HEADER TRANSCRIPTION 03-MAR-16 5FXY
TITLE STRUCTURE OF THE HUMAN RBBP4:MTA1(464-546) COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-BINDING PROTEIN RBBP4;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT C, CAF-1 SUBUNIT C, CHR
COMPND 5 OMATIN ASSEMBLY FACTOR I P48 SUBUNIT, CAF-I 48 KDA SUBUNIT, CAF-I
COMPND 6 P48, NUCLEOSOME-REMODELING FACTOR SUBUNIT RBAP48, RETINOBLASTOMA-B
COMPND 7 INDING PROTEIN 4, RBBP-4, RETINOBLASTOMA-BINDING PROTEIN P48, RBBP 4;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: METASTASIS-ASSOCIATED PROTEIN MTA1;
COMPND 11 CHAIN: B, D, F, H;
COMPND 12 FRAGMENT: RESIDUES 464-546;
COMPND 13 SYNONYM: MTA1;
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 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PCDNA3
KEYWDS TRANSCRIPTION, TRANSCRIPTION REPRESSION COMPLEX METASTASIS ASSOCIATED
KEYWDS 2 COMPLEX MTA1 RBBP4 RBBP7 HISTONE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.MILLARD,N.VARMA,L.FAIRALL,J.W.R.SCHWABE
REVDAT 4 10-JAN-24 5FXY 1 REMARK
REVDAT 3 22-MAR-17 5FXY 1 JRNL
REVDAT 2 25-MAY-16 5FXY 1 JRNL
REVDAT 1 18-MAY-16 5FXY 0
JRNL AUTH C.J.MILLARD,N.VARMA,A.SALEH,K.MORRIS,P.J.WATSON,
JRNL AUTH 2 A.R.BOTTRILL,L.FAIRALL,C.J.SMITH,J.W.SCHWABE
JRNL TITL THE STRUCTURE OF THE CORE NURD REPRESSION COMPLEX PROVIDES
JRNL TITL 2 INSIGHTS INTO ITS INTERACTION WITH CHROMATIN.
JRNL REF ELIFE V. 5 13941 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 27098840
JRNL DOI 10.7554/ELIFE.13941
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 35054
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) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1752
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2580
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14366
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.73000
REMARK 3 B22 (A**2) : -2.95000
REMARK 3 B33 (A**2) : -0.44000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.611
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.570
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.296
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.895
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.844
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14743 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 13697 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20063 ; 1.053 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 31583 ; 0.856 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1767 ; 5.573 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 710 ;30.387 ;24.169
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2411 ;13.115 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 87 ;11.872 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2204 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16518 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3405 ; 0.001 ; 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): 7155 ; 1.299 ; 9.165
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7154 ; 1.298 ; 9.164
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8893 ; 2.403 ;13.727
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7588 ; 0.733 ; 9.152
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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.
REMARK 4
REMARK 4 5FXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1290066307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96861
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PIXEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35054
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 95.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 4PC0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.21 M AMMONIUM CITRATE AND 19% PEG
REMARK 280 3350, PH 7.5
