HEADER TRANSCRIPTION 31-MAR-10 2XAQ
TITLE CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH A
TITLE 2 TRANYLCYPROMINE DERIVATIVE (MC2584, 13B)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC HISTONE DEMETHYLASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LYSINE-SPECIFIC HISTONE DEMETHYLASE LSD1,
COMPND 5 FLAVIN-CONTAINING AMINE OXIDASE DOMAIN-CONTAINING PROTEIN
COMPND 6 2, BRAF35-HDAC COMPLEX PROTEIN BHC110;
COMPND 7 EC: 1.-.-.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: REST COREPRESSOR 1;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: COREPRESSOR COREST, PROTEIN COREST;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMINE OXIDASE, CHROMATIN REGULATOR, HISTONE INHIBITOR
KEYWDS 2 BINDING, METHYLATION, NUCLEOSOME CORE, OXIDOREDUCTASE,
KEYWDS 3 OXIDOREDUCTASE/REPRESSOR COMPLEX, CHROMATIN REMODELLING,
KEYWDS 4 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BINDA,S.VALENTE,M.ROMANENGHI,S.PILOTTO,R.CIRILLI,
AUTHOR 2 A.KARYTINOS,G.CIOSSANI,O.A.BOTRUGNO,F.FORNERIS,M.TARDUGNO,
AUTHOR 3 D.E.EDMONDSON,S.MINUCCI,A.MATTEVI,A.MAI
REVDAT 2 12-OCT-11 2XAQ 1 JRNL REMARK VERSN
REVDAT 1 05-MAY-10 2XAQ 0
JRNL AUTH C.BINDA,S.VALENTE,M.ROMANENGHI,S.PILOTTO,R.CIRILLI,
JRNL AUTH 2 A.KARYTINOS,G.CIOSSANI,O.A.BOTRUGNO,F.FORNERIS,
JRNL AUTH 3 M.TARDUGNO,D.E.EDMONDSON,S.MINUCCI,A.MATTEVI,A.MAI
JRNL TITL BIOCHEMICAL, STRUCTURAL, AND BIOLOGICAL EVALUATION
JRNL TITL 2 OF TRANYLCYPROMINE DERIVATIVES AS INHIBITORS OF
JRNL TITL 3 HISTONE DEMETHYLASES LSD1 AND LSD2.
JRNL REF J.AM.CHEM.SOC. V. 132 6827 2010
JRNL REFN ISSN 0002-7863
JRNL PMID 20415477
JRNL DOI 10.1021/JA101557K
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 99.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.96
REMARK 3 NUMBER OF REFLECTIONS : 41775
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) : 0.24324
REMARK 3 R VALUE (WORKING SET) : 0.24280
REMARK 3 FREE R VALUE : 0.26380
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.9
REMARK 3 FREE R VALUE TEST SET COUNT : 822
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) : 3.200
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.283
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3052
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.433
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.449
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6293
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
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) : 92.591
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.58
REMARK 3 B22 (A**2) : -16.40
REMARK 3 B33 (A**2) : 4.81
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.489
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.332
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.260
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.280
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6501 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8821 ; 2.074 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 797 ; 8.911 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 295 ;41.070 ;24.475
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1130 ;24.810 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;21.436 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 987 ; 0.143 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4898 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3984 ; 0.924 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6437 ; 1.739 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2517 ; 2.107 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2384 ; 3.730 ; 4.500
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 : 1.40
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2XAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-APR-10.
REMARK 100 THE PDBE ID CODE IS EBI-43520.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42599
