HEADER HYDROLASE 05-JUN-14 4TO6
TITLE STRUCTURE BASIS OF CELLULAR DNTP REGULATION, SAMHD1-DGTP-DATP-
TITLE 2 DTTP/DGTP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYNUCLEOSIDE TRIPHOSPHATE TRIPHOSPHOHYDROLASE SAMHD1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DNTPASE,DENDRITIC CELL-DERIVED IFNG-INDUCED PROTEIN,DCIP,
COMPND 5 MONOCYTE PROTEIN 5,MOP-5,SAM DOMAIN AND HD DOMAIN-CONTAINING PROTEIN
COMPND 6 1;
COMPND 7 EC: 3.1.5.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SAMHD1, MOP5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SAMHD1, HIV, RESTRICTION FACTOR, DNTPASE, DNTP REGULATION, HOST
KEYWDS 2 PATHOGEN INTERACTION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.JI,C.TANG,Q.ZHAO,W.WANG,Y.XIONG
REVDAT 6 27-SEP-23 4TO6 1 REMARK
REVDAT 5 30-MAR-22 4TO6 1 REMARK LINK
REVDAT 4 22-NOV-17 4TO6 1 SOURCE JRNL REMARK
REVDAT 3 29-OCT-14 4TO6 1 JRNL
REVDAT 2 15-OCT-14 4TO6 1 JRNL
REVDAT 1 01-OCT-14 4TO6 0
JRNL AUTH X.JI,C.TANG,Q.ZHAO,W.WANG,Y.XIONG
JRNL TITL STRUCTURAL BASIS OF CELLULAR DNTP REGULATION BY SAMHD1.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 E4305 2014
JRNL REFN ESSN 1091-6490
JRNL PMID 25267621
JRNL DOI 10.1073/PNAS.1412289111
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 85283
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) : 0.225
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4259
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5638
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.4120
REMARK 3 BIN FREE R VALUE SET COUNT : 289
REMARK 3 BIN FREE R VALUE : 0.4260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15700
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 366
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.20000
REMARK 3 B22 (A**2) : 3.34000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.92000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.528
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.258
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.346
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.458
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16451 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 15619 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22289 ; 1.429 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35961 ; 0.930 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1912 ; 5.203 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 808 ;40.009 ;23.960
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2920 ;16.325 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 112 ;16.807 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2344 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18204 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3864 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7672 ; 2.887 ; 3.978
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7671 ; 2.887 ; 3.977
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9576 ; 4.614 ; 5.958
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 114 599 B 114 599 32108 0.020 0.050
REMARK 3 2 A 114 599 C 114 599 32105 0.020 0.050
REMARK 3 3 A 114 599 D 114 599 32055 0.030 0.050
REMARK 3 4 B 114 599 C 114 599 32070 0.020 0.050
REMARK 3 5 B 114 599 D 114 599 32021 0.030 0.050
REMARK 3 6 C 114 599 D 114 599 32039 0.030 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 114 A 599
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3434 2.9956 126.5837
REMARK 3 T TENSOR
REMARK 3 T11: 0.2216 T22: 0.0294
REMARK 3 T33: 0.2667 T12: 0.0274
REMARK 3 T13: 0.1366 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.6315 L22: 0.0086
REMARK 3 L33: 1.2737 L12: -0.0460
REMARK 3 L13: 0.8922 L23: -0.0582
REMARK 3 S TENSOR
REMARK 3 S11: 0.0481 S12: -0.0901 S13: -0.0262
REMARK 3 S21: -0.0352 S22: 0.0062 S23: -0.0283
REMARK 3 S31: 0.0136 S32: -0.1386 S33: -0.0542
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 114 B 599
REMARK 3 ORIGIN FOR THE GROUP (A): 61.0876 -3.0752 166.5349
REMARK 3 T TENSOR
REMARK 3 T11: 0.1448 T22: 0.1398
REMARK 3 T33: 0.2666 T12: 0.0047
REMARK 3 T13: 0.1098 T23: -0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 0.7758 L22: 0.0047
REMARK 3 L33: 1.9040 L12: -0.0042
REMARK 3 L13: 1.2017 L23: 0.0043
REMARK 3 S TENSOR
REMARK 3 S11: 0.1573 S12: -0.0176 S13: -0.0621
REMARK 3 S21: -0.0012 S22: 0.0282 S23: -0.0129
REMARK 3 S31: 0.1991 S32: 0.0245 S33: -0.1855
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 114 C 599
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7576 7.6395 164.9382
REMARK 3 T TENSOR
REMARK 3 T11: 0.1036 T22: 0.8470
REMARK 3 T33: 0.2744 T12: 0.0842
REMARK 3 T13: 0.1564 T23: -0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 0.7619 L22: 0.0539
