HEADER CHAPERONE 01-NOV-13 4NFT
TITLE CRYSTAL STRUCTURE OF HUMAN LNKH2B-H2A.Z-ANP32E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H2B TYPE 2-E, HISTONE H2A.Z;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 34-126, 16-114;
COMPND 5 SYNONYM: HISTONE H2B-GL105, HISTONE H2B.Q, H2B/Q, H2A/Z;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CHIMERA OF H2B AND H2A.Z;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER
COMPND 10 E;
COMPND 11 CHAIN: E, F;
COMPND 12 FRAGMENT: UNP RESIDUES 185-232;
COMPND 13 SYNONYM: ANP32E, LANP-LIKE PROTEIN, LANP-L;
COMPND 14 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: H2BFQ, H2AZ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ANP32E;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HISTONE BINDING PROTEIN, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHAN,L.PAN,Z.MAO,W.WANG,J.SUN,Q.DONG,X.LIANG,X.DING,S.CHEN,L.DAI,
AUTHOR 2 Z.ZHANG,B.ZHU,Z.ZHOU
REVDAT 4 20-MAR-24 4NFT 1 SEQADV
REVDAT 3 16-AUG-17 4NFT 1 SOURCE REMARK
REVDAT 2 23-SEP-15 4NFT 1 JRNL
REVDAT 1 09-APR-14 4NFT 0
JRNL AUTH Z.MAO,L.PAN,W.WANG,J.SUN,S.SHAN,Q.DONG,X.LIANG,L.DAI,X.DING,
JRNL AUTH 2 S.CHEN,Z.ZHANG,B.ZHU,Z.ZHOU
JRNL TITL ANP32E, A HIGHER EUKARYOTIC HISTONE CHAPERONE DIRECTS
JRNL TITL 2 PREFERENTIAL RECOGNITION FOR H2A.Z
JRNL REF CELL RES. V. 24 389 2014
JRNL REFN ISSN 1001-0602
JRNL PMID 24613878
JRNL DOI 10.1038/CR.2014.30
REMARK 2
REMARK 2 RESOLUTION. 2.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 28845
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1478
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.7999 - 5.8001 0.90 2332 124 0.1904 0.2006
REMARK 3 2 5.8001 - 4.6059 0.99 2516 142 0.1977 0.2671
REMARK 3 3 4.6059 - 4.0243 0.99 2531 132 0.1804 0.2413
REMARK 3 4 4.0243 - 3.6567 0.99 2533 121 0.1989 0.2697
REMARK 3 5 3.6567 - 3.3947 0.99 2518 114 0.2088 0.2447
REMARK 3 6 3.3947 - 3.1947 0.99 2495 153 0.2312 0.2764
REMARK 3 7 3.1947 - 3.0347 0.99 2526 146 0.2483 0.3123
REMARK 3 8 3.0347 - 2.9027 1.00 2506 146 0.2502 0.2794
REMARK 3 9 2.9027 - 2.7910 0.99 2505 140 0.2687 0.3725
REMARK 3 10 2.7910 - 2.6947 1.00 2511 126 0.2853 0.3777
REMARK 3 11 2.6947 - 2.6104 0.95 2394 134 0.3000 0.3222
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 46.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 5866
REMARK 3 ANGLE : 1.081 7888
REMARK 3 CHIRALITY : 0.071 924
REMARK 3 PLANARITY : 0.005 988
REMARK 3 DIHEDRAL : 17.635 2212
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NFT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083148.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29217
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM THIOCYANATE, 20%(W/V)
REMARK 280 POLYETHYLENE GLYCOL 3350, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.20600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.14850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.20600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.14850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 ALA A 96
REMARK 465 VAL A 97
REMARK 465 GLY A 187
REMARK 465 GLY A 188
REMARK 465 VAL A 189
REMARK 465 ILE A 190
REMARK 465 PRO A 191
REMARK 465 HIS A 192
REMARK 465 ILE A 193
REMARK 465 SER A 194
REMARK 465 GLY A 195