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 75.03600
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 5400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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: 5360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 LYS A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 PHE A 8
REMARK 465 ASP A 9
REMARK 465 ASP A 90
REMARK 465 ALA A 91
REMARK 465 GLN A 92
REMARK 465 PHE A 93
REMARK 465 ASP A 94
REMARK 465 ALA A 95
REMARK 465 SER A 96
REMARK 465 HIS A 97
REMARK 465 TYR A 98
REMARK 465 ASP A 99
REMARK 465 SER A 100
REMARK 465 GLU A 101
REMARK 465 LYS A 102
REMARK 465 SER A 164
REMARK 465 GLY A 165
REMARK 465 HIS A 176
REMARK 465 GLN A 177
REMARK 465 LYS A 178
REMARK 465 GLU A 179
REMARK 465 LYS A 212
REMARK 465 GLU A 213
REMARK 465 GLU A 412
REMARK 465 ASP A 413
REMARK 465 PRO A 414
REMARK 465 GLU A 415
REMARK 465 GLY A 416
REMARK 465 SER A 417
REMARK 465 VAL A 418
REMARK 465 ASP A 419
REMARK 465 PRO A 420
REMARK 465 GLU A 421
REMARK 465 GLY A 422
REMARK 465 GLN A 423
REMARK 465 GLY A 424
REMARK 465 SER A 425
REMARK 465 GLY B 462
REMARK 465 ALA B 463
REMARK 465 ALA B 464
REMARK 465 MET B 465
REMARK 465 LYS B 466
REMARK 465 THR B 467
REMARK 465 ALA B 519
REMARK 465 SER B 520
REMARK 465 GLN B 521
REMARK 465 SER B 522
REMARK 465 PRO B 523
REMARK 465 LEU B 524
REMARK 465 VAL B 525
REMARK 465 LEU B 526
REMARK 465 LYS B 527
REMARK 465 GLN B 528
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ASP C 3
REMARK 465 LYS C 4
REMARK 465 GLU C 5
REMARK 465 ALA C 6
REMARK 465 ALA C 7
REMARK 465 PHE C 8
REMARK 465 ASP C 9
REMARK 465 ASP C 90
REMARK 465 ALA C 91
REMARK 465 GLN C 92
REMARK 465 PHE C 93
REMARK 465 ASP C 94
REMARK 465 ALA C 95
REMARK 465 SER C 96
REMARK 465 HIS C 97
REMARK 465 TYR C 98
REMARK 465 ASP C 99
REMARK 465 SER C 100
REMARK 465 GLU C 101
REMARK 465 LYS C 102
REMARK 465 SER C 164
REMARK 465 GLY C 165
REMARK 465 HIS C 176
REMARK 465 GLN C 177
REMARK 465 LYS C 178
REMARK 465 GLU C 179
REMARK 465 PRO C 211
REMARK 465 LYS C 212
REMARK 465 GLU C 213
REMARK 465 GLU C 412
REMARK 465 ASP C 413
REMARK 465 PRO C 414
REMARK 465 GLU C 415
REMARK 465 GLY C 416
REMARK 465 SER C 417
REMARK 465 VAL C 418
REMARK 465 ASP C 419
REMARK 465 PRO C 420
REMARK 465 GLU C 421
REMARK 465 GLY C 422
REMARK 465 GLN C 423
REMARK 465 GLY C 424
REMARK 465 SER C 425
REMARK 465 GLY D 462
REMARK 465 ALA D 463
REMARK 465 ALA D 464
REMARK 465 MET D 465
REMARK 465 LYS D 466
REMARK 465 THR D 467
REMARK 465 ALA D 519
REMARK 465 SER D 520
REMARK 465 GLN D 521
REMARK 465 SER D 522
REMARK 465 PRO D 523
REMARK 465 LEU D 524
REMARK 465 VAL D 525
REMARK 465 LEU D 526
REMARK 465 LYS D 527
REMARK 465 GLN D 528
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 ASP E 3
REMARK 465 LYS E 4
REMARK 465 GLU E 5
REMARK 465 ALA E 6
REMARK 465 ALA E 7
REMARK 465 PHE E 8
REMARK 465 ASP E 9
REMARK 465 ASP E 90
REMARK 465 ALA E 91
REMARK 465 GLN E 92
REMARK 465 PHE E 93
REMARK 465 ASP E 94
REMARK 465 ALA E 95
REMARK 465 SER E 96
REMARK 465 HIS E 97
REMARK 465 TYR E 98
REMARK 465 ASP E 99
REMARK 465 SER E 100
REMARK 465 GLU E 101
REMARK 465 LYS E 102
REMARK 465 SER E 164
REMARK 465 GLY E 165
REMARK 465 HIS E 176
REMARK 465 GLN E 177
REMARK 465 LYS E 178
REMARK 465 GLU E 179
REMARK 465 PRO E 211
REMARK 465 LYS E 212
REMARK 465 GLU E 213
REMARK 465 GLU E 412
REMARK 465 ASP E 413
REMARK 465 PRO E 414
REMARK 465 GLU E 415
REMARK 465 GLY E 416
REMARK 465 SER E 417
REMARK 465 VAL E 418
REMARK 465 ASP E 419
REMARK 465 PRO E 420
REMARK 465 GLU E 421
REMARK 465 GLY E 422
REMARK 465 GLN E 423
REMARK 465 GLY E 424
REMARK 465 SER E 425
REMARK 465 GLY F 462
REMARK 465 ALA F 463
REMARK 465 ALA F 464
REMARK 465 MET F 465
REMARK 465 LYS F 466
REMARK 465 THR F 467
REMARK 465 ARG F 468
REMARK 465 ALA F 519
