HEADER TRANSFERASE 24-MAR-18 6G38
TITLE CRYSTAL STRUCTURE OF HASPIN IN COMPLEX WITH TUBERCIDIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE HASPIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GERM CELL-SPECIFIC GENE 2 PROTEIN,H-HASPIN,HAPLOID GERM
COMPND 5 CELL-SPECIFIC NUCLEAR PROTEIN KINASE;
COMPND 6 EC: 2.7.11.1;
COMPND 7 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: HASPIN, GSG2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS KINASE, INHIBITORS, SLOW OFF-RATE, KINETICS, HALOGEN, STRUCTURAL
KEYWDS 2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HEROVEN,A.CHAIKUAD,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,S.KNAPP,
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 17-JAN-24 6G38 1 REMARK
REVDAT 3 13-JUN-18 6G38 1 JRNL
REVDAT 2 16-MAY-18 6G38 1 JRNL
REVDAT 1 18-APR-18 6G38 0
JRNL AUTH C.HEROVEN,V.GEORGI,G.K.GANOTRA,P.BRENNAN,F.WOLFREYS,
JRNL AUTH 2 R.C.WADE,A.E.FERNANDEZ-MONTALVAN,A.CHAIKUAD,S.KNAPP
JRNL TITL HALOGEN-AROMATIC PI INTERACTIONS MODULATE INHIBITOR
JRNL TITL 2 RESIDENCE TIMES.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 57 7220 2018
JRNL REFN ESSN 1521-3773
JRNL PMID 29601130
JRNL DOI 10.1002/ANIE.201801666
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 80839
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4169
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) : 1.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5984
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 253
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2579
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 269
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.58000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : 0.55000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.797
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.974
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2701 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2545 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3662 ; 1.537 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5873 ; 0.967 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 334 ; 6.391 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 116 ;33.711 ;24.310
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 469 ;10.957 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;16.086 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 415 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3056 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 617 ; 0.002 ; 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): 1315 ; 1.671 ; 1.847
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1314 ; 1.583 ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1646 ; 1.949 ; 2.773
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1646 ; 1.949 ; 2.773
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1386 ; 2.601 ; 2.194
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1382 ; 2.510 ; 2.187
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2007 ; 2.902 ; 3.158
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3198 ; 3.024 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3199 ; 3.024 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2658 ; 3.679 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2599 ;10.882 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 31 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): 43.1357 44.3092 15.5981
REMARK 3 T TENSOR
REMARK 3 T11: 0.0017 T22: 0.0127
REMARK 3 T33: 0.0090 T12: 0.0017
REMARK 3 T13: -0.0001 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0578 L22: 0.1385
REMARK 3 L33: 0.0855 L12: 0.0086
REMARK 3 L13: -0.0019 L23: -0.0534
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: -0.0040 S13: -0.0066
REMARK 3 S21: 0.0040 S22: -0.0009 S23: 0.0041
REMARK 3 S31: 0.0074 S32: -0.0002 S33: -0.0018
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 : A 167 A 357
REMARK 3 ORIGIN FOR THE GROUP (A): 58.4641 58.8214 3.2821
REMARK 3 T TENSOR
REMARK 3 T11: 0.0026 T22: 0.0157
REMARK 3 T33: 0.0077 T12: 0.0005
REMARK 3 T13: 0.0043 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.1411 L22: 0.1210