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.20
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.1
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM-POTASSIUM TARTRATE, ADA
REMARK 280 BUFFER PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.05100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.17300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 117.96400
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.05100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.17300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 117.96400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.05100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.17300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 117.96400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.05100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.17300
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 117.96400
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.8 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 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 LEU A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 THR A 19
REMARK 465 GLY A 20
REMARK 465 THR A 21
REMARK 465 GLU A 22
REMARK 465 ALA A 23
REMARK 465 GLY A 24
REMARK 465 PRO A 25
REMARK 465 GLY A 26
REMARK 465 THR A 27
REMARK 465 ALA A 28
REMARK 465 GLY A 29
REMARK 465 GLY A 30
REMARK 465 SER A 31
REMARK 465 GLU A 32
REMARK 465 ASN A 33
REMARK 465 GLY A 34
REMARK 465 SER A 35
REMARK 465 GLU A 36
REMARK 465 VAL A 37
REMARK 465 ALA A 38
REMARK 465 ALA A 39
REMARK 465 GLN A 40
REMARK 465 PRO A 41
REMARK 465 ALA A 42
REMARK 465 GLY A 43
REMARK 465 LEU A 44
REMARK 465 SER A 45
REMARK 465 GLY A 46
REMARK 465 PRO A 47
REMARK 465 ALA A 48
REMARK 465 GLU A 49
REMARK 465 VAL A 50
REMARK 465 GLY A 51
REMARK 465 PRO A 52
REMARK 465 GLY A 53
REMARK 465 ALA A 54
REMARK 465 VAL A 55
REMARK 465 GLY A 56
REMARK 465 GLU A 57
REMARK 465 ARG A 58
REMARK 465 THR A 59
REMARK 465 PRO A 60
REMARK 465 ARG A 61
REMARK 465 LYS A 62
REMARK 465 LYS A 63
REMARK 465 GLU A 64
REMARK 465 PRO A 65
REMARK 465 PRO A 66
REMARK 465 ARG A 67
REMARK 465 ALA A 68
REMARK 465 SER A 69
REMARK 465 PRO A 70
REMARK 465 PRO A 71
REMARK 465 GLY A 72
REMARK 465 GLY A 73
REMARK 465 LEU A 74
REMARK 465 ALA A 75
REMARK 465 GLU A 76
REMARK 465 PRO A 77
REMARK 465 PRO A 78
REMARK 465 GLY A 79
REMARK 465 SER A 80
REMARK 465 ALA A 81
REMARK 465 GLY A 82
REMARK 465 PRO A 83
REMARK 465 GLN A 84
REMARK 465 ALA A 85
REMARK 465 GLY A 86
REMARK 465 PRO A 87
REMARK 465 THR A 88
REMARK 465 VAL A 89
REMARK 465 VAL A 90
REMARK 465 PRO A 91
REMARK 465 GLY A 92
REMARK 465 SER A 93
REMARK 465 ALA A 94
REMARK 465 THR A 95
REMARK 465 PRO A 96
REMARK 465 MET A 97
REMARK 465 GLU A 98
REMARK 465 THR A 99
REMARK 465 GLY A 100
REMARK 465 ILE A 101
REMARK 465 ALA A 102
REMARK 465 GLU A 103
REMARK 465 THR A 104
REMARK 465 PRO A 105
REMARK 465 GLU A 106
REMARK 465 GLY A 107
REMARK 465 ARG A 108
REMARK 465 ARG A 109
REMARK 465 THR A 110
REMARK 465 SER A 111
REMARK 465 ARG A 112
REMARK 465 ARG A 113
REMARK 465 LYS A 114
REMARK 465 ARG A 115
REMARK 465 ALA A 116
REMARK 465 LYS A 117
REMARK 465 VAL A 118
REMARK 465 GLU A 119
REMARK 465 TYR A 120
REMARK 465 ARG A 121
REMARK 465 GLU A 122
REMARK 465 MET A 123
REMARK 465 ASP A 124
REMARK 465 GLU A 125
REMARK 465 SER A 126
REMARK 465 LEU A 127
REMARK 465 ALA A 128
REMARK 465 ASN A 129
REMARK 465 LEU A 130
REMARK 465 SER A 131
REMARK 465 GLU A 132
REMARK 465 ASP A 133
REMARK 465 GLU A 134
REMARK 465 TYR A 135
REMARK 465 TYR A 136
REMARK 465 SER A 137
REMARK 465 GLU A 138
REMARK 465 GLU A 139
REMARK 465 GLU A 140
REMARK 465 ARG A 141
REMARK 465 ASN A 142
REMARK 465 ALA A 143
REMARK 465 LYS A 144
REMARK 465 ALA A 145
REMARK 465 GLU A 146
REMARK 465 LYS A 147
REMARK 465 GLU A 148
REMARK 465 LYS A 149
REMARK 465 LYS A 150
REMARK 465 LEU A 151