REMARK 465 SER F 520
REMARK 465 GLN F 521
REMARK 465 SER F 522
REMARK 465 PRO F 523
REMARK 465 LEU F 524
REMARK 465 VAL F 525
REMARK 465 LEU F 526
REMARK 465 LYS F 527
REMARK 465 GLN F 528
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 ASP G 3
REMARK 465 LYS G 4
REMARK 465 GLU G 5
REMARK 465 ALA G 6
REMARK 465 ALA G 7
REMARK 465 PHE G 8
REMARK 465 ASP G 9
REMARK 465 ASP G 90
REMARK 465 ALA G 91
REMARK 465 GLN G 92
REMARK 465 PHE G 93
REMARK 465 ASP G 94
REMARK 465 ALA G 95
REMARK 465 SER G 96
REMARK 465 HIS G 97
REMARK 465 TYR G 98
REMARK 465 ASP G 99
REMARK 465 SER G 100
REMARK 465 GLU G 101
REMARK 465 LYS G 102
REMARK 465 SER G 164
REMARK 465 GLY G 165
REMARK 465 HIS G 176
REMARK 465 GLN G 177
REMARK 465 LYS G 178
REMARK 465 GLU G 179
REMARK 465 LYS G 212
REMARK 465 GLU G 213
REMARK 465 GLU G 412
REMARK 465 ASP G 413
REMARK 465 PRO G 414
REMARK 465 GLU G 415
REMARK 465 GLY G 416
REMARK 465 SER G 417
REMARK 465 VAL G 418
REMARK 465 ASP G 419
REMARK 465 PRO G 420
REMARK 465 GLU G 421
REMARK 465 GLY G 422
REMARK 465 GLN G 423
REMARK 465 GLY G 424
REMARK 465 SER G 425
REMARK 465 GLY H 462
REMARK 465 ALA H 463
REMARK 465 ALA H 464
REMARK 465 MET H 465
REMARK 465 LYS H 466
REMARK 465 THR H 467
REMARK 465 ALA H 519
REMARK 465 SER H 520
REMARK 465 GLN H 521
REMARK 465 SER H 522
REMARK 465 PRO H 523
REMARK 465 LEU H 524
REMARK 465 VAL H 525
REMARK 465 LEU H 526
REMARK 465 LYS H 527
REMARK 465 GLN H 528
REMARK 465 ALA H 529
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 GLU B 518 CG CD OE1 OE2
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 ASN A 168 67.03 -151.89
REMARK 500 LEU A 189 76.21 56.44
REMARK 500 GLN A 250 30.22 70.37
REMARK 500 SER A 315 -44.98 167.30
REMARK 500 ASP A 396 36.03 -94.34
REMARK 500 GLN B 469 96.29 -170.88
REMARK 500 CYS B 486 54.89 -103.51
REMARK 500 ARG B 491 70.92 60.08
REMARK 500 ASN B 504 86.57 -69.55
REMARK 500 ARG B 515 53.93 -107.21
REMARK 500 LYS B 532 122.54 74.42
REMARK 500 HIS C 38 117.79 -161.23
REMARK 500 ASP C 199 37.44 -95.30
REMARK 500 SER C 315 -43.71 172.66
REMARK 500 HIS C 370 -76.62 -75.51
REMARK 500 ASP C 396 39.22 -94.17
REMARK 500 ASN C 397 -36.04 73.16
REMARK 500 CYS D 486 53.89 -111.29
REMARK 500 ARG D 491 78.63 59.94
REMARK 500 ASN D 504 88.34 -69.62
REMARK 500 ARG D 515 49.60 -105.05
REMARK 500 LYS D 532 123.47 69.04
REMARK 500 PRO D 545 -158.92 -101.53
REMARK 500 ARG E 55 75.93 59.41
REMARK 500 ASN E 168 68.82 60.14
REMARK 500 LYS E 215 -4.11 69.86
REMARK 500 GLU E 231 -62.59 -93.80
REMARK 500 LYS E 307 -78.23 -41.39
REMARK 500 SER E 315 -33.87 156.67
REMARK 500 ASP E 396 37.30 -92.19
REMARK 500 ASN E 397 -33.56 74.25
REMARK 500 CYS F 486 54.88 -102.53
REMARK 500 ARG F 491 71.37 61.05
REMARK 500 ARG F 515 49.42 -103.45
REMARK 500 LYS F 532 123.47 74.26
REMARK 500 HIS F 544 79.85 -118.67
REMARK 500 SER G 110 113.99 -160.59
REMARK 500 VAL G 127 95.46 -65.35
REMARK 500 ASN G 136 79.84 59.81
REMARK 500 PHE G 152 -160.27 -122.20
REMARK 500 ASN G 168 62.67 64.62
REMARK 500 THR G 224 74.94 -118.86
REMARK 500 GLN G 250 41.60 71.68
REMARK 500 SER G 315 -48.65 175.14
REMARK 500 HIS G 370 -76.95 -76.20
REMARK 500 CYS H 486 56.87 -101.05
REMARK 500 ARG H 491 73.66 60.31
REMARK 500 LYS H 532 111.74 71.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE G 139 ILE G 140 -137.73
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5FXY A 1 425 UNP Q09028 RBBP4_HUMAN 1 425
DBREF 5FXY B 464 546 UNP Q13330 MTA1_HUMAN 464 546
DBREF 5FXY C 1 425 UNP Q09028 RBBP4_HUMAN 1 425
DBREF 5FXY D 464 546 UNP Q13330 MTA1_HUMAN 464 546
DBREF 5FXY E 1 425 UNP Q09028 RBBP4_HUMAN 1 425
DBREF 5FXY F 464 546 UNP Q13330 MTA1_HUMAN 464 546
DBREF 5FXY G 1 425 UNP Q09028 RBBP4_HUMAN 1 425
DBREF 5FXY H 464 546 UNP Q13330 MTA1_HUMAN 464 546
SEQADV 5FXY GLY B 462 UNP Q13330 EXPRESSION TAG