REMARK 465 SER A 196
REMARK 465 GLY A 197
REMARK 465 GLY A 198
REMARK 465 SER A 199
REMARK 465 GLY A 200
REMARK 465 GLY A 201
REMARK 465 GLY A 202
REMARK 465 LEU A 203
REMARK 465 VAL A 204
REMARK 465 PRO A 205
REMARK 465 ARG A 206
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 ALA B 96
REMARK 465 VAL B 97
REMARK 465 GLY B 187
REMARK 465 GLY B 188
REMARK 465 VAL B 189
REMARK 465 ILE B 190
REMARK 465 PRO B 191
REMARK 465 HIS B 192
REMARK 465 ILE B 193
REMARK 465 SER B 194
REMARK 465 GLY B 195
REMARK 465 SER B 196
REMARK 465 GLY B 197
REMARK 465 GLY B 198
REMARK 465 SER B 199
REMARK 465 GLY B 200
REMARK 465 GLY B 201
REMARK 465 GLY B 202
REMARK 465 LEU B 203
REMARK 465 VAL B 204
REMARK 465 PRO B 205
REMARK 465 ARG B 206
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 LYS C 3
REMARK 465 GLU C 4
REMARK 465 LYS C 94
REMARK 465 LYS C 95
REMARK 465 ALA C 96
REMARK 465 VAL C 97
REMARK 465 GLY C 187
REMARK 465 GLY C 188
REMARK 465 VAL C 189
REMARK 465 ILE C 190
REMARK 465 PRO C 191
REMARK 465 HIS C 192
REMARK 465 ILE C 193
REMARK 465 SER C 194
REMARK 465 GLY C 195
REMARK 465 SER C 196
REMARK 465 GLY C 197
REMARK 465 GLY C 198
REMARK 465 SER C 199
REMARK 465 GLY C 200
REMARK 465 GLY C 201
REMARK 465 GLY C 202
REMARK 465 LEU C 203
REMARK 465 VAL C 204
REMARK 465 PRO C 205
REMARK 465 ARG C 206
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 LYS D 3
REMARK 465 GLU D 4
REMARK 465 LYS D 94
REMARK 465 LYS D 95
REMARK 465 ALA D 96
REMARK 465 VAL D 97
REMARK 465 GLY D 187
REMARK 465 GLY D 188
REMARK 465 VAL D 189
REMARK 465 ILE D 190
REMARK 465 PRO D 191
REMARK 465 HIS D 192
REMARK 465 ILE D 193
REMARK 465 SER D 194
REMARK 465 GLY D 195
REMARK 465 SER D 196
REMARK 465 GLY D 197
REMARK 465 GLY D 198
REMARK 465 SER D 199
REMARK 465 GLY D 200
REMARK 465 GLY D 201
REMARK 465 GLY D 202
REMARK 465 LEU D 203
REMARK 465 VAL D 204
REMARK 465 PRO D 205
REMARK 465 ARG D 206
REMARK 465 GLY E -27
REMARK 465 SER E -26
REMARK 465 HIS E -25
REMARK 465 MET E -24
REMARK 465 GLU E -23
REMARK 465 GLU E -22
REMARK 465 GLU E -21
REMARK 465 GLU E -20
REMARK 465 GLU E -19
REMARK 465 GLU E -18
REMARK 465 GLU E -17
REMARK 465 GLU E -16
REMARK 465 GLU E -15
REMARK 465 GLU E -14
REMARK 465 ASP E -13
REMARK 465 GLU E -12
REMARK 465 ASP E -11
REMARK 465 GLU E -10
REMARK 465 ASP E -9
REMARK 465 GLU E -8
REMARK 465 ASP E -7
REMARK 465 GLU E -6
REMARK 465 ASP E -5
REMARK 465 GLU E -4
REMARK 465 ALA E -3
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 GLU E 0
REMARK 465 LEU E 1
REMARK 465 GLY E 2
REMARK 465 GLU E 3
REMARK 465 GLY E 4
REMARK 465 GLU E 5
REMARK 465 GLU E 17
REMARK 465 ILE E 18
REMARK 465 GLN E 19
REMARK 465 ASP E 20
REMARK 465 GLU E 21
REMARK 465 GLU E 22
REMARK 465 ASP E 23
REMARK 465 ASP E 24
REMARK 465 GLY F -27
REMARK 465 SER F -26
REMARK 465 HIS F -25
REMARK 465 MET F -24
REMARK 465 GLU F -23
REMARK 465 GLU F -22
REMARK 465 GLU F -21
REMARK 465 GLU F -20
REMARK 465 GLU F -19
REMARK 465 GLU F -18
REMARK 465 GLU F -17
REMARK 465 GLU F -16
REMARK 465 GLU F -15
REMARK 465 GLU F -14
REMARK 465 ASP F -13
REMARK 465 GLU F -12
REMARK 465 ASP F -11
REMARK 465 GLU F -10
REMARK 465 ASP F -9
REMARK 465 GLU F -8
REMARK 465 ASP F -7
REMARK 465 GLU F -6
REMARK 465 ASP F -5
REMARK 465 GLU F -4