REMARK 3 L33: 2.0424 L12: 0.0647
REMARK 3 L13: 1.2186 L23: 0.0363
REMARK 3 S TENSOR
REMARK 3 S11: -0.1069 S12: -0.7954 S13: -0.0208
REMARK 3 S21: -0.0743 S22: -0.0295 S23: -0.1169
REMARK 3 S31: -0.0972 S32: -1.3115 S33: 0.1365
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 114 D 599
REMARK 3 ORIGIN FOR THE GROUP (A): 64.3415 15.7675 132.8093
REMARK 3 T TENSOR
REMARK 3 T11: 0.2561 T22: 0.4747
REMARK 3 T33: 0.3031 T12: -0.2632
REMARK 3 T13: 0.0810 T23: 0.1024
REMARK 3 L TENSOR
REMARK 3 L11: 0.5114 L22: 0.0360
REMARK 3 L33: 2.3418 L12: -0.1159
REMARK 3 L13: 1.0310 L23: -0.1848
REMARK 3 S TENSOR
REMARK 3 S11: -0.2677 S12: 0.4777 S13: 0.0212
REMARK 3 S21: 0.0849 S22: -0.0740 S23: 0.0492
REMARK 3 S31: -0.5159 S32: 1.0454 S33: 0.3416
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4TO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000201966.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-13
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 : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
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, DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85312
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.330
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.15500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.95000
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: NULL
REMARK 200 STARTING MODEL: 4BZB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SPG BUFFER, PEG 1500, BATCH MODE,
REMARK 280 TEMPERATURE 298K
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 70.40400
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 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: 29020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ASP A 113
REMARK 465 SER A 278
REMARK 465 PRO A 279
REMARK 465 VAL A 280
REMARK 465 GLU A 281
REMARK 465 ASP A 282
REMARK 465 SER A 283
REMARK 465 ASP A 600
REMARK 465 SER A 601
REMARK 465 THR A 602
REMARK 465 SER A 603
REMARK 465 VAL A 604
REMARK 465 GLN A 605
REMARK 465 ASN A 606
REMARK 465 PRO A 607
REMARK 465 THR A 608
REMARK 465 ARG A 609
REMARK 465 LEU A 610
REMARK 465 ARG A 611
REMARK 465 GLU A 612
REMARK 465 ALA A 613
REMARK 465 SER A 614
REMARK 465 LYS A 615
REMARK 465 SER A 616
REMARK 465 ARG A 617
REMARK 465 VAL A 618
REMARK 465 GLN A 619
REMARK 465 LEU A 620
REMARK 465 PHE A 621
REMARK 465 LYS A 622
REMARK 465 ASP A 623
REMARK 465 ASP A 624
REMARK 465 PRO A 625
REMARK 465 MET A 626
REMARK 465 ASP B 113
REMARK 465 SER B 278
REMARK 465 PRO B 279
REMARK 465 VAL B 280
REMARK 465 GLU B 281
REMARK 465 ASP B 282
REMARK 465 SER B 283
REMARK 465 ASP B 600
REMARK 465 SER B 601
REMARK 465 THR B 602
REMARK 465 SER B 603
REMARK 465 VAL B 604
REMARK 465 GLN B 605
REMARK 465 ASN B 606
REMARK 465 PRO B 607
REMARK 465 THR B 608
REMARK 465 ARG B 609
REMARK 465 LEU B 610
REMARK 465 ARG B 611
REMARK 465 GLU B 612
REMARK 465 ALA B 613
REMARK 465 SER B 614
REMARK 465 LYS B 615
REMARK 465 SER B 616
REMARK 465 ARG B 617
REMARK 465 VAL B 618
REMARK 465 GLN B 619
REMARK 465 LEU B 620
REMARK 465 PHE B 621
REMARK 465 LYS B 622
REMARK 465 ASP B 623
REMARK 465 ASP B 624
REMARK 465 PRO B 625
REMARK 465 MET B 626
REMARK 465 ASP C 113
REMARK 465 SER C 278
REMARK 465 PRO C 279
REMARK 465 VAL C 280
REMARK 465 GLU C 281
REMARK 465 ASP C 282
REMARK 465 SER C 283
REMARK 465 ASP C 600
REMARK 465 SER C 601
REMARK 465 THR C 602
REMARK 465 SER C 603
REMARK 465 VAL C 604
REMARK 465 GLN C 605
REMARK 465 ASN C 606
REMARK 465 PRO C 607
REMARK 465 THR C 608
REMARK 465 ARG C 609
REMARK 465 LEU C 610
REMARK 465 ARG C 611
REMARK 465 GLU C 612
REMARK 465 ALA C 613
REMARK 465 SER C 614
REMARK 465 LYS C 615
REMARK 465 SER C 616
REMARK 465 ARG C 617
REMARK 465 VAL C 618
REMARK 465 GLN C 619
REMARK 465 LEU C 620
REMARK 465 PHE C 621
REMARK 465 LYS C 622
REMARK 465 ASP C 623
REMARK 465 ASP C 624
REMARK 465 PRO C 625
REMARK 465 MET C 626
REMARK 465 ASP D 113
REMARK 465 SER D 278
REMARK 465 PRO D 279
REMARK 465 VAL D 280
REMARK 465 GLU D 281
REMARK 465 ASP D 282
REMARK 465 SER D 283
REMARK 465 ASP D 600
REMARK 465 SER D 601
REMARK 465 THR D 602
REMARK 465 SER D 603
REMARK 465 VAL D 604
REMARK 465 GLN D 605
REMARK 465 ASN D 606
REMARK 465 PRO D 607
REMARK 465 THR D 608
REMARK 465 ARG D 609
REMARK 465 LEU D 610
REMARK 465 ARG D 611
REMARK 465 GLU D 612
REMARK 465 ALA D 613
REMARK 465 SER D 614
REMARK 465 LYS D 615
REMARK 465 SER D 616
REMARK 465 ARG D 617
REMARK 465 VAL D 618
REMARK 465 GLN D 619
REMARK 465 LEU D 620
REMARK 465 PHE D 621
REMARK 465 LYS D 622
REMARK 465 ASP D 623
REMARK 465 ASP D 624
REMARK 465 PRO D 625
REMARK 465 MET D 626
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 O1G DGT B 702 MG MG C 702 1.59