SEQADV 5FXY ALA B 463 UNP Q13330 EXPRESSION TAG
SEQADV 5FXY GLY D 462 UNP Q13330 EXPRESSION TAG
SEQADV 5FXY ALA D 463 UNP Q13330 EXPRESSION TAG
SEQADV 5FXY GLY F 462 UNP Q13330 EXPRESSION TAG
SEQADV 5FXY ALA F 463 UNP Q13330 EXPRESSION TAG
SEQADV 5FXY GLY H 462 UNP Q13330 EXPRESSION TAG
SEQADV 5FXY ALA H 463 UNP Q13330 EXPRESSION TAG
SEQRES 1 A 425 MET ALA ASP LYS GLU ALA ALA PHE ASP ASP ALA VAL GLU
SEQRES 2 A 425 GLU ARG VAL ILE ASN GLU GLU TYR LYS ILE TRP LYS LYS
SEQRES 3 A 425 ASN THR PRO PHE LEU TYR ASP LEU VAL MET THR HIS ALA
SEQRES 4 A 425 LEU GLU TRP PRO SER LEU THR ALA GLN TRP LEU PRO ASP
SEQRES 5 A 425 VAL THR ARG PRO GLU GLY LYS ASP PHE SER ILE HIS ARG
SEQRES 6 A 425 LEU VAL LEU GLY THR HIS THR SER ASP GLU GLN ASN HIS
SEQRES 7 A 425 LEU VAL ILE ALA SER VAL GLN LEU PRO ASN ASP ASP ALA
SEQRES 8 A 425 GLN PHE ASP ALA SER HIS TYR ASP SER GLU LYS GLY GLU
SEQRES 9 A 425 PHE GLY GLY PHE GLY SER VAL SER GLY LYS ILE GLU ILE
SEQRES 10 A 425 GLU ILE LYS ILE ASN HIS GLU GLY GLU VAL ASN ARG ALA
SEQRES 11 A 425 ARG TYR MET PRO GLN ASN PRO CYS ILE ILE ALA THR LYS
SEQRES 12 A 425 THR PRO SER SER ASP VAL LEU VAL PHE ASP TYR THR LYS
SEQRES 13 A 425 HIS PRO SER LYS PRO ASP PRO SER GLY GLU CYS ASN PRO
SEQRES 14 A 425 ASP LEU ARG LEU ARG GLY HIS GLN LYS GLU GLY TYR GLY
SEQRES 15 A 425 LEU SER TRP ASN PRO ASN LEU SER GLY HIS LEU LEU SER
SEQRES 16 A 425 ALA SER ASP ASP HIS THR ILE CYS LEU TRP ASP ILE SER
SEQRES 17 A 425 ALA VAL PRO LYS GLU GLY LYS VAL VAL ASP ALA LYS THR
SEQRES 18 A 425 ILE PHE THR GLY HIS THR ALA VAL VAL GLU ASP VAL SER
SEQRES 19 A 425 TRP HIS LEU LEU HIS GLU SER LEU PHE GLY SER VAL ALA
SEQRES 20 A 425 ASP ASP GLN LYS LEU MET ILE TRP ASP THR ARG SER ASN
SEQRES 21 A 425 ASN THR SER LYS PRO SER HIS SER VAL ASP ALA HIS THR
SEQRES 22 A 425 ALA GLU VAL ASN CYS LEU SER PHE ASN PRO TYR SER GLU
SEQRES 23 A 425 PHE ILE LEU ALA THR GLY SER ALA ASP LYS THR VAL ALA
SEQRES 24 A 425 LEU TRP ASP LEU ARG ASN LEU LYS LEU LYS LEU HIS SER
SEQRES 25 A 425 PHE GLU SER HIS LYS ASP GLU ILE PHE GLN VAL GLN TRP
SEQRES 26 A 425 SER PRO HIS ASN GLU THR ILE LEU ALA SER SER GLY THR
SEQRES 27 A 425 ASP ARG ARG LEU ASN VAL TRP ASP LEU SER LYS ILE GLY
SEQRES 28 A 425 GLU GLU GLN SER PRO GLU ASP ALA GLU ASP GLY PRO PRO
SEQRES 29 A 425 GLU LEU LEU PHE ILE HIS GLY GLY HIS THR ALA LYS ILE
SEQRES 30 A 425 SER ASP PHE SER TRP ASN PRO ASN GLU PRO TRP VAL ILE
SEQRES 31 A 425 CYS SER VAL SER GLU ASP ASN ILE MET GLN VAL TRP GLN
SEQRES 32 A 425 MET ALA GLU ASN ILE TYR ASN ASP GLU ASP PRO GLU GLY
SEQRES 33 A 425 SER VAL ASP PRO GLU GLY GLN GLY SER
SEQRES 1 B 85 GLY ALA ALA MET LYS THR ARG GLN ALA PHE TYR LEU HIS
SEQRES 2 B 85 THR THR LYS LEU THR ARG ILE ALA ARG ARG LEU CYS ARG
SEQRES 3 B 85 GLU ILE LEU ARG PRO TRP HIS ALA ALA ARG HIS PRO TYR
SEQRES 4 B 85 LEU PRO ILE ASN SER ALA ALA ILE LYS ALA GLU CYS THR
SEQRES 5 B 85 ALA ARG LEU PRO GLU ALA SER GLN SER PRO LEU VAL LEU
SEQRES 6 B 85 LYS GLN ALA VAL ARG LYS PRO LEU GLU ALA VAL LEU ARG
SEQRES 7 B 85 TYR LEU GLU THR HIS PRO ARG
SEQRES 1 C 425 MET ALA ASP LYS GLU ALA ALA PHE ASP ASP ALA VAL GLU
SEQRES 2 C 425 GLU ARG VAL ILE ASN GLU GLU TYR LYS ILE TRP LYS LYS
SEQRES 3 C 425 ASN THR PRO PHE LEU TYR ASP LEU VAL MET THR HIS ALA
SEQRES 4 C 425 LEU GLU TRP PRO SER LEU THR ALA GLN TRP LEU PRO ASP
SEQRES 5 C 425 VAL THR ARG PRO GLU GLY LYS ASP PHE SER ILE HIS ARG
SEQRES 6 C 425 LEU VAL LEU GLY THR HIS THR SER ASP GLU GLN ASN HIS
SEQRES 7 C 425 LEU VAL ILE ALA SER VAL GLN LEU PRO ASN ASP ASP ALA
SEQRES 8 C 425 GLN PHE ASP ALA SER HIS TYR ASP SER GLU LYS GLY GLU
SEQRES 9 C 425 PHE GLY GLY PHE GLY SER VAL SER GLY LYS ILE GLU ILE
SEQRES 10 C 425 GLU ILE LYS ILE ASN HIS GLU GLY GLU VAL ASN ARG ALA
SEQRES 11 C 425 ARG TYR MET PRO GLN ASN PRO CYS ILE ILE ALA THR LYS