REMARK 465 PRO A 152
REMARK 465 PRO A 153
REMARK 465 PRO A 154
REMARK 465 PRO A 155
REMARK 465 PRO A 156
REMARK 465 GLN A 157
REMARK 465 ALA A 158
REMARK 465 PRO A 159
REMARK 465 PRO A 160
REMARK 465 GLU A 161
REMARK 465 GLU A 162
REMARK 465 GLU A 163
REMARK 465 ASN A 164
REMARK 465 GLU A 165
REMARK 465 SER A 166
REMARK 465 GLU A 167
REMARK 465 PRO A 168
REMARK 465 GLU A 169
REMARK 465 GLU A 170
REMARK 465 PRO A 837
REMARK 465 ARG A 838
REMARK 465 GLN A 839
REMARK 465 ALA A 840
REMARK 465 THR A 841
REMARK 465 PRO A 842
REMARK 465 GLY A 843
REMARK 465 VAL A 844
REMARK 465 PRO A 845
REMARK 465 ALA A 846
REMARK 465 GLN A 847
REMARK 465 GLN A 848
REMARK 465 SER A 849
REMARK 465 PRO A 850
REMARK 465 SER A 851
REMARK 465 MET A 852
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 GLU B 3
REMARK 465 LYS B 4
REMARK 465 GLY B 5
REMARK 465 PRO B 6
REMARK 465 GLU B 7
REMARK 465 VAL B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 LYS B 11
REMARK 465 ARG B 12
REMARK 465 ARG B 13
REMARK 465 GLY B 14
REMARK 465 ARG B 15
REMARK 465 ASN B 16
REMARK 465 ASN B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 SER B 21
REMARK 465 ALA B 22
REMARK 465 SER B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 ALA B 26
REMARK 465 ALA B 27
REMARK 465 SER B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
REMARK 465 ALA B 31
REMARK 465 SER B 32
REMARK 465 ALA B 33
REMARK 465 ALA B 34
REMARK 465 CYS B 35
REMARK 465 ALA B 36
REMARK 465 SER B 37
REMARK 465 PRO B 38
REMARK 465 ALA B 39
REMARK 465 ALA B 40
REMARK 465 THR B 41
REMARK 465 ALA B 42
REMARK 465 ALA B 43
REMARK 465 SER B 44
REMARK 465 GLY B 45
REMARK 465 ALA B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 SER B 49
REMARK 465 SER B 50
REMARK 465 ALA B 51
REMARK 465 SER B 52
REMARK 465 ALA B 53
REMARK 465 ALA B 54
REMARK 465 ALA B 55
REMARK 465 ALA B 56
REMARK 465 SER B 57
REMARK 465 ALA B 58
REMARK 465 ALA B 59
REMARK 465 ALA B 60
REMARK 465 ALA B 61
REMARK 465 PRO B 62
REMARK 465 ASN B 63
REMARK 465 ASN B 64
REMARK 465 GLY B 65
REMARK 465 GLN B 66
REMARK 465 ASN B 67
REMARK 465 LYS B 68
REMARK 465 SER B 69
REMARK 465 LEU B 70
REMARK 465 ALA B 71
REMARK 465 ALA B 72
REMARK 465 ALA B 73
REMARK 465 ALA B 74
REMARK 465 PRO B 75
REMARK 465 ASN B 76
REMARK 465 GLY B 77
REMARK 465 ASN B 78
REMARK 465 SER B 79
REMARK 465 SER B 80
REMARK 465 SER B 81
REMARK 465 ASN B 82
REMARK 465 SER B 83
REMARK 465 TRP B 84
REMARK 465 GLU B 85
REMARK 465 GLU B 86
REMARK 465 GLY B 87
REMARK 465 SER B 88
REMARK 465 SER B 89
REMARK 465 GLY B 90
REMARK 465 SER B 91
REMARK 465 SER B 92
REMARK 465 SER B 93
REMARK 465 ASP B 94
REMARK 465 GLU B 95
REMARK 465 GLU B 96
REMARK 465 HIS B 97
REMARK 465 GLY B 98
REMARK 465 GLY B 99
REMARK 465 GLY B 100
REMARK 465 GLY B 101
REMARK 465 MET B 102
REMARK 465 ARG B 103
REMARK 465 VAL B 104
REMARK 465 GLY B 105
REMARK 465 PRO B 106
REMARK 465 GLN B 107
REMARK 465 TYR B 108
REMARK 465 GLN B 109
REMARK 465 ALA B 110
REMARK 465 VAL B 111
REMARK 465 VAL B 112
REMARK 465 PRO B 113
REMARK 465 ASP B 114
REMARK 465 PHE B 115
REMARK 465 ASP B 116
REMARK 465 PRO B 117
REMARK 465 ALA B 118
REMARK 465 LYS B 119
REMARK 465 LEU B 120
REMARK 465 ALA B 121
REMARK 465 ARG B 122
REMARK 465 ARG B 123
REMARK 465 SER B 124
REMARK 465 GLN B 125
REMARK 465 GLU B 126
REMARK 465 ARG B 127
REMARK 465 ASP B 128
REMARK 465 ASN B 129
REMARK 465 LEU B 130
REMARK 465 GLY B 131
REMARK 465 MET B 132
REMARK 465 LEU B 133
REMARK 465 VAL B 134
REMARK 465 TRP B 135
REMARK 465 SER B 136
REMARK 465 PRO B 137
REMARK 465 ASN B 138
REMARK 465 GLN B 139
REMARK 465 ASN B 140
REMARK 465 LEU B 141
REMARK 465 SER B 142
REMARK 465 GLU B 143
REMARK 465 ALA B 144
REMARK 465 LYS B 145
REMARK 465 LEU B 146
REMARK 465 ASP B 147
REMARK 465 GLU B 148
REMARK 465 TYR B 149
REMARK 465 ILE B 150
REMARK 465 ALA B 151
REMARK 465 ILE B 152
REMARK 465 ALA B 153
REMARK 465 LYS B 154
REMARK 465 GLU B 155