REMARK 3 L33: 0.1068 L12: 0.0154
REMARK 3 L13: -0.0112 L23: 0.0123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: 0.0064 S13: 0.0005
REMARK 3 S21: -0.0064 S22: 0.0034 S23: -0.0140
REMARK 3 S31: -0.0023 S32: 0.0146 S33: -0.0023
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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
REMARK 4
REMARK 4 6G38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.0-6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92144
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 24.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4OUC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 51-63% MPD AND 0.1M SPG BUFFER, PH 6.0
REMARK 280 -6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 39.28000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.01000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.38000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.01000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.28000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.38000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 442
REMARK 465 HIS A 443
REMARK 465 HIS A 444
REMARK 465 HIS A 445
REMARK 465 HIS A 446
REMARK 465 HIS A 447
REMARK 465 HIS A 448
REMARK 465 SER A 449
REMARK 465 SER A 450
REMARK 465 GLY A 451
REMARK 465 VAL A 452
REMARK 465 ASP A 453
REMARK 465 LEU A 454
REMARK 465 GLY A 455
REMARK 465 THR A 456
REMARK 465 GLU A 457
REMARK 465 ASN A 458
REMARK 465 LEU A 459
REMARK 465 TYR A 460
REMARK 465 PHE A 461
REMARK 465 GLN A 462
REMARK 465 SER A 463
REMARK 465 MET A 464
REMARK 465 GLY A 465
REMARK 465 GLU A 466
REMARK 465 CYS A 467
REMARK 465 SER A 468
REMARK 465 GLN A 469
REMARK 465 LYS A 470
REMARK 465 GLY A 471
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 ARG A 486 NE CZ NH1 NH2
REMARK 470 GLU A 530 CD OE1 OE2
REMARK 470 LYS A 540 CE NZ
REMARK 470 LYS A 575 CE NZ
REMARK 470 LYS A 584 NZ
REMARK 470 LYS A 659 CD CE NZ
REMARK 470 LYS A 663 CD CE NZ
REMARK 470 LYS A 664 CE NZ
REMARK 470 LYS A 672 CE NZ
REMARK 470 GLU A 708 CG CD OE1 OE2
REMARK 470 LYS A 727 CE NZ
REMARK 470 ASN A 763 CB CG OD1 ND2
REMARK 470 THR A 764 OG1 CG2
REMARK 470 LYS A 768 CD CE NZ
REMARK 470 GLN A 769 CG CD OE1 NE2
REMARK 470 GLN A 793 OE1 NE2
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 ARG A 732 NE - CZ - NH1 ANGL. DEV. = 3.1 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 GLU A 516 -4.47 74.51
REMARK 500 PHE A 556 -150.47 -93.29
REMARK 500 ASP A 649 47.52 -155.45
REMARK 500 LEU A 650 55.17 -91.10
REMARK 500 ASP A 687 90.96 73.49
REMARK 500 ASN A 763 45.82 -144.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TBN A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6G34 RELATED DB: PDB
DBREF 6G38 A 465 798 UNP Q8TF76 HASP_HUMAN 465 798
SEQADV 6G38 MET A 442 UNP Q8TF76 INITIATING METHIONINE
SEQADV 6G38 HIS A 443 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 HIS A 444 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 HIS A 445 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 HIS A 446 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 HIS A 447 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 HIS A 448 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 SER A 449 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 SER A 450 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 GLY A 451 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 VAL A 452 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 ASP A 453 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 LEU A 454 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 GLY A 455 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 THR A 456 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 GLU A 457 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 ASN A 458 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 LEU A 459 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 TYR A 460 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 PHE A 461 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 GLN A 462 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 SER A 463 UNP Q8TF76 EXPRESSION TAG