REMARK 500 O2G DGT A 702 MG MG D 701 1.64
REMARK 500 NZ LYS B 116 O3G DGT C 704 2.02
REMARK 500 NZ LYS A 523 O1G DGT C 704 2.10
REMARK 500 O TYR A 298 O HOH A 812 2.18
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 NH2 ARG A 408 CG LYS B 478 1454 1.86
REMARK 500 O GLU B 543 OE1 GLN C 465 1655 2.07
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 ASP A 388 CB - CG - OD2 ANGL. DEV. = -5.8 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 SER A 214 -111.92 51.31
REMARK 500 ARG A 220 -51.43 -120.02
REMARK 500 ASN A 306 -1.17 -143.36
REMARK 500 ASN A 345 18.58 57.23
REMARK 500 ALA A 373 -58.66 -129.30
REMARK 500 ARG A 451 30.79 70.47
REMARK 500 MET A 509 45.21 -140.42
REMARK 500 GLN A 510 -125.97 45.34
REMARK 500 SER B 214 -113.37 51.95
REMARK 500 ARG B 220 -52.15 -120.02
REMARK 500 ASN B 306 -0.70 -145.01
REMARK 500 ASN B 345 17.28 58.84
REMARK 500 ALA B 373 -59.19 -128.28
REMARK 500 TYR B 507 30.73 -93.85
REMARK 500 GLN B 510 -125.63 44.32
REMARK 500 SER C 214 -112.44 52.03
REMARK 500 ASN C 306 -2.44 -144.17
REMARK 500 ASN C 345 17.09 57.46
REMARK 500 ALA C 373 -60.79 -126.00
REMARK 500 TYR C 507 30.68 -93.85
REMARK 500 GLN C 510 -124.65 44.72
REMARK 500 SER D 214 -113.56 53.02
REMARK 500 ARG D 220 -52.56 -120.45
REMARK 500 ASN D 306 -1.02 -145.00
REMARK 500 ASN D 345 16.93 58.18
REMARK 500 ALA D 373 -60.72 -129.78
REMARK 500 GLN D 510 -124.63 44.81
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 D 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DGT A 702 O1B
REMARK 620 2 DGT A 702 O1A 79.4
REMARK 620 3 DTP C 701 O3G 87.5 157.7
REMARK 620 4 DTP C 701 O2B 81.1 86.4 73.7
REMARK 620 5 HOH C 802 O 160.2 102.1 84.4 79.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DTP A 703 O3G
REMARK 620 2 DTP A 703 O2B 76.4
REMARK 620 3 HOH A 808 O 84.6 91.7
REMARK 620 4 DGT C 704 O2B 85.8 97.2 165.1
REMARK 620 5 DGT C 704 O3G 123.5 159.9 87.7 88.1
REMARK 620 6 DGT C 704 O1A 161.8 87.5 104.5 88.0 73.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DTP B 704 O1B
REMARK 620 2 DTP B 704 O2G 76.4
REMARK 620 3 HOH B 803 O 94.2 87.5
REMARK 620 4 DGT D 704 O3G 160.5 93.6 102.2
REMARK 620 5 DGT D 704 O1B 85.2 74.0 161.2 75.9
REMARK 620 6 DGT D 704 O2A 87.4 152.1 116.7 94.5 82.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DGT B 702 O2B
REMARK 620 2 DGT B 702 O2A 76.2
REMARK 620 3 DTP D 702 O1B 86.0 86.4
REMARK 620 4 DTP D 702 O3G 91.3 160.5 77.7
REMARK 620 5 HOH D 805 O 173.2 100.4 87.9 90.3
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 TTP A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGT A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTP A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TTP B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGT B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTP B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTP C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGT C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGT C 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTP D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TTP D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGT D 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TNP RELATED DB: PDB
REMARK 900 RELATED ID: 4TNR RELATED DB: PDB
REMARK 900 RELATED ID: 4TNQ RELATED DB: PDB
REMARK 900 RELATED ID: 4TNX RELATED DB: PDB
REMARK 900 RELATED ID: 4TNY RELATED DB: PDB
REMARK 900 RELATED ID: 4TNZ RELATED DB: PDB
REMARK 900 RELATED ID: 4TO0 RELATED DB: PDB
REMARK 900 RELATED ID: 4TO1 RELATED DB: PDB
REMARK 900 RELATED ID: 4TO2 RELATED DB: PDB
REMARK 900 RELATED ID: 4TO3 RELATED DB: PDB
REMARK 900 RELATED ID: 4TO4 RELATED DB: PDB
REMARK 900 RELATED ID: 4TO5 RELATED DB: PDB
DBREF 4TO6 A 113 626 UNP Q9Y3Z3 SAMH1_HUMAN 113 626
DBREF 4TO6 B 113 626 UNP Q9Y3Z3 SAMH1_HUMAN 113 626
DBREF 4TO6 C 113 626 UNP Q9Y3Z3 SAMH1_HUMAN 113 626
DBREF 4TO6 D 113 626 UNP Q9Y3Z3 SAMH1_HUMAN 113 626
SEQADV 4TO6 ARG A 206 UNP Q9Y3Z3 HIS 206 ENGINEERED MUTATION
SEQADV 4TO6 ASN A 207 UNP Q9Y3Z3 ASP 207 ENGINEERED MUTATION
SEQADV 4TO6 ARG B 206 UNP Q9Y3Z3 HIS 206 ENGINEERED MUTATION
SEQADV 4TO6 ASN B 207 UNP Q9Y3Z3 ASP 207 ENGINEERED MUTATION
SEQADV 4TO6 ARG C 206 UNP Q9Y3Z3 HIS 206 ENGINEERED MUTATION
SEQADV 4TO6 ASN C 207 UNP Q9Y3Z3 ASP 207 ENGINEERED MUTATION
SEQADV 4TO6 ARG D 206 UNP Q9Y3Z3 HIS 206 ENGINEERED MUTATION
SEQADV 4TO6 ASN D 207 UNP Q9Y3Z3 ASP 207 ENGINEERED MUTATION
SEQRES 1 A 514 ASP THR MET LYS VAL ILE ASN ASP PRO ILE HIS GLY HIS
SEQRES 2 A 514 ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP THR
SEQRES 3 A 514 PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU GLY
SEQRES 4 A 514 GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN ARG