REMARK 465 ALA F -3
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 GLU F 0
REMARK 465 LEU F 1
REMARK 465 GLY F 2
REMARK 465 GLU F 3
REMARK 465 GLY F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 17
REMARK 465 ILE F 18
REMARK 465 GLN F 19
REMARK 465 ASP F 20
REMARK 465 GLU F 21
REMARK 465 GLU F 22
REMARK 465 ASP F 23
REMARK 465 ASP F 24
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 THR A 121 O HIS A 123 1.80
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 THR C 121 -173.78 -68.34
REMARK 500 HIS C 123 -8.68 -140.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4NFT A 2 94 UNP Q16778 H2B2E_HUMAN 34 126
DBREF 4NFT A 95 193 UNP P0C0S5 H2AZ_HUMAN 16 114
DBREF 4NFT B 2 94 UNP Q16778 H2B2E_HUMAN 34 126
DBREF 4NFT B 95 193 UNP P0C0S5 H2AZ_HUMAN 16 114
DBREF 4NFT C 2 94 UNP Q16778 H2B2E_HUMAN 34 126
DBREF 4NFT C 95 193 UNP P0C0S5 H2AZ_HUMAN 16 114
DBREF 4NFT D 2 94 UNP Q16778 H2B2E_HUMAN 34 126
DBREF 4NFT D 95 193 UNP P0C0S5 H2AZ_HUMAN 16 114
DBREF 4NFT E -23 24 UNP Q9BTT0 AN32E_HUMAN 185 232
DBREF 4NFT F -23 24 UNP Q9BTT0 AN32E_HUMAN 185 232
SEQADV 4NFT GLY A -2 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER A -1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT HIS A 0 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT MET A 1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER A 194 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY A 195 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER A 196 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY A 197 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY A 198 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER A 199 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY A 200 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY A 201 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY A 202 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT LEU A 203 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT VAL A 204 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT PRO A 205 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT ARG A 206 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY B -2 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER B -1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT HIS B 0 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT MET B 1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER B 194 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY B 195 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER B 196 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY B 197 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY B 198 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER B 199 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY B 200 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY B 201 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY B 202 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT LEU B 203 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT VAL B 204 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT PRO B 205 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT ARG B 206 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY C -2 