SEQRES 12 C 425 THR PRO SER SER ASP VAL LEU VAL PHE ASP TYR THR LYS
SEQRES 13 C 425 HIS PRO SER LYS PRO ASP PRO SER GLY GLU CYS ASN PRO
SEQRES 14 C 425 ASP LEU ARG LEU ARG GLY HIS GLN LYS GLU GLY TYR GLY
SEQRES 15 C 425 LEU SER TRP ASN PRO ASN LEU SER GLY HIS LEU LEU SER
SEQRES 16 C 425 ALA SER ASP ASP HIS THR ILE CYS LEU TRP ASP ILE SER
SEQRES 17 C 425 ALA VAL PRO LYS GLU GLY LYS VAL VAL ASP ALA LYS THR
SEQRES 18 C 425 ILE PHE THR GLY HIS THR ALA VAL VAL GLU ASP VAL SER
SEQRES 19 C 425 TRP HIS LEU LEU HIS GLU SER LEU PHE GLY SER VAL ALA
SEQRES 20 C 425 ASP ASP GLN LYS LEU MET ILE TRP ASP THR ARG SER ASN
SEQRES 21 C 425 ASN THR SER LYS PRO SER HIS SER VAL ASP ALA HIS THR
SEQRES 22 C 425 ALA GLU VAL ASN CYS LEU SER PHE ASN PRO TYR SER GLU
SEQRES 23 C 425 PHE ILE LEU ALA THR GLY SER ALA ASP LYS THR VAL ALA
SEQRES 24 C 425 LEU TRP ASP LEU ARG ASN LEU LYS LEU LYS LEU HIS SER
SEQRES 25 C 425 PHE GLU SER HIS LYS ASP GLU ILE PHE GLN VAL GLN TRP
SEQRES 26 C 425 SER PRO HIS ASN GLU THR ILE LEU ALA SER SER GLY THR
SEQRES 27 C 425 ASP ARG ARG LEU ASN VAL TRP ASP LEU SER LYS ILE GLY
SEQRES 28 C 425 GLU GLU GLN SER PRO GLU ASP ALA GLU ASP GLY PRO PRO
SEQRES 29 C 425 GLU LEU LEU PHE ILE HIS GLY GLY HIS THR ALA LYS ILE
SEQRES 30 C 425 SER ASP PHE SER TRP ASN PRO ASN GLU PRO TRP VAL ILE
SEQRES 31 C 425 CYS SER VAL SER GLU ASP ASN ILE MET GLN VAL TRP GLN
SEQRES 32 C 425 MET ALA GLU ASN ILE TYR ASN ASP GLU ASP PRO GLU GLY
SEQRES 33 C 425 SER VAL ASP PRO GLU GLY GLN GLY SER
SEQRES 1 D 85 GLY ALA ALA MET LYS THR ARG GLN ALA PHE TYR LEU HIS
SEQRES 2 D 85 THR THR LYS LEU THR ARG ILE ALA ARG ARG LEU CYS ARG
SEQRES 3 D 85 GLU ILE LEU ARG PRO TRP HIS ALA ALA ARG HIS PRO TYR
SEQRES 4 D 85 LEU PRO ILE ASN SER ALA ALA ILE LYS ALA GLU CYS THR
SEQRES 5 D 85 ALA ARG LEU PRO GLU ALA SER GLN SER PRO LEU VAL LEU
SEQRES 6 D 85 LYS GLN ALA VAL ARG LYS PRO LEU GLU ALA VAL LEU ARG
SEQRES 7 D 85 TYR LEU GLU THR HIS PRO ARG
SEQRES 1 E 425 MET ALA ASP LYS GLU ALA ALA PHE ASP ASP ALA VAL GLU
SEQRES 2 E 425 GLU ARG VAL ILE ASN GLU GLU TYR LYS ILE TRP LYS LYS
SEQRES 3 E 425 ASN THR PRO PHE LEU TYR ASP LEU VAL MET THR HIS ALA
SEQRES 4 E 425 LEU GLU TRP PRO SER LEU THR ALA GLN TRP LEU PRO ASP
SEQRES 5 E 425 VAL THR ARG PRO GLU GLY LYS ASP PHE SER ILE HIS ARG
SEQRES 6 E 425 LEU VAL LEU GLY THR HIS THR SER ASP GLU GLN ASN HIS
SEQRES 7 E 425 LEU VAL ILE ALA SER VAL GLN LEU PRO ASN ASP ASP ALA
SEQRES 8 E 425 GLN PHE ASP ALA SER HIS TYR ASP SER GLU LYS GLY GLU
SEQRES 9 E 425 PHE GLY GLY PHE GLY SER VAL SER GLY LYS ILE GLU ILE
SEQRES 10 E 425 GLU ILE LYS ILE ASN HIS GLU GLY GLU VAL ASN ARG ALA
SEQRES 11 E 425 ARG TYR MET PRO GLN ASN PRO CYS ILE ILE ALA THR LYS
SEQRES 12 E 425 THR PRO SER SER ASP VAL LEU VAL PHE ASP TYR THR LYS
SEQRES 13 E 425 HIS PRO SER LYS PRO ASP PRO SER GLY GLU CYS ASN PRO
SEQRES 14 E 425 ASP LEU ARG LEU ARG GLY HIS GLN LYS GLU GLY TYR GLY
SEQRES 15 E 425 LEU SER TRP ASN PRO ASN LEU SER GLY HIS LEU LEU SER
SEQRES 16 E 425 ALA SER ASP ASP HIS THR ILE CYS LEU TRP ASP ILE SER
SEQRES 17 E 425 ALA VAL PRO LYS GLU GLY LYS VAL VAL ASP ALA LYS THR
SEQRES 18 E 425 ILE PHE THR GLY HIS THR ALA VAL VAL GLU ASP VAL SER
SEQRES 19 E 425 TRP HIS LEU LEU HIS GLU SER LEU PHE GLY SER VAL ALA
SEQRES 20 E 425 ASP ASP GLN LYS LEU MET ILE TRP ASP THR ARG SER ASN
SEQRES 21 E 425 ASN THR SER LYS PRO SER HIS SER VAL ASP ALA HIS THR
SEQRES 22 E 425 ALA GLU VAL ASN CYS LEU SER PHE ASN PRO TYR SER GLU
SEQRES 23 E 425 PHE ILE LEU ALA THR GLY SER ALA ASP LYS THR VAL ALA
SEQRES 24 E 425 LEU TRP ASP LEU ARG ASN LEU LYS LEU LYS LEU HIS SER
SEQRES 25 E 425 PHE GLU SER HIS LYS ASP GLU ILE PHE GLN VAL GLN TRP
SEQRES 26 E 425 SER PRO HIS ASN GLU THR ILE LEU ALA SER SER GLY THR
SEQRES 27 E 425 ASP ARG ARG LEU ASN VAL TRP ASP LEU SER LYS ILE GLY
SEQRES 28 E 425 GLU GLU GLN SER PRO GLU ASP ALA GLU ASP GLY PRO PRO