SEQRES 5 A 514 PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY CYS
SEQRES 6 A 514 LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU GLN
SEQRES 7 A 514 ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA GLY
SEQRES 8 A 514 LEU CYS ARG ASN LEU GLY HIS GLY PRO PHE SER HIS MET
SEQRES 9 A 514 PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU VAL
SEQRES 10 A 514 LYS TRP THR HIS GLU GLN GLY SER VAL MET MET PHE GLU
SEQRES 11 A 514 HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MET GLU
SEQRES 12 A 514 GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE ILE
SEQRES 13 A 514 LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL GLU
SEQRES 14 A 514 ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN LYS
SEQRES 15 A 514 SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN GLY
SEQRES 16 A 514 ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP CYS
SEQRES 17 A 514 HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS ARG
SEQRES 18 A 514 PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN GLU
SEQRES 19 A 514 LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN LEU
SEQRES 20 A 514 TYR ASP MET PHE HIS THR ARG ASN SER LEU HIS ARG ARG
SEQRES 21 A 514 ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR MET
SEQRES 22 A 514 ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE GLU
SEQRES 23 A 514 ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER THR
SEQRES 24 A 514 ALA ILE ASP ASP MET GLU ALA TYR THR LYS LEU THR ASP
SEQRES 25 A 514 ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO LYS
SEQRES 26 A 514 LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU TYR
SEQRES 27 A 514 ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO THR
SEQRES 28 A 514 GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER LEU
SEQRES 29 A 514 PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU LEU
SEQRES 30 A 514 ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP VAL
SEQRES 31 A 514 ILE ASN MET ASP TYR GLY MET GLN GLU LYS ASN PRO ILE
SEQRES 32 A 514 ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN ARG
SEQRES 33 A 514 ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU LEU
SEQRES 34 A 514 PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR CYS
SEQRES 35 A 514 LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG GLN
SEQRES 36 A 514 TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR LYS
SEQRES 37 A 514 PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR PRO
SEQRES 38 A 514 GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN ASN
SEQRES 39 A 514 PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL GLN
SEQRES 40 A 514 LEU PHE LYS ASP ASP PRO MET
SEQRES 1 B 514 ASP THR MET LYS VAL ILE ASN ASP PRO ILE HIS GLY HIS
SEQRES 2 B 514 ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP THR
SEQRES 3 B 514 PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU GLY
SEQRES 4 B 514 GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN ARG
SEQRES 5 B 514 PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY CYS
SEQRES 6 B 514 LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU GLN
SEQRES 7 B 514 ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA GLY
SEQRES 8 B 514 LEU CYS ARG ASN LEU GLY HIS GLY PRO PHE SER HIS MET
SEQRES 9 B 514 PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU VAL
SEQRES 10 B 514 LYS TRP THR HIS GLU GLN GLY SER VAL MET MET PHE GLU
SEQRES 11 B 514 HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MET GLU
SEQRES 12 B 514 GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE ILE
SEQRES 13 B 514 LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL GLU
SEQRES 14 B 514 ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN LYS
SEQRES 15 B 514 SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN GLY
SEQRES 16 B 514 ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP CYS
SEQRES 17 B 514 HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS ARG
SEQRES 18 B 514 PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN GLU
SEQRES 19 B 514 LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN LEU
SEQRES 20 B 514 TYR ASP MET PHE HIS THR ARG ASN SER LEU HIS ARG ARG
SEQRES 21 B 514 ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR MET
SEQRES 22 B 514 ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE GLU
SEQRES 23 B 514 ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER THR
SEQRES 24 B 514 ALA ILE ASP ASP MET GLU ALA TYR THR LYS LEU THR ASP
SEQRES 25 B 514 ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO LYS
SEQRES 26 B 514 LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU TYR
SEQRES 27 B 514 ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO THR