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER C -1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT HIS C 0 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT MET C 1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER C 194 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY C 195 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER C 196 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY C 197 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY C 198 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER C 199 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY C 200 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY C 201 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY C 202 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT LEU C 203 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT VAL C 204 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT PRO C 205 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT ARG C 206 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY D -2 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER D -1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT HIS D 0 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT MET D 1 UNP Q16778 EXPRESSION TAG
SEQADV 4NFT SER D 194 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY D 195 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER D 196 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY D 197 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY D 198 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT SER D 199 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY D 200 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY D 201 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY D 202 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT LEU D 203 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT VAL D 204 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT PRO D 205 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT ARG D 206 UNP P0C0S5 EXPRESSION TAG
SEQADV 4NFT GLY E -27 UNP Q9BTT0 EXPRESSION TAG
SEQADV 4NFT SER E -26 UNP Q9BTT0 EXPRESSION TAG
SEQADV 4NFT HIS E -25 UNP Q9BTT0 EXPRESSION TAG
SEQADV 4NFT MET E -24 UNP Q9BTT0 EXPRESSION TAG
SEQADV 4NFT GLY F -27 UNP Q9BTT0 EXPRESSION TAG
SEQADV 4NFT SER F -26 UNP Q9BTT0 EXPRESSION TAG
SEQADV 4NFT HIS F -25 UNP Q9BTT0 EXPRESSION TAG
SEQADV 4NFT MET F -24 UNP Q9BTT0 EXPRESSION TAG
SEQRES 1 A 209 GLY SER HIS MET ARG LYS GLU SER TYR SER ILE TYR VAL
SEQRES 2 A 209 TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE
SEQRES 3 A 209 SER SER LYS ALA MET GLY ILE MET ASN SER PHE VAL ASN
SEQRES 4 A 209 ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU
SEQRES 5 A 209 ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU
SEQRES 6 A 209 ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU
SEQRES 7 A 209 ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR
SEQRES 8 A 209 LYS TYR THR SER SER LYS LYS ALA VAL SER ARG SER GLN
SEQRES 9 A 209 ARG ALA GLY LEU GLN PHE PRO VAL GLY ARG ILE HIS ARG
SEQRES 10 A 209 HIS LEU LYS SER ARG THR THR SER HIS GLY ARG VAL GLY
SEQRES 11 A 209 ALA THR ALA ALA VAL TYR SER ALA ALA ILE LEU GLU TYR