REMARK 465 LYS B 156
REMARK 465 HIS B 157
REMARK 465 GLY B 158
REMARK 465 TYR B 159
REMARK 465 ASN B 160
REMARK 465 MET B 161
REMARK 465 GLU B 162
REMARK 465 GLN B 163
REMARK 465 ALA B 164
REMARK 465 LEU B 165
REMARK 465 GLY B 166
REMARK 465 MET B 167
REMARK 465 LEU B 168
REMARK 465 PHE B 169
REMARK 465 TRP B 170
REMARK 465 HIS B 171
REMARK 465 LYS B 172
REMARK 465 HIS B 173
REMARK 465 ASN B 174
REMARK 465 ILE B 175
REMARK 465 GLU B 176
REMARK 465 LYS B 177
REMARK 465 SER B 178
REMARK 465 LEU B 179
REMARK 465 ALA B 180
REMARK 465 ASP B 181
REMARK 465 LEU B 182
REMARK 465 PRO B 183
REMARK 465 ASN B 184
REMARK 465 PHE B 185
REMARK 465 THR B 186
REMARK 465 PRO B 187
REMARK 465 PHE B 188
REMARK 465 PRO B 189
REMARK 465 ASP B 190
REMARK 465 GLU B 191
REMARK 465 TRP B 192
REMARK 465 THR B 193
REMARK 465 VAL B 194
REMARK 465 GLU B 195
REMARK 465 ASP B 196
REMARK 465 LYS B 197
REMARK 465 VAL B 198
REMARK 465 LEU B 199
REMARK 465 PHE B 200
REMARK 465 GLU B 201
REMARK 465 GLN B 202
REMARK 465 ALA B 203
REMARK 465 PHE B 204
REMARK 465 SER B 205
REMARK 465 PHE B 206
REMARK 465 HIS B 207
REMARK 465 GLY B 208
REMARK 465 LYS B 209
REMARK 465 THR B 210
REMARK 465 PHE B 211
REMARK 465 HIS B 212
REMARK 465 ARG B 213
REMARK 465 ILE B 214
REMARK 465 GLN B 215
REMARK 465 GLN B 216
REMARK 465 MET B 217
REMARK 465 LEU B 218
REMARK 465 PRO B 219
REMARK 465 ASP B 220
REMARK 465 LYS B 221
REMARK 465 SER B 222
REMARK 465 ILE B 223
REMARK 465 ALA B 224
REMARK 465 SER B 225
REMARK 465 LEU B 226
REMARK 465 VAL B 227
REMARK 465 LYS B 228
REMARK 465 PHE B 229
REMARK 465 TYR B 230
REMARK 465 TYR B 231
REMARK 465 SER B 232
REMARK 465 TRP B 233
REMARK 465 LYS B 234
REMARK 465 LYS B 235
REMARK 465 THR B 236
REMARK 465 ARG B 237
REMARK 465 THR B 238
REMARK 465 LYS B 239
REMARK 465 THR B 240
REMARK 465 SER B 241
REMARK 465 VAL B 242
REMARK 465 MET B 243
REMARK 465 ASP B 244
REMARK 465 ARG B 245
REMARK 465 HIS B 246
REMARK 465 ALA B 247
REMARK 465 ARG B 248
REMARK 465 LYS B 249
REMARK 465 GLN B 250
REMARK 465 LYS B 251
REMARK 465 ARG B 252
REMARK 465 GLU B 253
REMARK 465 ARG B 254
REMARK 465 GLU B 255
REMARK 465 GLU B 256
REMARK 465 SER B 257
REMARK 465 GLU B 258
REMARK 465 ASP B 259
REMARK 465 GLU B 260
REMARK 465 LEU B 261
REMARK 465 GLU B 262
REMARK 465 GLU B 263
REMARK 465 ALA B 264
REMARK 465 ASN B 265
REMARK 465 GLY B 266
REMARK 465 ASN B 267
REMARK 465 ASN B 268
REMARK 465 PRO B 269
REMARK 465 ILE B 270
REMARK 465 ASP B 271
REMARK 465 ILE B 272
REMARK 465 GLU B 273
REMARK 465 VAL B 274
REMARK 465 ASP B 275
REMARK 465 GLN B 276
REMARK 465 ASN B 277
REMARK 465 LYS B 278
REMARK 465 GLU B 279
REMARK 465 SER B 280
REMARK 465 LYS B 281
REMARK 465 LYS B 282
REMARK 465 GLU B 283
REMARK 465 VAL B 284
REMARK 465 PRO B 285
REMARK 465 PRO B 286
REMARK 465 THR B 287
REMARK 465 GLU B 288
REMARK 465 THR B 289
REMARK 465 VAL B 290
REMARK 465 PRO B 291
REMARK 465 GLN B 292
REMARK 465 VAL B 293
REMARK 465 LYS B 294
REMARK 465 LYS B 295
REMARK 465 GLU B 296
REMARK 465 LYS B 297
REMARK 465 HIS B 298
REMARK 465 SER B 299
REMARK 465 THR B 300
REMARK 465 GLN B 301
REMARK 465 ALA B 302
REMARK 465 LYS B 303
REMARK 465 ASN B 304
REMARK 465 ARG B 305
REMARK 465 ALA B 306
REMARK 465 LYS B 307
REMARK 465 HIS B 441
REMARK 465 GLY B 442
REMARK 465 LYS B 443
REMARK 465 GLU B 444
REMARK 465 GLU B 445
REMARK 465 THR B 446
REMARK 465 ASN B 447
REMARK 465 GLY B 448
REMARK 465 PRO B 449
REMARK 465 SER B 450
REMARK 465 ASN B 451
REMARK 465 GLN B 452
REMARK 465 LYS B 453
REMARK 465 PRO B 454
REMARK 465 VAL B 455
REMARK 465 LYS B 456
REMARK 465 SER B 457
REMARK 465 PRO B 458
REMARK 465 ASP B 459
REMARK 465 ASN B 460
REMARK 465 SER B 461
REMARK 465 ILE B 462
REMARK 465 LYS B 463
REMARK 465 MET B 464
REMARK 465 PRO B 465
REMARK 465 GLU B 466
REMARK 465 GLU B 467
REMARK 465 GLU B 468
REMARK 465 ASP B 469
REMARK 465 GLU B 470
REMARK 465 ALA B 471
REMARK 465 PRO B 472
REMARK 465 VAL B 473