SEQRES 28 B 514 GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER LEU
SEQRES 29 B 514 PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU LEU
SEQRES 30 B 514 ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP VAL
SEQRES 31 B 514 ILE ASN MET ASP TYR GLY MET GLN GLU LYS ASN PRO ILE
SEQRES 32 B 514 ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN ARG
SEQRES 33 B 514 ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU LEU
SEQRES 34 B 514 PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR CYS
SEQRES 35 B 514 LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG GLN
SEQRES 36 B 514 TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR LYS
SEQRES 37 B 514 PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR PRO
SEQRES 38 B 514 GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN ASN
SEQRES 39 B 514 PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL GLN
SEQRES 40 B 514 LEU PHE LYS ASP ASP PRO MET
SEQRES 1 C 514 ASP THR MET LYS VAL ILE ASN ASP PRO ILE HIS GLY HIS
SEQRES 2 C 514 ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP THR
SEQRES 3 C 514 PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU GLY
SEQRES 4 C 514 GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN ARG
SEQRES 5 C 514 PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY CYS
SEQRES 6 C 514 LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU GLN
SEQRES 7 C 514 ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA GLY
SEQRES 8 C 514 LEU CYS ARG ASN LEU GLY HIS GLY PRO PHE SER HIS MET
SEQRES 9 C 514 PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU VAL
SEQRES 10 C 514 LYS TRP THR HIS GLU GLN GLY SER VAL MET MET PHE GLU
SEQRES 11 C 514 HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MET GLU
SEQRES 12 C 514 GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE ILE
SEQRES 13 C 514 LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL GLU
SEQRES 14 C 514 ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN LYS
SEQRES 15 C 514 SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN GLY
SEQRES 16 C 514 ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP CYS
SEQRES 17 C 514 HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS ARG
SEQRES 18 C 514 PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN GLU
SEQRES 19 C 514 LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN LEU
SEQRES 20 C 514 TYR ASP MET PHE HIS THR ARG ASN SER LEU HIS ARG ARG
SEQRES 21 C 514 ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR MET
SEQRES 22 C 514 ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE GLU
SEQRES 23 C 514 ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER THR
SEQRES 24 C 514 ALA ILE ASP ASP MET GLU ALA TYR THR LYS LEU THR ASP
SEQRES 25 C 514 ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO LYS
SEQRES 26 C 514 LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU TYR
SEQRES 27 C 514 ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO THR
SEQRES 28 C 514 GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER LEU
SEQRES 29 C 514 PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU LEU
SEQRES 30 C 514 ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP VAL
SEQRES 31 C 514 ILE ASN MET ASP TYR GLY MET GLN GLU LYS ASN PRO ILE
SEQRES 32 C 514 ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN ARG
SEQRES 33 C 514 ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU LEU
SEQRES 34 C 514 PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR CYS
SEQRES 35 C 514 LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG GLN
SEQRES 36 C 514 TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR LYS
SEQRES 37 C 514 PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR PRO
SEQRES 38 C 514 GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN ASN
SEQRES 39 C 514 PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL GLN
SEQRES 40 C 514 LEU PHE LYS ASP ASP PRO MET
SEQRES 1 D 514 ASP THR MET LYS VAL ILE ASN ASP PRO ILE HIS GLY HIS
SEQRES 2 D 514 ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP THR
SEQRES 3 D 514 PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU GLY
SEQRES 4 D 514 GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN ARG
SEQRES 5 D 514 PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY CYS
SEQRES 6 D 514 LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU GLN
SEQRES 7 D 514 ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA GLY
SEQRES 8 D 514 LEU CYS ARG ASN LEU GLY HIS GLY PRO PHE SER HIS MET
SEQRES 9 D 514 PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU VAL
SEQRES 10 D 514 LYS TRP THR HIS GLU GLN GLY SER VAL MET MET PHE GLU
SEQRES 11 D 514 HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MET GLU