SEQRES 29 E 425 GLU LEU LEU PHE ILE HIS GLY GLY HIS THR ALA LYS ILE
SEQRES 30 E 425 SER ASP PHE SER TRP ASN PRO ASN GLU PRO TRP VAL ILE
SEQRES 31 E 425 CYS SER VAL SER GLU ASP ASN ILE MET GLN VAL TRP GLN
SEQRES 32 E 425 MET ALA GLU ASN ILE TYR ASN ASP GLU ASP PRO GLU GLY
SEQRES 33 E 425 SER VAL ASP PRO GLU GLY GLN GLY SER
SEQRES 1 F 85 GLY ALA ALA MET LYS THR ARG GLN ALA PHE TYR LEU HIS
SEQRES 2 F 85 THR THR LYS LEU THR ARG ILE ALA ARG ARG LEU CYS ARG
SEQRES 3 F 85 GLU ILE LEU ARG PRO TRP HIS ALA ALA ARG HIS PRO TYR
SEQRES 4 F 85 LEU PRO ILE ASN SER ALA ALA ILE LYS ALA GLU CYS THR
SEQRES 5 F 85 ALA ARG LEU PRO GLU ALA SER GLN SER PRO LEU VAL LEU
SEQRES 6 F 85 LYS GLN ALA VAL ARG LYS PRO LEU GLU ALA VAL LEU ARG
SEQRES 7 F 85 TYR LEU GLU THR HIS PRO ARG
SEQRES 1 G 425 MET ALA ASP LYS GLU ALA ALA PHE ASP ASP ALA VAL GLU
SEQRES 2 G 425 GLU ARG VAL ILE ASN GLU GLU TYR LYS ILE TRP LYS LYS
SEQRES 3 G 425 ASN THR PRO PHE LEU TYR ASP LEU VAL MET THR HIS ALA
SEQRES 4 G 425 LEU GLU TRP PRO SER LEU THR ALA GLN TRP LEU PRO ASP
SEQRES 5 G 425 VAL THR ARG PRO GLU GLY LYS ASP PHE SER ILE HIS ARG
SEQRES 6 G 425 LEU VAL LEU GLY THR HIS THR SER ASP GLU GLN ASN HIS
SEQRES 7 G 425 LEU VAL ILE ALA SER VAL GLN LEU PRO ASN ASP ASP ALA
SEQRES 8 G 425 GLN PHE ASP ALA SER HIS TYR ASP SER GLU LYS GLY GLU
SEQRES 9 G 425 PHE GLY GLY PHE GLY SER VAL SER GLY LYS ILE GLU ILE
SEQRES 10 G 425 GLU ILE LYS ILE ASN HIS GLU GLY GLU VAL ASN ARG ALA
SEQRES 11 G 425 ARG TYR MET PRO GLN ASN PRO CYS ILE ILE ALA THR LYS
SEQRES 12 G 425 THR PRO SER SER ASP VAL LEU VAL PHE ASP TYR THR LYS
SEQRES 13 G 425 HIS PRO SER LYS PRO ASP PRO SER GLY GLU CYS ASN PRO
SEQRES 14 G 425 ASP LEU ARG LEU ARG GLY HIS GLN LYS GLU GLY TYR GLY
SEQRES 15 G 425 LEU SER TRP ASN PRO ASN LEU SER GLY HIS LEU LEU SER
SEQRES 16 G 425 ALA SER ASP ASP HIS THR ILE CYS LEU TRP ASP ILE SER
SEQRES 17 G 425 ALA VAL PRO LYS GLU GLY LYS VAL VAL ASP ALA LYS THR
SEQRES 18 G 425 ILE PHE THR GLY HIS THR ALA VAL VAL GLU ASP VAL SER
SEQRES 19 G 425 TRP HIS LEU LEU HIS GLU SER LEU PHE GLY SER VAL ALA
SEQRES 20 G 425 ASP ASP GLN LYS LEU MET ILE TRP ASP THR ARG SER ASN
SEQRES 21 G 425 ASN THR SER LYS PRO SER HIS SER VAL ASP ALA HIS THR
SEQRES 22 G 425 ALA GLU VAL ASN CYS LEU SER PHE ASN PRO TYR SER GLU
SEQRES 23 G 425 PHE ILE LEU ALA THR GLY SER ALA ASP LYS THR VAL ALA
SEQRES 24 G 425 LEU TRP ASP LEU ARG ASN LEU LYS LEU LYS LEU HIS SER
SEQRES 25 G 425 PHE GLU SER HIS LYS ASP GLU ILE PHE GLN VAL GLN TRP
SEQRES 26 G 425 SER PRO HIS ASN GLU THR ILE LEU ALA SER SER GLY THR
SEQRES 27 G 425 ASP ARG ARG LEU ASN VAL TRP ASP LEU SER LYS ILE GLY
SEQRES 28 G 425 GLU GLU GLN SER PRO GLU ASP ALA GLU ASP GLY PRO PRO
SEQRES 29 G 425 GLU LEU LEU PHE ILE HIS GLY GLY HIS THR ALA LYS ILE
SEQRES 30 G 425 SER ASP PHE SER TRP ASN PRO ASN GLU PRO TRP VAL ILE
SEQRES 31 G 425 CYS SER VAL SER GLU ASP ASN ILE MET GLN VAL TRP GLN
SEQRES 32 G 425 MET ALA GLU ASN ILE TYR ASN ASP GLU ASP PRO GLU GLY
SEQRES 33 G 425 SER VAL ASP PRO GLU GLY GLN GLY SER
SEQRES 1 H 85 GLY ALA ALA MET LYS THR ARG GLN ALA PHE TYR LEU HIS
SEQRES 2 H 85 THR THR LYS LEU THR ARG ILE ALA ARG ARG LEU CYS ARG
SEQRES 3 H 85 GLU ILE LEU ARG PRO TRP HIS ALA ALA ARG HIS PRO TYR
SEQRES 4 H 85 LEU PRO ILE ASN SER ALA ALA ILE LYS ALA GLU CYS THR
SEQRES 5 H 85 ALA ARG LEU PRO GLU ALA SER GLN SER PRO LEU VAL LEU
SEQRES 6 H 85 LYS GLN ALA VAL ARG LYS PRO LEU GLU ALA VAL LEU ARG
SEQRES 7 H 85 TYR LEU GLU THR HIS PRO ARG
HELIX 1 1 ASP A 10 LEU A 31 1 22
HELIX 2 2 SER A 348 ILE A 350 5 3
HELIX 3 3 SER A 355 GLY A 362 1 8
HELIX 4 4 ALA A 405 ASN A 410 1 6
HELIX 5 5 THR B 476 CYS B 486 1 11
HELIX 6 6 CYS B 486 ARG B 491 1 6
HELIX 7 7 ARG B 491 ALA B 496 1 6
HELIX 8 8 ASN B 504 ARG B 515 1 12
HELIX 9 9 PRO B 533 HIS B 544 1 12
HELIX 10 10 ASP C 10 LEU C 31 1 22