REMARK 465 LEU B 474
REMARK 465 ASP B 475
REMARK 465 VAL B 476
REMARK 465 ARG B 477
REMARK 465 TYR B 478
REMARK 465 ALA B 479
REMARK 465 SER B 480
REMARK 465 ALA B 481
REMARK 465 SER B 482
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 ILE A 284 OG1 THR A 624 2.06
REMARK 500 OE1 GLU A 308 O3B FAD A 900 2.04
REMARK 500 OG1 THR A 319 OD1 ASP A 328 2.01
REMARK 500 OD1 ASP A 486 OH TYR B 398 2.05
REMARK 500 O GLU A 506 N LEU A 508 2.13
REMARK 500 O ASP A 525 N GLN A 527 2.05
REMARK 500 O ILE A 528 N TRP A 531 2.18
REMARK 500 OD1 ASN A 660 O SER A 749 2.13
REMARK 500 OG SER B 406 O LYS B 412 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 801 CD GLU A 801 OE1 0.079
REMARK 500 GLU A 821 CD GLU A 821 OE2 0.072
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 543 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASP A 774 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU A 815 CA - CB - CG ANGL. DEV. = 21.9 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 ARG A 182 36.80 86.57
REMARK 500 GLU A 192 -73.04 -71.12
REMARK 500 ALA A 193 -42.99 -29.79
REMARK 500 LEU A 211 -76.73 -50.13
REMARK 500 LEU A 222 -76.87 -60.65
REMARK 500 ASP A 223 -8.40 -35.43
REMARK 500 ASN A 224 107.09 -171.25
REMARK 500 GLU A 232 -71.89 -57.52
REMARK 500 ALA A 233 -29.94 -36.65
REMARK 500 GLN A 236 -65.85 -22.01
REMARK 500 LEU A 248 -103.60 -60.98
REMARK 500 VAL A 249 -72.40 3.83
REMARK 500 VAL A 252 -72.76 -38.67
REMARK 500 TYR A 255 -76.08 -68.07
REMARK 500 LEU A 256 -78.84 -29.02
REMARK 500 GLU A 257 -33.86 -29.97
REMARK 500 PRO A 272 168.29 -37.17
REMARK 500 PRO A 274 83.01 -14.41
REMARK 500 THR A 275 -59.26 1.79
REMARK 500 VAL A 288 -88.96 -33.35
REMARK 500 SER A 289 -74.34 -12.47
REMARK 500 ALA A 292 -18.75 -35.08
REMARK 500 ARG A 295 -81.79 -57.72
REMARK 500 GLN A 296 -54.69 -25.15
REMARK 500 ARG A 316 21.66 -76.64
REMARK 500 MET A 332 -41.33 -164.35
REMARK 500 PRO A 341 -33.51 -37.37
REMARK 500 LYS A 355 -175.13 -63.65
REMARK 500 GLU A 364 152.34 -35.03
REMARK 500 ALA A 369 136.90 -29.27
REMARK 500 TYR A 391 -49.40 -26.84
REMARK 500 ASN A 403 -44.72 84.45
REMARK 500 GLN A 410 -58.46 -19.46
REMARK 500 LEU A 418 -9.78 -52.72
REMARK 500 LYS A 421 -78.57 -33.87
REMARK 500 LYS A 424 -71.76 -55.26
REMARK 500 ASP A 425 -33.88 -30.16
REMARK 500 LYS A 432 0.71 -42.61
REMARK 500 VAL A 435 -73.34 -45.74
REMARK 500 LYS A 436 -19.25 -37.20
REMARK 500 LYS A 442 -73.21 -35.12
REMARK 500 GLU A 443 -30.37 -35.84
REMARK 500 ASN A 450 9.93 -57.08
REMARK 500 GLU A 453 -85.84 -49.10
REMARK 500 GLN A 460 -76.16 -31.27
REMARK 500 VAL A 468 82.14 -40.06
REMARK 500 PRO A 470 164.10 -48.21
REMARK 500 SER A 482 -72.40 -42.25
REMARK 500 ARG A 485 -80.00 -40.10
REMARK 500 ASP A 486 -21.59 -33.12
REMARK 500
REMARK 500 THIS ENTRY HAS 136 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 627 GLY A 628 146.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 747 24.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 MC2584 IS AN INHIBITOR THAT HAS REACTED COVALENTLY
REMARK 600 WITH FAD. THE COVALENT LINKAGE IS BETWEEN THE N5 ATOM OF
REMARK 600 FAD AND THE C1B ATOM OF M84.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M84 A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XAJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX
REMARK 900 WITH (-)-TRANS-2-PHENYLCYCLOPROPYL-1-AMINE
REMARK 900 RELATED ID: 2X0L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A NEURO-SPECIFIC
REMARK 900 SPLICING VARIANT OF HUMAN HISTONE LYSINE
REMARK 900 DEMETHYLASE LSD1.
REMARK 900 RELATED ID: 2UXX RELATED DB: PDB
REMARK 900 HUMAN LSD1 HISTONE DEMETHYLASE-COREST IN
REMARK 900 COMPLEX WITH AN FAD-TRANYLCYPROMINE ADDUCT
REMARK 900 RELATED ID: 2IW5 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR COREST-DEPENDENT
REMARK 900 DEMETHYLATION OF NUCLEOSOMES BY THE HUMAN
REMARK 900 LSD1 HISTONE DEMETHYLASE