SEQRES 12 D 514 GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE ILE
SEQRES 13 D 514 LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL GLU
SEQRES 14 D 514 ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN LYS
SEQRES 15 D 514 SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN GLY
SEQRES 16 D 514 ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP CYS
SEQRES 17 D 514 HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS ARG
SEQRES 18 D 514 PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN GLU
SEQRES 19 D 514 LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN LEU
SEQRES 20 D 514 TYR ASP MET PHE HIS THR ARG ASN SER LEU HIS ARG ARG
SEQRES 21 D 514 ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR MET
SEQRES 22 D 514 ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE GLU
SEQRES 23 D 514 ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER THR
SEQRES 24 D 514 ALA ILE ASP ASP MET GLU ALA TYR THR LYS LEU THR ASP
SEQRES 25 D 514 ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO LYS
SEQRES 26 D 514 LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU TYR
SEQRES 27 D 514 ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO THR
SEQRES 28 D 514 GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER LEU
SEQRES 29 D 514 PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU LEU
SEQRES 30 D 514 ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP VAL
SEQRES 31 D 514 ILE ASN MET ASP TYR GLY MET GLN GLU LYS ASN PRO ILE
SEQRES 32 D 514 ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN ARG
SEQRES 33 D 514 ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU LEU
SEQRES 34 D 514 PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR CYS
SEQRES 35 D 514 LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG GLN
SEQRES 36 D 514 TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR LYS
SEQRES 37 D 514 PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR PRO
SEQRES 38 D 514 GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN ASN
SEQRES 39 D 514 PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL GLN
SEQRES 40 D 514 LEU PHE LYS ASP ASP PRO MET
HET TTP A 701 29
HET DGT A 702 31
HET DTP A 703 30
HET MG A 704 1
HET TTP B 701 29
HET DGT B 702 31
HET MG B 703 1
HET DTP B 704 30
HET DTP C 701 30
HET MG C 702 1
HET DGT C 703 31
HET DGT C 704 31
HET MG D 701 1
HET DTP D 702 30
HET TTP D 703 29
HET DGT D 704 31
HETNAM TTP THYMIDINE-5'-TRIPHOSPHATE
HETNAM DGT 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE
HETNAM DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 5 TTP 3(C10 H17 N2 O14 P3)
FORMUL 6 DGT 5(C10 H16 N5 O13 P3)
FORMUL 7 DTP 4(C10 H16 N5 O12 P3)
FORMUL 8 MG 4(MG 2+)
FORMUL 21 HOH *32(H2 O)
HELIX 1 AA1 HIS A 129 ASP A 137 1 9
HELIX 2 AA2 THR A 138 ARG A 143 1 6
HELIX 3 AA3 LEU A 144 ILE A 147 5 4
HELIX 4 AA4 LEU A 150 VAL A 156 5 7
HELIX 5 AA5 ASN A 163 GLN A 186 1 24
HELIX 6 AA6 PRO A 187 GLN A 190 5 4
HELIX 7 AA7 SER A 192 ARG A 206 1 15
HELIX 8 AA8 SER A 214 ARG A 220 1 7
HELIX 9 AA9 ARG A 220 ARG A 226 1 7
HELIX 10 AB1 THR A 232 ASN A 248 1 17
HELIX 11 AB2 GLY A 249 TYR A 257 1 9
HELIX 12 AB3 ILE A 260 GLY A 274 1 15
HELIX 13 AB4 PRO A 291 ILE A 300 5 10
HELIX 14 AB5 ASP A 309 GLY A 324 1 16
HELIX 15 AB6 ASP A 330 PHE A 337 1 8
HELIX 16 AB7 GLU A 355 ALA A 373 1 19
HELIX 17 AB8 HIS A 376 ASP A 394 1 19
HELIX 18 AB9 ALA A 402 GLY A 404 5 3
HELIX 19 AC1 THR A 411 ASP A 414 5 4
HELIX 20 AC2 ASP A 415 THR A 420 1 6
HELIX 21 AC3 LYS A 421 THR A 423 5 3
HELIX 22 AC4 ASP A 424 SER A 433 1 10
HELIX 23 AC5 ASP A 435 LYS A 437 5 3
HELIX 24 AC6 LEU A 438 ARG A 451 1 14
HELIX 25 AC7 LYS A 469 GLU A 474 5 6
HELIX 26 AC8 SER A 475 ALA A 483 1 9
HELIX 27 AC9 LYS A 494 GLU A 496 5 3
HELIX 28 AD1 ASN A 513 VAL A 518 5 6
HELIX 29 AD2 THR A 533 VAL A 537 5 5
HELIX 30 AD3 ASP A 558 ASN A 577 1 20
HELIX 31 AD4 ASP A 583 ALA A 588 1 6
HELIX 32 AD5 ILE A 591 LYS A 595 5 5
HELIX 33 AD6 HIS B 129 ASP B 137 1 9
HELIX 34 AD7 THR B 138 ARG B 143 1 6
HELIX 35 AD8 LEU B 144 ILE B 147 5 4
HELIX 36 AD9 LEU B 150 VAL B 156 5 7
HELIX 37 AE1 ASN B 163 GLN B 186 1 24
HELIX 38 AE2 PRO B 187 GLN B 190 5 4
HELIX 39 AE3 SER B 192 ARG B 206 1 15
HELIX 40 AE4 SER B 214 ARG B 220 1 7
HELIX 41 AE5 ARG B 220 ARG B 226 1 7
HELIX 42 AE6 THR B 232 ASN B 248 1 17
HELIX 43 AE7 GLY B 249 TYR B 257 1 9
HELIX 44 AE8 ILE B 260 GLY B 274 1 15
HELIX 45 AE9 PRO B 291 ILE B 300 5 10
HELIX 46 AF1 ASP B 309 GLY B 324 1 16
HELIX 47 AF2 ASP B 330 PHE B 337 1 8
HELIX 48 AF3 GLU B 355 ALA B 373 1 19
HELIX 49 AF4 HIS B 376 ASP B 394 1 19
HELIX 50 AF5 ALA B 402 GLY B 404 5 3
HELIX 51 AF6 THR B 411 ASP B 414 5 4
HELIX 52 AF7 ASP B 415 THR B 420 1 6
HELIX 53 AF8 LYS B 421 THR B 423 5 3
HELIX 54 AF9 ASP B 424 SER B 433 1 10