SEQRES 12 A 209 LEU THR ALA GLU VAL LEU GLU LEU ALA GLY ASN ALA SER
SEQRES 13 A 209 LYS ASP LEU LYS VAL LYS ARG ILE THR PRO ARG HIS LEU
SEQRES 14 A 209 GLN LEU ALA ILE ARG GLY ASP GLU GLU LEU ASP SER LEU
SEQRES 15 A 209 ILE LYS ALA THR ILE ALA GLY GLY GLY VAL ILE PRO HIS
SEQRES 16 A 209 ILE SER GLY SER GLY GLY SER GLY GLY GLY LEU VAL PRO
SEQRES 17 A 209 ARG
SEQRES 1 B 209 GLY SER HIS MET ARG LYS GLU SER TYR SER ILE TYR VAL
SEQRES 2 B 209 TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE
SEQRES 3 B 209 SER SER LYS ALA MET GLY ILE MET ASN SER PHE VAL ASN
SEQRES 4 B 209 ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU
SEQRES 5 B 209 ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU
SEQRES 6 B 209 ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU
SEQRES 7 B 209 ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR
SEQRES 8 B 209 LYS TYR THR SER SER LYS LYS ALA VAL SER ARG SER GLN
SEQRES 9 B 209 ARG ALA GLY LEU GLN PHE PRO VAL GLY ARG ILE HIS ARG
SEQRES 10 B 209 HIS LEU LYS SER ARG THR THR SER HIS GLY ARG VAL GLY
SEQRES 11 B 209 ALA THR ALA ALA VAL TYR SER ALA ALA ILE LEU GLU TYR
SEQRES 12 B 209 LEU THR ALA GLU VAL LEU GLU LEU ALA GLY ASN ALA SER
SEQRES 13 B 209 LYS ASP LEU LYS VAL LYS ARG ILE THR PRO ARG HIS LEU
SEQRES 14 B 209 GLN LEU ALA ILE ARG GLY ASP GLU GLU LEU ASP SER LEU
SEQRES 15 B 209 ILE LYS ALA THR ILE ALA GLY GLY GLY VAL ILE PRO HIS
SEQRES 16 B 209 ILE SER GLY SER GLY GLY SER GLY GLY GLY LEU VAL PRO
SEQRES 17 B 209 ARG
SEQRES 1 C 209 GLY SER HIS MET ARG LYS GLU SER TYR SER ILE TYR VAL
SEQRES 2 C 209 TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE
SEQRES 3 C 209 SER SER LYS ALA MET GLY ILE MET ASN SER PHE VAL ASN
SEQRES 4 C 209 ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU
SEQRES 5 C 209 ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU
SEQRES 6 C 209 ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU
SEQRES 7 C 209 ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR
SEQRES 8 C 209 LYS TYR THR SER SER LYS LYS ALA VAL SER ARG SER GLN
SEQRES 9 C 209 ARG ALA GLY LEU GLN PHE PRO VAL GLY ARG ILE HIS ARG
SEQRES 10 C 209 HIS LEU LYS SER ARG THR THR SER HIS GLY ARG VAL GLY
SEQRES 11 C 209 ALA THR ALA ALA VAL TYR SER ALA ALA ILE LEU GLU TYR
SEQRES 12 C 209 LEU THR ALA GLU VAL LEU GLU LEU ALA GLY ASN ALA SER
SEQRES 13 C 209 LYS ASP LEU LYS VAL LYS ARG ILE THR PRO ARG HIS LEU
SEQRES 14 C 209 GLN LEU ALA ILE ARG GLY ASP GLU GLU LEU ASP SER LEU
SEQRES 15 C 209 ILE LYS ALA THR ILE ALA GLY GLY GLY VAL ILE PRO HIS
SEQRES 16 C 209 ILE SER GLY SER GLY GLY SER GLY GLY GLY LEU VAL PRO
SEQRES 17 C 209 ARG
SEQRES 1 D 209 GLY SER HIS MET ARG LYS GLU SER TYR SER ILE TYR VAL
SEQRES 2 D 209 TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE
SEQRES 3 D 209 SER SER LYS ALA MET GLY ILE MET ASN SER PHE VAL ASN
SEQRES 4 D 209 ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU
SEQRES 5 D 209 ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU
SEQRES 6 D 209 ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU
SEQRES 7 D 209 ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR
SEQRES 8 D 209 LYS TYR THR SER SER LYS LYS ALA VAL SER ARG SER GLN
SEQRES 9 D 209 ARG ALA GLY LEU GLN PHE PRO VAL GLY ARG ILE HIS ARG
SEQRES 10 D 209 HIS LEU LYS SER ARG THR THR SER HIS GLY ARG VAL GLY