REMARK 900 RELATED ID: 2V1D RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY
REMARK 900 IN HISTONE H3 RECOGNITION
REMARK 900 RELATED ID: 2UXN RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF HISTONE DEMETHYLATION BY
REMARK 900 LSD1 REVEALED BY SUICIDE INACTIVATION
REMARK 900 RELATED ID: 2H94 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE AND MECHANISM OF HUMAN
REMARK 900 LYSINE-SPECIFICDEMETHYLASE-1
REMARK 900 RELATED ID: 2COM RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF THE 33RD
REMARK 900 FIBRONECTIN TYPE IIIDOMAIN OF HUMAN TENASCIN-X
REMARK 900 RELATED ID: 2XAG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX
REMARK 900 WITH PARA-BROMO-(-)-TRANS-2-
REMARK 900 PHENYLCYCLOPROPYL-1-AMINE
REMARK 900 RELATED ID: 2XAF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX
REMARK 900 WITH PARA-BROMO-CIS-2-PHENYLCYCLOPROPYL-1
REMARK 900 -AMINE
REMARK 900 RELATED ID: 2XAH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX
REMARK 900 WITH (PLUS)-TRANS-2-PHENYLCYCLOPROPYL-1-
REMARK 900 AMINE
REMARK 900 RELATED ID: 2XAS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX
REMARK 900 WITH A TRANYCYPROMINE DERIVATIVE (MC2580,
REMARK 900 14E)
DBREF 2XAQ A 1 852 UNP O60341 KDM1_HUMAN 1 852
DBREF 2XAQ B 1 482 UNP Q9UKL0 RCOR1_HUMAN 1 482
SEQRES 1 A 852 MET LEU SER GLY LYS LYS ALA ALA ALA ALA ALA ALA ALA
SEQRES 2 A 852 ALA ALA ALA ALA ALA THR GLY THR GLU ALA GLY PRO GLY
SEQRES 3 A 852 THR ALA GLY GLY SER GLU ASN GLY SER GLU VAL ALA ALA
SEQRES 4 A 852 GLN PRO ALA GLY LEU SER GLY PRO ALA GLU VAL GLY PRO
SEQRES 5 A 852 GLY ALA VAL GLY GLU ARG THR PRO ARG LYS LYS GLU PRO
SEQRES 6 A 852 PRO ARG ALA SER PRO PRO GLY GLY LEU ALA GLU PRO PRO
SEQRES 7 A 852 GLY SER ALA GLY PRO GLN ALA GLY PRO THR VAL VAL PRO
SEQRES 8 A 852 GLY SER ALA THR PRO MET GLU THR GLY ILE ALA GLU THR
SEQRES 9 A 852 PRO GLU GLY ARG ARG THR SER ARG ARG LYS ARG ALA LYS
SEQRES 10 A 852 VAL GLU TYR ARG GLU MET ASP GLU SER LEU ALA ASN LEU
SEQRES 11 A 852 SER GLU ASP GLU TYR TYR SER GLU GLU GLU ARG ASN ALA
SEQRES 12 A 852 LYS ALA GLU LYS GLU LYS LYS LEU PRO PRO PRO PRO PRO
SEQRES 13 A 852 GLN ALA PRO PRO GLU GLU GLU ASN GLU SER GLU PRO GLU
SEQRES 14 A 852 GLU PRO SER GLY VAL GLU GLY ALA ALA PHE GLN SER ARG
SEQRES 15 A 852 LEU PRO HIS ASP ARG MET THR SER GLN GLU ALA ALA CYS
SEQRES 16 A 852 PHE PRO ASP ILE ILE SER GLY PRO GLN GLN THR GLN LYS
SEQRES 17 A 852 VAL PHE LEU PHE ILE ARG ASN ARG THR LEU GLN LEU TRP
SEQRES 18 A 852 LEU ASP ASN PRO LYS ILE GLN LEU THR PHE GLU ALA THR
SEQRES 19 A 852 LEU GLN GLN LEU GLU ALA PRO TYR ASN SER ASP THR VAL
SEQRES 20 A 852 LEU VAL HIS ARG VAL HIS SER TYR LEU GLU ARG HIS GLY
SEQRES 21 A 852 LEU ILE ASN PHE GLY ILE TYR LYS ARG ILE LYS PRO LEU
SEQRES 22 A 852 PRO THR LYS LYS THR GLY LYS VAL ILE ILE ILE GLY SER
SEQRES 23 A 852 GLY VAL SER GLY LEU ALA ALA ALA ARG GLN LEU GLN SER
SEQRES 24 A 852 PHE GLY MET ASP VAL THR LEU LEU GLU ALA ARG ASP ARG
SEQRES 25 A 852 VAL GLY GLY ARG VAL ALA THR PHE ARG LYS GLY ASN TYR
SEQRES 26 A 852 VAL ALA ASP LEU GLY ALA MET VAL VAL THR GLY LEU GLY
SEQRES 27 A 852 GLY ASN PRO MET ALA VAL VAL SER LYS GLN VAL ASN MET
SEQRES 28 A 852 GLU LEU ALA LYS ILE LYS GLN LYS CYS PRO LEU TYR GLU
SEQRES 29 A 852 ALA ASN GLY GLN ALA VAL PRO LYS GLU LYS ASP GLU MET
SEQRES 30 A 852 VAL GLU GLN GLU PHE ASN ARG LEU LEU GLU ALA THR SER
SEQRES 31 A 852 TYR LEU SER HIS GLN LEU ASP PHE ASN VAL LEU ASN ASN
SEQRES 32 A 852 LYS PRO VAL SER LEU GLY GLN ALA LEU GLU VAL VAL ILE
SEQRES 33 A 852 GLN LEU GLN GLU LYS HIS VAL LYS ASP GLU GLN ILE GLU
SEQRES 34 A 852 HIS TRP LYS LYS ILE VAL LYS THR GLN GLU GLU LEU LYS
SEQRES 35 A 852 GLU LEU LEU ASN LYS MET VAL ASN LEU LYS GLU LYS ILE
SEQRES 36 A 852 LYS GLU LEU HIS GLN GLN TYR LYS GLU ALA SER GLU VAL
SEQRES 37 A 852 LYS PRO PRO ARG ASP ILE THR ALA GLU PHE LEU VAL LYS
SEQRES 38 A 852 SER LYS HIS ARG ASP LEU THR ALA LEU CYS LYS GLU TYR
SEQRES 39 A 852 ASP GLU LEU ALA GLU THR GLN GLY LYS LEU GLU GLU LYS