HELIX 55 AG1 ASP B 435 LYS B 437 5 3
HELIX 56 AG2 LEU B 438 TYR B 450 1 13
HELIX 57 AG3 LYS B 469 GLU B 474 5 6
HELIX 58 AG4 SER B 475 ALA B 483 1 9
HELIX 59 AG5 LYS B 494 GLU B 496 5 3
HELIX 60 AG6 ASN B 513 VAL B 518 5 6
HELIX 61 AG7 THR B 533 VAL B 537 5 5
HELIX 62 AG8 ASP B 558 ASN B 577 1 20
HELIX 63 AG9 ASP B 583 ALA B 588 1 6
HELIX 64 AH1 ILE B 591 LYS B 595 5 5
HELIX 65 AH2 HIS C 129 ASP C 137 1 9
HELIX 66 AH3 THR C 138 ARG C 143 1 6
HELIX 67 AH4 LEU C 144 ILE C 147 5 4
HELIX 68 AH5 LEU C 150 VAL C 156 5 7
HELIX 69 AH6 ASN C 163 GLN C 186 1 24
HELIX 70 AH7 PRO C 187 GLN C 190 5 4
HELIX 71 AH8 SER C 192 ARG C 206 1 15
HELIX 72 AH9 SER C 214 ARG C 220 1 7
HELIX 73 AI1 ARG C 220 ARG C 226 1 7
HELIX 74 AI2 THR C 232 ASN C 248 1 17
HELIX 75 AI3 GLY C 249 TYR C 257 1 9
HELIX 76 AI4 ILE C 260 GLY C 274 1 15
HELIX 77 AI5 PRO C 291 ILE C 300 5 10
HELIX 78 AI6 ASP C 309 GLY C 324 1 16
HELIX 79 AI7 ASP C 330 PHE C 337 1 8
HELIX 80 AI8 GLU C 355 ALA C 373 1 19
HELIX 81 AI9 HIS C 376 ASP C 394 1 19
HELIX 82 AJ1 ALA C 402 GLY C 404 5 3
HELIX 83 AJ2 THR C 411 ASP C 414 5 4
HELIX 84 AJ3 ASP C 415 THR C 420 1 6
HELIX 85 AJ4 LYS C 421 THR C 423 5 3
HELIX 86 AJ5 ASP C 424 SER C 433 1 10
HELIX 87 AJ6 ASP C 435 LYS C 437 5 3
HELIX 88 AJ7 LEU C 438 ARG C 451 1 14
HELIX 89 AJ8 LYS C 469 GLU C 474 5 6
HELIX 90 AJ9 SER C 475 ALA C 483 1 9
HELIX 91 AK1 LYS C 494 GLU C 496 5 3
HELIX 92 AK2 ASN C 513 VAL C 518 5 6
HELIX 93 AK3 THR C 533 VAL C 537 5 5
HELIX 94 AK4 ASP C 558 ASN C 577 1 20
HELIX 95 AK5 ASP C 583 ALA C 588 1 6
HELIX 96 AK6 ILE C 591 LYS C 595 5 5
HELIX 97 AK7 HIS D 129 ASP D 137 1 9
HELIX 98 AK8 THR D 138 ARG D 143 1 6
HELIX 99 AK9 LEU D 144 ILE D 147 5 4
HELIX 100 AL1 LEU D 150 VAL D 156 5 7
HELIX 101 AL2 ASN D 163 GLN D 186 1 24
HELIX 102 AL3 PRO D 187 GLN D 190 5 4
HELIX 103 AL4 SER D 192 ARG D 206 1 15
HELIX 104 AL5 SER D 214 ARG D 220 1 7
HELIX 105 AL6 ARG D 220 ARG D 226 1 7
HELIX 106 AL7 THR D 232 ASN D 248 1 17
HELIX 107 AL8 GLY D 249 TYR D 257 1 9
HELIX 108 AL9 ILE D 260 GLY D 274 1 15
HELIX 109 AM1 PRO D 291 ILE D 300 5 10
HELIX 110 AM2 ASP D 309 GLY D 324 1 16
HELIX 111 AM3 ASP D 330 PHE D 337 1 8
HELIX 112 AM4 GLU D 355 ALA D 373 1 19
HELIX 113 AM5 HIS D 376 ASP D 394 1 19
HELIX 114 AM6 ALA D 402 GLY D 404 5 3
HELIX 115 AM7 THR D 411 ASP D 414 5 4
HELIX 116 AM8 ASP D 415 THR D 420 1 6
HELIX 117 AM9 LYS D 421 THR D 423 5 3
HELIX 118 AN1 ASP D 424 SER D 433 1 10
HELIX 119 AN2 ASP D 435 LYS D 437 5 3
HELIX 120 AN3 LEU D 438 ARG D 451 1 14
HELIX 121 AN4 LYS D 469 GLU D 474 5 6
HELIX 122 AN5 SER D 475 ALA D 483 1 9
HELIX 123 AN6 LYS D 494 GLU D 496 5 3
HELIX 124 AN7 ASN D 513 VAL D 518 5 6
HELIX 125 AN8 THR D 533 VAL D 537 5 5
HELIX 126 AN9 ASP D 558 ASN D 577 1 20
HELIX 127 AO1 ASP D 583 ALA D 588 1 6
HELIX 128 AO2 ILE D 591 LYS D 595 5 5
SHEET 1 AA1 2 LYS A 116 ASP A 120 0
SHEET 2 AA1 2 GLY A 124 LEU A 128 -1 O LEU A 128 N LYS A 116
SHEET 1 AA2 4 ALA A 338 VAL A 343 0
SHEET 2 AA2 4 GLU A 346 ARG A 352 -1 O CYS A 350 N ARG A 339
SHEET 3 AA2 4 PHE A 520 TYR A 521 1 O TYR A 521 N ALA A 351
SHEET 4 AA2 4 ALA A 529 ILE A 530 -1 O ILE A 530 N PHE A 520
SHEET 1 AA3 2 ILE A 399 THR A 400 0
SHEET 2 AA3 2 LYS A 406 TYR A 407 -1 O TYR A 407 N ILE A 399
SHEET 1 AA4 3 LYS A 455 THR A 460 0
SHEET 2 AA4 3 ALA A 546 CYS A 554 -1 O VAL A 552 N VAL A 457
SHEET 3 AA4 3 PHE A 498 ASP A 506 -1 N ILE A 499 O TYR A 553
SHEET 1 AA5 2 LYS B 116 ASP B 120 0
SHEET 2 AA5 2 GLY B 124 LEU B 128 -1 O LEU B 128 N LYS B 116
SHEET 1 AA6 4 ARG B 339 VAL B 343 0
SHEET 2 AA6 4 GLU B 346 ARG B 352 -1 O CYS B 350 N ARG B 339
SHEET 3 AA6 4 PHE B 520 TYR B 521 1 O TYR B 521 N ALA B 351
SHEET 4 AA6 4 ALA B 529 ILE B 530 -1 O ILE B 530 N PHE B 520
SHEET 1 AA7 2 ILE B 399 THR B 400 0
SHEET 2 AA7 2 LYS B 406 TYR B 407 -1 O TYR B 407 N ILE B 399
SHEET 1 AA8 3 LYS B 455 THR B 460 0
SHEET 2 AA8 3 ALA B 546 CYS B 554 -1 O VAL B 552 N VAL B 457
SHEET 3 AA8 3 PHE B 498 ASP B 506 -1 N ILE B 503 O LEU B 549
SHEET 1 AA9 2 LYS C 116 ASP C 120 0
SHEET 2 AA9 2 GLY C 124 LEU C 128 -1 O LEU C 128 N LYS C 116
SHEET 1 AB1 4 ALA C 338 VAL C 343 0
SHEET 2 AB1 4 GLU C 346 ARG C 352 -1 O CYS C 350 N ARG C 339
SHEET 3 AB1 4 PHE C 520 TYR C 521 1 O TYR C 521 N ALA C 351
SHEET 4 AB1 4 ALA C 529 ILE C 530 -1 O ILE C 530 N PHE C 520
SHEET 1 AB2 2 ILE C 399 THR C 400 0
SHEET 2 AB2 2 LYS C 406 TYR C 407 -1 O TYR C 407 N ILE C 399
SHEET 1 AB3 3 LYS C 455 THR C 460 0
SHEET 2 AB3 3 ALA C 546 CYS C 554 -1 O VAL C 552 N VAL C 457
SHEET 3 AB3 3 PHE C 498 ASP C 506 -1 N ILE C 503 O LEU C 549
SHEET 1 AB4 2 LYS D 116 ASP D 120 0
SHEET 2 AB4 2 GLY D 124 LEU D 128 -1 O LEU D 128 N LYS D 116
SHEET 1 AB5 5 ALA D 338 VAL D 343 0
SHEET 2 AB5 5 GLU D 346 ARG D 352 -1 O CYS D 350 N ARG D 339