SEQRES 11 D 209 ALA THR ALA ALA VAL TYR SER ALA ALA ILE LEU GLU TYR
SEQRES 12 D 209 LEU THR ALA GLU VAL LEU GLU LEU ALA GLY ASN ALA SER
SEQRES 13 D 209 LYS ASP LEU LYS VAL LYS ARG ILE THR PRO ARG HIS LEU
SEQRES 14 D 209 GLN LEU ALA ILE ARG GLY ASP GLU GLU LEU ASP SER LEU
SEQRES 15 D 209 ILE LYS ALA THR ILE ALA GLY GLY GLY VAL ILE PRO HIS
SEQRES 16 D 209 ILE SER GLY SER GLY GLY SER GLY GLY GLY LEU VAL PRO
SEQRES 17 D 209 ARG
SEQRES 1 E 52 GLY SER HIS MET GLU GLU GLU GLU GLU GLU GLU GLU GLU
SEQRES 2 E 52 GLU ASP GLU ASP GLU ASP GLU ASP GLU ASP GLU ALA GLY
SEQRES 3 E 52 SER GLU LEU GLY GLU GLY GLU GLU GLU VAL GLY LEU SER
SEQRES 4 E 52 TYR LEU MET LYS GLU GLU ILE GLN ASP GLU GLU ASP ASP
SEQRES 1 F 52 GLY SER HIS MET GLU GLU GLU GLU GLU GLU GLU GLU GLU
SEQRES 2 F 52 GLU ASP GLU ASP GLU ASP GLU ASP GLU ASP GLU ALA GLY
SEQRES 3 F 52 SER GLU LEU GLY GLU GLY GLU GLU GLU VAL GLY LEU SER
SEQRES 4 F 52 TYR LEU MET LYS GLU GLU ILE GLN ASP GLU GLU ASP ASP
FORMUL 7 HOH *146(H2 O)
HELIX 1 1 TYR A 6 HIS A 18 1 13
HELIX 2 2 SER A 24 HIS A 51 1 28
HELIX 3 3 THR A 59 LEU A 71 1 13
HELIX 4 4 PRO A 72 SER A 92 1 21
HELIX 5 5 ARG A 99 GLY A 104 1 6
HELIX 6 6 PRO A 108 SER A 118 1 11
HELIX 7 7 THR A 129 LEU A 156 1 28
HELIX 8 8 THR A 162 GLY A 172 1 11
HELIX 9 9 ASP A 173 ALA A 185 1 13
HELIX 10 10 TYR B 6 HIS B 18 1 13
HELIX 11 11 SER B 24 HIS B 51 1 28
HELIX 12 12 THR B 59 LEU B 71 1 13
HELIX 13 13 PRO B 72 SER B 92 1 21
HELIX 14 14 ARG B 99 GLY B 104 1 6
HELIX 15 15 PRO B 108 SER B 118 1 11
HELIX 16 16 THR B 129 LEU B 156 1 28
HELIX 17 17 THR B 162 GLY B 172 1 11
HELIX 18 18 ASP B 173 ALA B 185 1 13
HELIX 19 19 TYR C 6 HIS C 18 1 13
HELIX 20 20 SER C 24 ALA C 50 1 27
HELIX 21 21 ASN C 53 THR C 57 5 5
HELIX 22 22 THR C 59 LEU C 71 1 13
HELIX 23 23 PRO C 72 THR C 91 1 20
HELIX 24 24 ARG C 99 ALA C 103 1 5
HELIX 25 25 PRO C 108 THR C 120 1 13
HELIX 26 26 THR C 129 LEU C 156 1 28
HELIX 27 27 THR C 162 GLY C 172 1 11
HELIX 28 28 ASP C 173 GLY C 186 1 14
HELIX 29 29 TYR D 6 HIS D 18 1 13
HELIX 30 30 SER D 24 ALA D 50 1 27
HELIX 31 31 ASN D 53 THR D 57 5 5
HELIX 32 32 THR D 59 LEU D 71 1 13
HELIX 33 33 PRO D 72 SER D 92 1 21
HELIX 34 34 ARG D 99 ALA D 103 1 5
HELIX 35 35 PRO D 108 THR D 120 1 13
HELIX 36 36 THR D 129 LEU D 156 1 28
HELIX 37 37 THR D 162 GLY D 172 1 11
HELIX 38 38 ASP D 173 GLY D 186 1 14
HELIX 39 39 GLY E 9 LYS E 15 5 7
HELIX 40 40 GLY F 9 LYS F 15 5 7
SHEET 1 A 2 GLY A 22 ILE A 23 0
SHEET 2 A 2 ARG A 160 ILE A 161 1 O ILE A 161 N GLY A 22
SHEET 1 B 2 THR A 57 ILE A 58 0
SHEET 2 B 2 ARG A 125 VAL A 126 1 O ARG A 125 N ILE A 58
SHEET 1 C 2 GLY B 22 ILE B 23 0
SHEET 2 C 2 ARG B 160 ILE B 161 1 O ILE B 161 N GLY B 22
SHEET 1 D 2 THR B 57 ILE B 58 0
SHEET 2 D 2 ARG B 125 VAL B 126 1 O ARG B 125 N ILE B 58
SHEET 1 E 2 GLY C 22 ILE C 23 0
SHEET 2 E 2 ARG C 160 ILE C 161 1 O ILE C 161 N GLY C 22
SHEET 1 F 2 GLY D 22 ILE D 23 0
SHEET 2 F 2 ARG D 160 ILE D 161 1 O ILE D 161 N GLY D 22
CRYST1 76.412 104.297 124.743 90.00 99.15 90.00 C 1 2 1 16
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 0.013087 0.000000 0.002108 0.00000
SCALE2 0.000000 0.009588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008120 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