HELIX 11 11 SER C 348 ILE C 350 5 3
HELIX 12 12 SER C 355 GLY C 362 1 8
HELIX 13 13 ALA C 405 ASN C 410 1 6
HELIX 14 14 THR D 476 CYS D 486 1 11
HELIX 15 15 CYS D 486 ARG D 491 1 6
HELIX 16 16 ARG D 491 ALA D 496 1 6
HELIX 17 17 ASN D 504 ARG D 515 1 12
HELIX 18 18 PRO D 533 HIS D 544 1 12
HELIX 19 19 ALA E 11 LEU E 31 1 21
HELIX 20 20 SER E 348 ILE E 350 5 3
HELIX 21 21 SER E 355 GLY E 362 1 8
HELIX 22 22 ALA E 405 ASN E 410 1 6
HELIX 23 23 THR F 476 CYS F 486 1 11
HELIX 24 24 CYS F 486 ARG F 491 1 6
HELIX 25 25 ARG F 491 ALA F 496 1 6
HELIX 26 26 ASN F 504 ARG F 515 1 12
HELIX 27 27 PRO F 533 HIS F 544 1 12
HELIX 28 28 ASP G 10 LEU G 31 1 22
HELIX 29 29 SER G 348 ILE G 350 5 3
HELIX 30 30 SER G 355 GLY G 362 1 8
HELIX 31 31 ALA G 405 ASN G 410 1 6
HELIX 32 32 THR H 476 CYS H 486 1 11
HELIX 33 33 CYS H 486 ARG H 491 1 6
HELIX 34 34 ARG H 491 ALA H 496 1 6
HELIX 35 35 ASN H 504 ARG H 515 1 12
HELIX 36 36 PRO H 533 HIS H 544 1 12
SHEET 1 AA 5 ILE A 377 TRP A 382 0
SHEET 2 AA 5 VAL A 389 SER A 394 -1 O CYS A 391 N SER A 381
SHEET 3 AA 5 ILE A 398 MET A 404 -1 O ILE A 398 N SER A 394
SHEET 4 AA 5 TYR A 32 ALA A 39 -1 N ASP A 33 O GLN A 403
SHEET 5 AA 5 TYR B 472 HIS B 474 -1 O LEU B 473 N VAL A 35
SHEET 1 AB 4 TRP A 49 THR A 54 0
SHEET 2 AB 4 PHE A 61 LEU A 66 -1 O ILE A 63 N THR A 54
SHEET 3 AB 4 ASN A 77 PRO A 87 -1 O ALA A 82 N LEU A 66
SHEET 4 AB 4 GLU A 116 HIS A 123 -1 O GLU A 116 N SER A 83
SHEET 1 AC 5 ARG A 129 TYR A 132 0
SHEET 2 AC 5 ILE A 139 LYS A 143 -1 O ALA A 141 N ARG A 131
SHEET 3 AC 5 VAL A 149 ASP A 153 -1 O LEU A 150 N THR A 142
SHEET 4 AC 5 LEU A 171 LEU A 173 -1 O LEU A 171 N VAL A 151
SHEET 5 AC 5 VAL A 216 VAL A 217 1 N VAL A 217 O ARG A 172
SHEET 1 AD 4 LEU A 183 TRP A 185 0
SHEET 2 AD 4 HIS A 192 ALA A 196 -1 O LEU A 194 N SER A 184
SHEET 3 AD 4 ILE A 202 ASP A 206 -1 O CYS A 203 N SER A 195
SHEET 4 AD 4 THR A 221 PHE A 223 -1 O THR A 221 N LEU A 204
SHEET 1 AE 4 VAL A 230 TRP A 235 0
SHEET 2 AE 4 LEU A 242 ALA A 247 -1 O GLY A 244 N SER A 234
SHEET 3 AE 4 LYS A 251 ASP A 256 -1 O LYS A 251 N ALA A 247
SHEET 4 AE 4 HIS A 267 ASP A 270 -1 O HIS A 267 N ILE A 254
SHEET 1 AF 4 VAL A 276 PHE A 281 0
SHEET 2 AF 4 ILE A 288 SER A 293 -1 O ALA A 290 N SER A 280
SHEET 3 AF 4 THR A 297 ASP A 302 -1 O THR A 297 N SER A 293
SHEET 4 AF 4 HIS A 311 GLU A 314 -1 O HIS A 311 N LEU A 300
SHEET 1 AG 4 ILE A 320 TRP A 325 0
SHEET 2 AG 4 ILE A 332 GLY A 337 -1 O ALA A 334 N GLN A 324
SHEET 3 AG 4 LEU A 342 ASP A 346 -1 O ASN A 343 N SER A 335
SHEET 4 AG 4 LEU A 366 HIS A 370 -1 N LEU A 367 O VAL A 344
SHEET 1 CA 6 PHE C 108 GLY C 109 0
SHEET 2 CA 6 PHE D 471 HIS D 474 -1 O TYR D 472 N GLY C 109
SHEET 3 CA 6 TYR C 32 ALA C 39 -1 O VAL C 35 N LEU D 473
SHEET 4 CA 6 ILE C 398 MET C 404 -1 O MET C 399 N HIS C 38
SHEET 5 CA 6 VAL C 389 SER C 394 -1 O ILE C 390 N TRP C 402
SHEET 6 CA 6 ILE C 377 TRP C 382 -1 N SER C 378 O VAL C 393
SHEET 1 CB 3 PHE C 61 GLY C 69 0
SHEET 2 CB 3 ASN C 77 PRO C 87 -1 O VAL C 80 N LEU C 68
SHEET 3 CB 3 ILE C 115 HIS C 123 -1 O GLU C 116 N SER C 83
SHEET 1 CC 5 ARG C 129 TYR C 132 0
SHEET 2 CC 5 ILE C 139 LYS C 143 -1 O ALA C 141 N ARG C 131
SHEET 3 CC 5 VAL C 149 ASP C 153 -1 O LEU C 150 N THR C 142
SHEET 4 CC 5 LEU C 171 LEU C 173 -1 O LEU C 171 N VAL C 151
SHEET 5 CC 5 VAL C 216 VAL C 217 1 N VAL C 217 O ARG C 172
SHEET 1 CD 4 LEU C 183 TRP C 185 0
SHEET 2 CD 4 HIS C 192 ALA C 196 -1 O LEU C 194 N SER C 184
SHEET 3 CD 4 ILE C 202 ASP C 206 -1 O CYS C 203 N SER C 195
SHEET 4 CD 4 THR C 221 PHE C 223 -1 O THR C 221 N LEU C 204
SHEET 1 CE 4 VAL C 230 TRP C 235 0
SHEET 2 CE 4 LEU C 242 ALA C 247 -1 O GLY C 244 N SER C 234
SHEET 3 CE 4 LYS C 251 ASP C 256 -1 O LYS C 251 N ALA C 247
SHEET 4 CE 4 HIS C 267 ASP C 270 -1 O HIS C 267 N ILE C 254
SHEET 1 CF 4 VAL C 276 PHE C 281 0