SEQRES 40 A 852 LEU GLN GLU LEU GLU ALA ASN PRO PRO SER ASP VAL TYR
SEQRES 41 A 852 LEU SER SER ARG ASP ARG GLN ILE LEU ASP TRP HIS PHE
SEQRES 42 A 852 ALA ASN LEU GLU PHE ALA ASN ALA THR PRO LEU SER THR
SEQRES 43 A 852 LEU SER LEU LYS HIS TRP ASP GLN ASP ASP ASP PHE GLU
SEQRES 44 A 852 PHE THR GLY SER HIS LEU THR VAL ARG ASN GLY TYR SER
SEQRES 45 A 852 CYS VAL PRO VAL ALA LEU ALA GLU GLY LEU ASP ILE LYS
SEQRES 46 A 852 LEU ASN THR ALA VAL ARG GLN VAL ARG TYR THR ALA SER
SEQRES 47 A 852 GLY CYS GLU VAL ILE ALA VAL ASN THR ARG SER THR SER
SEQRES 48 A 852 GLN THR PHE ILE TYR LYS CYS ASP ALA VAL LEU CYS THR
SEQRES 49 A 852 LEU PRO LEU GLY VAL LEU LYS GLN GLN PRO PRO ALA VAL
SEQRES 50 A 852 GLN PHE VAL PRO PRO LEU PRO GLU TRP LYS THR SER ALA
SEQRES 51 A 852 VAL GLN ARG MET GLY PHE GLY ASN LEU ASN LYS VAL VAL
SEQRES 52 A 852 LEU CYS PHE ASP ARG VAL PHE TRP ASP PRO SER VAL ASN
SEQRES 53 A 852 LEU PHE GLY HIS VAL GLY SER THR THR ALA SER ARG GLY
SEQRES 54 A 852 GLU LEU PHE LEU PHE TRP ASN LEU TYR LYS ALA PRO ILE
SEQRES 55 A 852 LEU LEU ALA LEU VAL ALA GLY GLU ALA ALA GLY ILE MET
SEQRES 56 A 852 GLU ASN ILE SER ASP ASP VAL ILE VAL GLY ARG CYS LEU
SEQRES 57 A 852 ALA ILE LEU LYS GLY ILE PHE GLY SER SER ALA VAL PRO
SEQRES 58 A 852 GLN PRO LYS GLU THR VAL VAL SER ARG TRP ARG ALA ASP
SEQRES 59 A 852 PRO TRP ALA ARG GLY SER TYR SER TYR VAL ALA ALA GLY
SEQRES 60 A 852 SER SER GLY ASN ASP TYR ASP LEU MET ALA GLN PRO ILE
SEQRES 61 A 852 THR PRO GLY PRO SER ILE PRO GLY ALA PRO GLN PRO ILE
SEQRES 62 A 852 PRO ARG LEU PHE PHE ALA GLY GLU HIS THR ILE ARG ASN
SEQRES 63 A 852 TYR PRO ALA THR VAL HIS GLY ALA LEU LEU SER GLY LEU
SEQRES 64 A 852 ARG GLU ALA GLY ARG ILE ALA ASP GLN PHE LEU GLY ALA
SEQRES 65 A 852 MET TYR THR LEU PRO ARG GLN ALA THR PRO GLY VAL PRO
SEQRES 66 A 852 ALA GLN GLN SER PRO SER MET
SEQRES 1 B 482 MET VAL GLU LYS GLY PRO GLU VAL SER GLY LYS ARG ARG
SEQRES 2 B 482 GLY ARG ASN ASN ALA ALA ALA SER ALA SER ALA ALA ALA
SEQRES 3 B 482 ALA SER ALA ALA ALA SER ALA ALA CYS ALA SER PRO ALA
SEQRES 4 B 482 ALA THR ALA ALA SER GLY ALA ALA ALA SER SER ALA SER
SEQRES 5 B 482 ALA ALA ALA ALA SER ALA ALA ALA ALA PRO ASN ASN GLY
SEQRES 6 B 482 GLN ASN LYS SER LEU ALA ALA ALA ALA PRO ASN GLY ASN
SEQRES 7 B 482 SER SER SER ASN SER TRP GLU GLU GLY SER SER GLY SER
SEQRES 8 B 482 SER SER ASP GLU GLU HIS GLY GLY GLY GLY MET ARG VAL
SEQRES 9 B 482 GLY PRO GLN TYR GLN ALA VAL VAL PRO ASP PHE ASP PRO
SEQRES 10 B 482 ALA LYS LEU ALA ARG ARG SER GLN GLU ARG ASP ASN LEU
SEQRES 11 B 482 GLY MET LEU VAL TRP SER PRO ASN GLN ASN LEU SER GLU
SEQRES 12 B 482 ALA LYS LEU ASP GLU TYR ILE ALA ILE ALA LYS GLU LYS
SEQRES 13 B 482 HIS GLY TYR ASN MET GLU GLN ALA LEU GLY MET LEU PHE
SEQRES 14 B 482 TRP HIS LYS HIS ASN ILE GLU LYS SER LEU ALA ASP LEU
SEQRES 15 B 482 PRO ASN PHE THR PRO PHE PRO ASP GLU TRP THR VAL GLU
SEQRES 16 B 482 ASP LYS VAL LEU PHE GLU GLN ALA PHE SER PHE HIS GLY
SEQRES 17 B 482 LYS THR PHE HIS ARG ILE GLN GLN MET LEU PRO ASP LYS
SEQRES 18 B 482 SER ILE ALA SER LEU VAL LYS PHE TYR TYR SER TRP LYS
SEQRES 19 B 482 LYS THR ARG THR LYS THR SER VAL MET ASP ARG HIS ALA
SEQRES 20 B 482 ARG LYS GLN LYS ARG GLU ARG GLU GLU SER GLU ASP GLU
SEQRES 21 B 482 LEU GLU GLU ALA ASN GLY ASN ASN PRO ILE ASP ILE GLU
SEQRES 22 B 482 VAL ASP GLN ASN LYS GLU SER LYS LYS GLU VAL PRO PRO
SEQRES 23 B 482 THR GLU THR VAL PRO GLN VAL LYS LYS GLU LYS HIS SER
SEQRES 24 B 482 THR GLN ALA LYS ASN ARG ALA LYS ARG LYS PRO PRO LYS
SEQRES 25 B 482 GLY MET PHE LEU SER GLN GLU ASP VAL GLU ALA VAL SER
SEQRES 26 B 482 ALA ASN ALA THR ALA ALA THR THR VAL LEU ARG GLN LEU
SEQRES 27 B 482 ASP MET GLU LEU VAL SER VAL LYS ARG GLN ILE GLN ASN
SEQRES 28 B 482 ILE LYS GLN THR ASN SER ALA LEU LYS GLU LYS LEU ASP
SEQRES 29 B 482 GLY GLY ILE GLU PRO TYR ARG LEU PRO GLU VAL ILE GLN
SEQRES 30 B 482 LYS CYS ASN ALA ARG TRP THR THR GLU GLU GLN LEU LEU