SEQADV 6G38 MET A 464 UNP Q8TF76 EXPRESSION TAG
SEQRES 1 A 357 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 357 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY GLU CYS
SEQRES 3 A 357 SER GLN LYS GLY PRO VAL PRO PHE SER HIS CYS LEU PRO
SEQRES 4 A 357 THR GLU LYS LEU GLN ARG CYS GLU LYS ILE GLY GLU GLY
SEQRES 5 A 357 VAL PHE GLY GLU VAL PHE GLN THR ILE ALA ASP HIS THR
SEQRES 6 A 357 PRO VAL ALA ILE LYS ILE ILE ALA ILE GLU GLY PRO ASP
SEQRES 7 A 357 LEU VAL ASN GLY SER HIS GLN LYS THR PHE GLU GLU ILE
SEQRES 8 A 357 LEU PRO GLU ILE ILE ILE SER LYS GLU LEU SER LEU LEU
SEQRES 9 A 357 SER GLY GLU VAL CYS ASN ARG THR GLU GLY PHE ILE GLY
SEQRES 10 A 357 LEU ASN SER VAL HIS CYS VAL GLN GLY SER TYR PRO PRO
SEQRES 11 A 357 LEU LEU LEU LYS ALA TRP ASP HIS TYR ASN SER THR LYS
SEQRES 12 A 357 GLY SER ALA ASN ASP ARG PRO ASP PHE PHE LYS ASP ASP
SEQRES 13 A 357 GLN LEU PHE ILE VAL LEU GLU PHE GLU PHE GLY GLY ILE
SEQRES 14 A 357 ASP LEU GLU GLN MET ARG THR LYS LEU SER SER LEU ALA
SEQRES 15 A 357 THR ALA LYS SER ILE LEU HIS GLN LEU THR ALA SER LEU
SEQRES 16 A 357 ALA VAL ALA GLU ALA SER LEU ARG PHE GLU HIS ARG ASP
SEQRES 17 A 357 LEU HIS TRP GLY ASN VAL LEU LEU LYS LYS THR SER LEU
SEQRES 18 A 357 LYS LYS LEU HIS TYR THR LEU ASN GLY LYS SER SER THR
SEQRES 19 A 357 ILE PRO SER CYS GLY LEU GLN VAL SER ILE ILE ASP TYR
SEQRES 20 A 357 THR LEU SER ARG LEU GLU ARG ASP GLY ILE VAL VAL PHE
SEQRES 21 A 357 CYS ASP VAL SER MET ASP GLU ASP LEU PHE THR GLY ASP
SEQRES 22 A 357 GLY ASP TYR GLN PHE ASP ILE TYR ARG LEU MET LYS LYS
SEQRES 23 A 357 GLU ASN ASN ASN ARG TRP GLY GLU TYR HIS PRO TYR SER
SEQRES 24 A 357 ASN VAL LEU TRP LEU HIS TYR LEU THR ASP LYS MET LEU
SEQRES 25 A 357 LYS GLN MET THR PHE LYS THR LYS CYS ASN THR PRO ALA
SEQRES 26 A 357 MET LYS GLN ILE LYS ARG LYS ILE GLN GLU PHE HIS ARG
SEQRES 27 A 357 THR MET LEU ASN PHE SER SER ALA THR ASP LEU LEU CYS
SEQRES 28 A 357 GLN HIS SER LEU PHE LYS
HET TBN A 800 19
HET DMS A 801 4
HET EPE A 802 15
HET PO4 A 803 5
HETNAM TBN '2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-
HETNAM 2 TBN HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM PO4 PHOSPHATE ION
HETSYN TBN 7-DEAZAADENOSINE
HETSYN EPE HEPES
FORMUL 2 TBN C11 H14 N4 O4
FORMUL 3 DMS C2 H6 O S
FORMUL 4 EPE C8 H18 N2 O4 S
FORMUL 5 PO4 O4 P 3-
FORMUL 6 HOH *269(H2 O)
HELIX 1 AA1 PRO A 474 LEU A 479 1 6
HELIX 2 AA2 PRO A 480 ARG A 486 1 7
HELIX 3 AA3 THR A 528 LEU A 545 1 18
HELIX 4 AA4 SER A 546 GLU A 548 5 3
HELIX 5 AA5 PRO A 570 LYS A 584 1 15
HELIX 6 AA6 SER A 621 ARG A 644 1 24
HELIX 7 AA7 GLU A 708 THR A 712 5 5
HELIX 8 AA8 ASP A 716 ASN A 730 1 15
HELIX 9 AA9 PRO A 738 GLN A 755 1 18
HELIX 10 AB1 THR A 764 MET A 781 1 18
HELIX 11 AB2 LEU A 782 PHE A 784 5 3
HELIX 12 AB3 SER A 786 HIS A 794 1 9
HELIX 13 AB4 SER A 795 LYS A 798 5 4
SHEET 1 AA1 5 GLU A 488 GLY A 493 0
SHEET 2 AA1 5 GLY A 496 ALA A 503 -1 O GLN A 500 N GLU A 488
SHEET 3 AA1 5 THR A 506 ILE A 515 -1 O ILE A 510 N PHE A 499
SHEET 4 AA1 5 LEU A 599 GLU A 606 -1 O PHE A 605 N ALA A 509
SHEET 5 AA1 5 LEU A 559 GLN A 566 -1 N HIS A 563 O VAL A 602
SHEET 1 AA2 3 ILE A 610 ASP A 611 0
SHEET 2 AA2 3 VAL A 655 LYS A 659 -1 O LEU A 657 N ILE A 610
SHEET 3 AA2 3 LEU A 681 ILE A 685 -1 O GLN A 682 N LYS A 658
SHEET 1 AA3 2 LYS A 664 LEU A 669 0
SHEET 2 AA3 2 LYS A 672 PRO A 677 -1 O ILE A 676 N LEU A 665
SHEET 1 AA4 2 LEU A 693 ARG A 695 0
SHEET 2 AA4 2 ILE A 698 VAL A 700 -1 O VAL A 700 N LEU A 693
SITE 1 AC1 17 ILE A 490 GLY A 491 ALA A 509 GLU A 606
SITE 2 AC1 17 PHE A 607 GLY A 608 GLY A 609 ASP A 611
SITE 3 AC1 17 GLY A 653 LEU A 656 ILE A 686 HOH A 832
SITE 4 AC1 17 HOH A 844 HOH A 878 HOH A 906 HOH A 914
SITE 5 AC1 17 HOH A 951
SITE 1 AC2 4 TYR A 667 LYS A 672 SER A 674 HOH A 952
SITE 1 AC3 6 GLU A 728 ASN A 730 HIS A 737 LEU A 782
SITE 2 AC3 6 ASN A 783 PHE A 784
SITE 1 AC4 3 PRO A 571 ILE A 698 HOH A 973
CRYST1 78.560 78.760 80.020 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012729 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012697 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012497 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