SHEET 2 CF 4 ILE C 288 SER C 293 -1 O ALA C 290 N SER C 280
SHEET 3 CF 4 THR C 297 ASP C 302 -1 O THR C 297 N SER C 293
SHEET 4 CF 4 HIS C 311 GLU C 314 -1 O HIS C 311 N LEU C 300
SHEET 1 CG 4 ILE C 320 TRP C 325 0
SHEET 2 CG 4 ILE C 332 GLY C 337 -1 O ALA C 334 N GLN C 324
SHEET 3 CG 4 LEU C 342 ASP C 346 -1 O ASN C 343 N SER C 335
SHEET 4 CG 4 LEU C 366 ILE C 369 -1 N LEU C 367 O VAL C 344
SHEET 1 EA 5 ILE E 377 TRP E 382 0
SHEET 2 EA 5 VAL E 389 SER E 394 -1 O CYS E 391 N SER E 381
SHEET 3 EA 5 ILE E 398 MET E 404 -1 O ILE E 398 N SER E 394
SHEET 4 EA 5 TYR E 32 ALA E 39 -1 N ASP E 33 O GLN E 403
SHEET 5 EA 5 PHE F 471 HIS F 474 -1 O PHE F 471 N THR E 37
SHEET 1 EB 3 PHE E 61 LEU E 68 0
SHEET 2 EB 3 HIS E 78 PRO E 87 -1 O VAL E 80 N LEU E 68
SHEET 3 EB 3 GLU E 116 ASN E 122 -1 O GLU E 116 N SER E 83
SHEET 1 EC 5 ARG E 129 TYR E 132 0
SHEET 2 EC 5 ILE E 139 LYS E 143 -1 O ALA E 141 N ARG E 131
SHEET 3 EC 5 VAL E 149 ASP E 153 -1 O LEU E 150 N THR E 142
SHEET 4 EC 5 LEU E 171 LEU E 173 -1 O LEU E 171 N VAL E 151
SHEET 5 EC 5 VAL E 216 VAL E 217 1 N VAL E 217 O ARG E 172
SHEET 1 ED 4 LEU E 183 TRP E 185 0
SHEET 2 ED 4 HIS E 192 ALA E 196 -1 O LEU E 194 N SER E 184
SHEET 3 ED 4 ILE E 202 ASP E 206 -1 O CYS E 203 N SER E 195
SHEET 4 ED 4 THR E 221 PHE E 223 -1 O THR E 221 N LEU E 204
SHEET 1 EE 4 VAL E 230 TRP E 235 0
SHEET 2 EE 4 LEU E 242 ALA E 247 -1 O GLY E 244 N SER E 234
SHEET 3 EE 4 LYS E 251 ASP E 256 -1 O LYS E 251 N ALA E 247
SHEET 4 EE 4 HIS E 267 ASP E 270 -1 O HIS E 267 N ILE E 254
SHEET 1 EF 4 VAL E 276 PHE E 281 0
SHEET 2 EF 4 ILE E 288 SER E 293 -1 O ALA E 290 N SER E 280
SHEET 3 EF 4 THR E 297 ASP E 302 -1 O THR E 297 N SER E 293
SHEET 4 EF 4 HIS E 311 GLU E 314 -1 O HIS E 311 N LEU E 300
SHEET 1 EG 4 ILE E 320 TRP E 325 0
SHEET 2 EG 4 ILE E 332 GLY E 337 -1 O ALA E 334 N GLN E 324
SHEET 3 EG 4 LEU E 342 ASP E 346 -1 O ASN E 343 N SER E 335
SHEET 4 EG 4 LEU E 366 HIS E 370 -1 N LEU E 367 O VAL E 344
SHEET 1 GA 5 ILE G 377 TRP G 382 0
SHEET 2 GA 5 VAL G 389 SER G 394 -1 O CYS G 391 N SER G 381
SHEET 3 GA 5 ILE G 398 MET G 404 -1 O ILE G 398 N SER G 394
SHEET 4 GA 5 TYR G 32 ALA G 39 -1 N ASP G 33 O GLN G 403
SHEET 5 GA 5 TYR H 472 HIS H 474 -1 O LEU H 473 N VAL G 35
SHEET 1 GB 3 PHE G 61 ARG G 65 0
SHEET 2 GB 3 HIS G 78 PRO G 87 -1 O VAL G 84 N HIS G 64
SHEET 3 GB 3 ILE G 117 ASN G 122 -1 N GLU G 118 O ILE G 81
SHEET 1 GC 5 ARG G 129 TYR G 132 0
SHEET 2 GC 5 ILE G 140 LYS G 143 -1 O ALA G 141 N ARG G 131
SHEET 3 GC 5 VAL G 149 VAL G 151 -1 O LEU G 150 N THR G 142
SHEET 4 GC 5 LEU G 171 LEU G 173 -1 O LEU G 171 N VAL G 151
SHEET 5 GC 5 VAL G 216 VAL G 217 1 N VAL G 217 O ARG G 172
SHEET 1 GD 4 LEU G 183 TRP G 185 0
SHEET 2 GD 4 HIS G 192 ALA G 196 -1 O LEU G 194 N SER G 184
SHEET 3 GD 4 ILE G 202 ASP G 206 -1 O CYS G 203 N SER G 195
SHEET 4 GD 4 THR G 221 PHE G 223 -1 O THR G 221 N LEU G 204
SHEET 1 GE 4 VAL G 230 TRP G 235 0
SHEET 2 GE 4 LEU G 242 ALA G 247 -1 O GLY G 244 N SER G 234
SHEET 3 GE 4 LEU G 252 ASP G 256 -1 O MET G 253 N SER G 245
SHEET 4 GE 4 HIS G 267 VAL G 269 -1 O HIS G 267 N ILE G 254
SHEET 1 GF 4 VAL G 276 PHE G 281 0
SHEET 2 GF 4 ILE G 288 SER G 293 -1 O ALA G 290 N SER G 280
SHEET 3 GF 4 THR G 297 ASP G 302 -1 O THR G 297 N SER G 293
SHEET 4 GF 4 HIS G 311 GLU G 314 -1 O HIS G 311 N LEU G 300
SHEET 1 GG 4 ILE G 320 TRP G 325 0
SHEET 2 GG 4 ILE G 332 GLY G 337 -1 O ALA G 334 N GLN G 324
SHEET 3 GG 4 ASN G 343 ASP G 346 -1 O ASN G 343 N SER G 335
SHEET 4 GG 4 LEU G 366 ILE G 369 -1 N LEU G 367 O VAL G 344
CRYST1 81.294 150.072 95.591 90.00 94.54 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 0.012301 0.000000 0.000977 0.00000
SCALE2 0.000000 0.006663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010494 0.00000
(ATOM LINES ARE NOT SHOWN.)
END