SEQRES 31 B 482 ALA VAL GLN ALA ILE ARG LYS TYR GLY ARG ASP PHE GLN
SEQRES 32 B 482 ALA ILE SER ASP VAL ILE GLY ASN LYS SER VAL VAL GLN
SEQRES 33 B 482 VAL LYS ASN PHE PHE VAL ASN TYR ARG ARG ARG PHE ASN
SEQRES 34 B 482 ILE ASP GLU VAL LEU GLN GLU TRP GLU ALA GLU HIS GLY
SEQRES 35 B 482 LYS GLU GLU THR ASN GLY PRO SER ASN GLN LYS PRO VAL
SEQRES 36 B 482 LYS SER PRO ASP ASN SER ILE LYS MET PRO GLU GLU GLU
SEQRES 37 B 482 ASP GLU ALA PRO VAL LEU ASP VAL ARG TYR ALA SER ALA
SEQRES 38 B 482 SER
HET FAD A 900 53
HET M84 A 901 19
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM M84 3-{4-[(PHENYLCARBONYL)AMINO]PHENYL}PROPANOIC
HETNAM 2 M84 ACID
FORMUL 3 FAD C27 H33 N9 O15 P2
FORMUL 4 M84 C16 H15 N O3
HELIX 1 1 GLY A 173 GLN A 180 1 8
HELIX 2 2 THR A 189 ALA A 194 1 6
HELIX 3 3 PHE A 196 GLY A 202 1 7
HELIX 4 4 PRO A 203 ASN A 224 1 22
HELIX 5 5 THR A 230 GLN A 237 1 8
HELIX 6 6 ASP A 245 HIS A 259 1 15
HELIX 7 7 GLY A 287 PHE A 300 1 14
HELIX 8 8 ASN A 340 VAL A 349 1 10
HELIX 9 9 PRO A 371 LEU A 396 1 26
HELIX 10 10 SER A 407 LYS A 432 1 26
HELIX 11 11 ILE A 434 VAL A 468 1 35
HELIX 12 12 ASP A 473 LYS A 507 1 35
HELIX 13 13 LEU A 508 ASN A 514 1 7
HELIX 14 14 ARG A 524 GLN A 527 5 4
HELIX 15 15 ILE A 528 ASN A 540 1 13
HELIX 16 16 SER A 572 ALA A 579 1 8
HELIX 17 17 PRO A 626 GLN A 632 1 7
HELIX 18 18 PRO A 644 MET A 654 1 11
HELIX 19 19 ALA A 711 GLU A 716 1 6
HELIX 20 20 SER A 719 GLY A 736 1 18
HELIX 21 21 GLY A 770 GLN A 778 1 9
HELIX 22 22 THR A 810 GLY A 831 1 22
HELIX 23 23 ALA A 832 LEU A 836 5 5
HELIX 24 24 SER B 317 VAL B 324 1 8
HELIX 25 25 THR B 329 LYS B 362 1 34
HELIX 26 26 ILE B 367 ARG B 371 5 5
HELIX 27 27 THR B 384 GLY B 399 1 16
HELIX 28 28 GLN B 403 GLY B 410 1 8
HELIX 29 29 SER B 413 TYR B 424 1 12
HELIX 30 30 ASN B 429 ALA B 439 1 11
SHEET 1 AA 5 ASP A 583 LYS A 585 0
SHEET 2 AA 5 ASP A 303 LEU A 307 1 O VAL A 304 N ASP A 583
SHEET 3 AA 5 LYS A 280 ILE A 284 1 O VAL A 281 N THR A 305
SHEET 4 AA 5 ALA A 620 CYS A 623 1 O ALA A 620 N ILE A 282
SHEET 5 AA 5 LEU A 796 PHE A 798 1 O PHE A 797 N CYS A 623
SHEET 1 AB 2 PHE A 320 LYS A 322 0
SHEET 2 AB 2 TYR A 325 ALA A 327 -1 O TYR A 325 N LYS A 322
SHEET 1 AC 3 VAL A 333 VAL A 334 0
SHEET 2 AC 3 LEU A 565 VAL A 567 -1 O LEU A 565 N VAL A 334
SHEET 3 AC 3 LEU A 353 LYS A 355 -1 O ALA A 354 N THR A 566
SHEET 1 AD 2 VAL A 400 LEU A 401 0
SHEET 2 AD 2 LYS A 404 PRO A 405 -1 O LYS A 404 N LEU A 401
SHEET 1 AE 4 THR A 613 CYS A 618 0
SHEET 2 AE 4 GLY A 599 ASN A 606 -1 O CYS A 600 N CYS A 618
SHEET 3 AE 4 THR A 588 THR A 596 -1 O ALA A 589 N VAL A 605
SHEET 4 AE 4 GLN A 638 VAL A 640 1 O GLN A 638 N VAL A 593
SHEET 1 AF 5 LEU A 677 PHE A 678 0
SHEET 2 AF 5 PHE A 694 ASN A 696 -1 O PHE A 694 N PHE A 678
SHEET 3 AF 5 ILE A 702 VAL A 707 -1 O LEU A 704 N TRP A 695
SHEET 4 AF 5 ASN A 660 CYS A 665 -1 O ASN A 660 N VAL A 707
SHEET 5 AF 5 GLU A 745 VAL A 748 -1 O GLU A 745 N CYS A 665
LINK N5 FAD A 900 C1B M84 A 901 1555 1555 1.41
CISPEP 1 ALA A 240 PRO A 241 0 4.12
CISPEP 2 PRO A 470 PRO A 471 0 -6.95
CISPEP 3 GLN A 633 PRO A 634 0 8.86
CISPEP 4 VAL A 640 PRO A 641 0 7.62
SITE 1 AC1 31 GLY A 285 SER A 286 GLY A 287 VAL A 288
SITE 2 AC1 31 SER A 289 GLU A 308 ALA A 309 ARG A 310
SITE 3 AC1 31 GLY A 314 GLY A 315 ARG A 316 LEU A 329
SITE 4 AC1 31 GLY A 330 ALA A 331 MET A 332 VAL A 333
SITE 5 AC1 31 THR A 588 ALA A 589 VAL A 590 LEU A 625
SITE 6 AC1 31 PRO A 626 TRP A 751 SER A 760 TYR A 761
SITE 7 AC1 31 GLY A 800 GLU A 801 ALA A 809 THR A 810
SITE 8 AC1 31 VAL A 811 ALA A 814 M84 A 901
SITE 1 AC2 7 THR A 335 ASP A 556 GLU A 559 TYR A 761
SITE 2 AC2 7 ALA A 809 THR A 810 FAD A 900
CRYST1 120.102 180.346 235.928 90.00 90.00 90.00 I 2 2 2 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 0.008326 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005545 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004239 0.00000
(ATOM LINES ARE NOT SHOWN.)
END