SHEET 3 AB5 5 PHE D 520 CYS D 522 1 O TYR D 521 N ALA D 351
SHEET 4 AB5 5 ALA D 525 ILE D 530 -1 O ILE D 530 N PHE D 520
SHEET 5 AB5 5 ALA D 338 VAL D 343 1 N GLU D 342 O ASN D 527
SHEET 1 AB6 2 ILE D 399 THR D 400 0
SHEET 2 AB6 2 LYS D 406 TYR D 407 -1 O TYR D 407 N ILE D 399
SHEET 1 AB7 3 LYS D 455 THR D 460 0
SHEET 2 AB7 3 ALA D 546 CYS D 554 -1 O VAL D 552 N VAL D 457
SHEET 3 AB7 3 PHE D 498 ASP D 506 -1 N ILE D 503 O LEU D 549
LINK O1B DGT A 702 MG MG D 701 1555 1555 1.95
LINK O1A DGT A 702 MG MG D 701 1555 1555 1.97
LINK O3G DTP A 703 MG MG B 703 1555 1555 1.85
LINK O2B DTP A 703 MG MG B 703 1555 1555 1.88
LINK MG MG A 704 O1B DTP B 704 1555 1555 2.02
LINK MG MG A 704 O2G DTP B 704 1555 1555 1.89
LINK MG MG A 704 O HOH B 803 1555 1555 1.96
LINK MG MG A 704 O3G DGT D 704 1555 1555 1.72
LINK MG MG A 704 O1B DGT D 704 1555 1555 2.24
LINK MG MG A 704 O2A DGT D 704 1555 1555 1.87
LINK O HOH A 808 MG MG B 703 1555 1555 1.98
LINK O2B DGT B 702 MG MG C 702 1555 1555 2.13
LINK O2A DGT B 702 MG MG C 702 1555 1555 1.99
LINK MG MG B 703 O2B DGT C 704 1555 1555 2.00
LINK MG MG B 703 O3G DGT C 704 1555 1555 2.06
LINK MG MG B 703 O1A DGT C 704 1555 1555 1.77
LINK O3G DTP C 701 MG MG D 701 1555 1555 1.94
LINK O2B DTP C 701 MG MG D 701 1555 1555 2.01
LINK MG MG C 702 O1B DTP D 702 1555 1555 1.96
LINK MG MG C 702 O3G DTP D 702 1555 1555 1.90
LINK MG MG C 702 O HOH D 805 1555 1555 1.79
LINK O HOH C 802 MG MG D 701 1555 1555 1.84
SITE 1 AC1 15 GLN A 149 ARG A 164 ARG A 206 ASN A 207
SITE 2 AC1 15 HIS A 210 HIS A 215 ASP A 311 LYS A 312
SITE 3 AC1 15 TYR A 315 ASP A 319 ARG A 366 TYR A 374
SITE 4 AC1 15 GLN A 375 HOH A 813 HOH A 816
SITE 1 AC2 17 TYR A 155 VAL A 156 VAL A 378 ARG A 451
SITE 2 AC2 17 LYS A 455 HOH A 807 LYS C 523 DTP C 701
SITE 3 AC2 17 HOH C 802 LYS D 116 VAL D 117 ILE D 118
SITE 4 AC2 17 ASP D 137 GLN D 142 ARG D 145 PHE D 165
SITE 5 AC2 17 MG D 701
SITE 1 AC3 17 ARG A 333 ARG A 352 LYS A 354 ASN A 358
SITE 2 AC3 17 LYS A 523 HOH A 808 HOH A 809 VAL B 117
SITE 3 AC3 17 ASN B 119 HIS B 125 MG B 703 VAL C 156
SITE 4 AC3 17 PHE C 157 ARG C 372 HIS C 376 LYS C 377
SITE 5 AC3 17 DGT C 704
SITE 1 AC4 4 LYS A 116 DTP B 704 HOH B 803 DGT D 704
SITE 1 AC5 15 GLN B 149 LEU B 150 ARG B 164 ARG B 206
SITE 2 AC5 15 HIS B 210 HIS B 215 HIS B 233 ASP B 311
SITE 3 AC5 15 LYS B 312 TYR B 315 ASP B 319 ARG B 366
SITE 4 AC5 15 TYR B 374 GLN B 375 HOH B 802
SITE 1 AC6 16 TYR B 155 VAL B 156 VAL B 378 ARG B 451
SITE 2 AC6 16 LYS B 455 LYS C 116 VAL C 117 ILE C 118
SITE 3 AC6 16 ASP C 137 GLN C 142 ARG C 145 PHE C 165
SITE 4 AC6 16 MG C 702 LYS D 523 DTP D 702 HOH D 805
SITE 1 AC7 5 LYS A 523 DTP A 703 HOH A 808 LYS B 116
SITE 2 AC7 5 DGT C 704
SITE 1 AC8 16 VAL A 117 ASN A 119 MG A 704 ARG B 333
SITE 2 AC8 16 ARG B 352 LYS B 354 ASN B 358 LYS B 523
SITE 3 AC8 16 HOH B 803 HOH B 804 VAL D 156 PHE D 157
SITE 4 AC8 16 ARG D 372 HIS D 376 LYS D 377 DGT D 704
SITE 1 AC9 17 VAL A 156 PHE A 157 ARG A 372 HIS A 376
SITE 2 AC9 17 LYS A 377 DGT A 702 ARG C 333 PHE C 337
SITE 3 AC9 17 ARG C 352 LYS C 354 ASN C 358 LYS C 523
SITE 4 AC9 17 HOH C 802 HOH C 804 VAL D 117 ASN D 119
SITE 5 AC9 17 MG D 701
SITE 1 AD1 4 DGT B 702 LYS C 116 DTP D 702 HOH D 805
SITE 1 AD2 14 GLN C 149 LEU C 150 ARG C 164 ARG C 206
SITE 2 AD2 14 HIS C 210 HIS C 215 HIS C 233 ASP C 311
SITE 3 AD2 14 LYS C 312 TYR C 315 ASP C 319 ARG C 366
SITE 4 AD2 14 TYR C 374 GLN C 375
SITE 1 AD3 17 LYS A 523 DTP A 703 HOH A 808 LYS B 116
SITE 2 AD3 17 VAL B 117 ILE B 118 ASP B 137 GLN B 142
SITE 3 AD3 17 ARG B 145 PHE B 165 MG B 703 TYR C 155
SITE 4 AD3 17 VAL C 156 VAL C 378 ARG C 451 LYS C 455
SITE 5 AD3 17 HOH C 805
SITE 1 AD4 5 DGT A 702 LYS C 523 DTP C 701 HOH C 802
SITE 2 AD4 5 LYS D 116
SITE 1 AD5 17 VAL B 156 PHE B 157 ARG B 372 HIS B 376
SITE 2 AD5 17 LYS B 377 VAL B 378 DGT B 702 VAL C 117
SITE 3 AD5 17 ASN C 119 MG C 702 ARG D 333 PHE D 337
SITE 4 AD5 17 ARG D 352 LYS D 354 ASN D 358 LYS D 523
SITE 5 AD5 17 HOH D 805
SITE 1 AD6 15 GLN D 149 LEU D 150 ARG D 164 ARG D 206
SITE 2 AD6 15 HIS D 210 HIS D 215 HIS D 233 ASP D 311
SITE 3 AD6 15 LYS D 312 TYR D 315 ASP D 319 ARG D 366
SITE 4 AD6 15 HIS D 370 TYR D 374 GLN D 375
SITE 1 AD7 17 LYS A 116 VAL A 117 ILE A 118 ASP A 137
SITE 2 AD7 17 GLN A 142 ARG A 145 PHE A 165 MG A 704
SITE 3 AD7 17 LYS B 523 DTP B 704 HOH B 803 TYR D 155
SITE 4 AD7 17 VAL D 156 VAL D 378 ARG D 451 LYS D 455
SITE 5 AD7 17 HOH D 806
CRYST1 82.587 140.808 96.900 90.00 114.94 90.00 P 1 21 1 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 0.012108 0.000000 0.005630 0.00000
SCALE2 0.000000 0.007102 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011381 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
