2.32
LINK OD2 ASP A 498 MG MG A 601 1555 1555 2.38
CISPEP 1 PRO A 225 PRO A 226 0 -5.11
CISPEP 2 PRO A 420 PRO A 421 0 7.76
CISPEP 3 GLY A 543 GLY A 544 0 4.97
CISPEP 4 GLY B 213 LEU B 214 0 1.93
SITE 1 AC1 4 ASP A 443 GLY A 444 GLU A 478 ASP A 498
SITE 1 AC2 3 DG P 816 DG P 817 DG T 710
SITE 1 AC3 2 DG T 707 DG T 708
CRYST1 166.998 169.070 96.398 90.00 90.00 90.00 C 2 2 21 8
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 0.005988 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005915 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010374 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
