HEADER OXIDOREDUCTASE 05-JAN-11 2Y48
TITLE CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH A N-TERMINAL SNAIL
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 1A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 123-852;
COMPND 5 SYNONYM: LYSINE-SPECIFIC DEMETHYLASE 1, BRAF35-HDAC COMPLEX PROTEIN
COMPND 6 BHC110, FLAVIN-CONTAINING AMINE OXIDASE DOMAIN-CONTAINING PROTEIN 2;
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 FRAGMENT: RESIDUES 305-482;
COMPND 13 SYNONYM: COREPRESSOR COREST, PROTEIN COREST;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: ZINC FINGER PROTEIN SNAI1;
COMPND 17 CHAIN: C;
COMPND 18 FRAGMENT: N-TERMINAL 20 AMINO ACIDS TAIL, RESIUDES 2-21;
COMPND 19 SYNONYM: TRANSCRIPTION FACTOR SNAIL, PROTEIN SNAIL HOMOLOG 1, PROTEIN
COMPND 20 SNA;
COMPND 21 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606
KEYWDS OXIDOREDUCTASE, FLAVIN, HISTONE, REPRESSOR, TRANSCRIPTION REGULATION,
KEYWDS 2 CHROMATIN, NUCLEAR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BARON,C.BINDA,M.TORTORICI,J.A.MCCAMMON,A.MATTEVI
REVDAT 2 20-DEC-23 2Y48 1 REMARK
REVDAT 1 16-FEB-11 2Y48 0
JRNL AUTH R.BARON,C.BINDA,M.TORTORICI,J.A.MCCAMMON,A.MATTEVI
JRNL TITL MOLECULAR MIMICRY AND LIGAND RECOGNITION IN BINDING AND
JRNL TITL 2 CATALYSIS BY THE HISTONE DEMETHYLASE LSD1-COREST COMPLEX.
JRNL REF STRUCTURE V. 19 212 2011
JRNL REFN ISSN 0969-2126
JRNL PMID 21300290
JRNL DOI 10.1016/J.STR.2011.01.001
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 49943
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.900
REMARK 3 FREE R VALUE TEST SET COUNT : 992
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3666
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6363
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
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) : 77.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.75000
REMARK 3 B22 (A**2) : -3.24000
REMARK 3 B33 (A**2) : -1.50000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.330
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.266
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.219
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.084
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.871
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6551 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8885 ; 1.493 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 804 ; 6.318 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 298 ;38.038 ;24.362
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1145 ;21.126 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;18.580 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 994 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4924 ; 0.006 ; 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): 4024 ; 0.785 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6502 ; 1.520 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2527 ; 1.775 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2383 ; 3.213 ; 4.500
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 : 1.40
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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2Y48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1290046899.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-10
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50937
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 70.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.64000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2V1D
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM/POTASSIUM TARTRATE, 100
REMARK 280 MM ADA 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 59.58500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.73000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 117.22000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 59.58500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.73000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 117.22000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 59.58500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.73000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 117.22000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 59.58500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.73000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 117.22000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 171
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 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 465 SER C 10
REMARK 465 ASP C 11
REMARK 465 PRO C 12
REMARK 465 ASN C 13
REMARK 465 ARG C 14
REMARK 465 LYS C 15
REMARK 465 PRO C 16
REMARK 465 ASN C 17
REMARK 465 TYR C 18
REMARK 465 SER C 19
REMARK 465 GLU C 20
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 635 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 196 44.69 -141.32
REMARK 500 PRO A 272 152.58 -39.86
REMARK 500 PRO A 274 121.86 -25.54
REMARK 500 LYS A 322 117.26 179.49
REMARK 500 ASN A 350 90.67 -65.47
REMARK 500 GLU A 364 172.45 -49.67
REMARK 500 ASN A 403 -33.38 77.72
REMARK 500 ASP A 425 -38.23 -33.34
REMARK 500 VAL A 468 93.12 -54.76
REMARK 500 SER A 482 -70.19 -53.59
REMARK 500 TYR A 494 -5.18 -54.68
REMARK 500 LYS A 507 -1.97 -59.08
REMARK 500 GLU A 510 -76.55 -59.34
REMARK 500 ASN A 514 77.75 -108.97
REMARK 500 PRO A 543 121.50 -38.03
REMARK 500 ALA A 597 -19.62 -46.21
REMARK 500 SER A 737 3.61 -49.40
REMARK 500 SER A 738 18.61 -152.81
REMARK 500 ALA A 757 -57.47 -143.97
REMARK 500 SER A 768 -166.89 -102.96
REMARK 500 SER A 769 -175.64 -171.36
REMARK 500 SER A 785 -77.05 -73.08
REMARK 500 ILE A 793 143.94 -25.00
REMARK 500 TYR A 807 43.60 -144.45
REMARK 500 ALA A 832 77.61 -115.45
REMARK 500 PRO B 310 171.23 -51.52
REMARK 500 LEU B 316 88.60 -159.41
REMARK 500 ALA B 326 -9.69 -53.59
REMARK 500 ASN B 327 -166.55 -166.85
REMARK 500 PRO B 369 21.78 -79.48
REMARK 500 PRO B 373 145.08 -35.12
REMARK 500 ILE B 376 78.32 -113.55
REMARK 500 TYR B 398 13.39 -141.13
REMARK 500 ASP B 401 77.07 -64.08
REMARK 500 ASN B 429 52.34 20.15
REMARK 500 ALA B 439 2.82 -57.95
REMARK 500 SER C 3 -14.72 -46.34
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 PRO A 792 ILE A 793 142.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X0L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A NEURO-SPECIFIC SPLICING VARIANT OF HUMAN
REMARK 900 HISTONE LYSINE DEMETHYLASE LSD1.
REMARK 900 RELATED ID: 2UXX RELATED DB: PDB
REMARK 900 HUMAN LSD1 HISTONE DEMETHYLASE-COREST IN COMPLEX WITH AN FAD-
REMARK 900 TRANYLCYPROMINE ADDUCT
REMARK 900 RELATED ID: 2XAQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH A TRANYLCYPROMINE
REMARK 900 DERIVATIVE (MC2584, 13B)
REMARK 900 RELATED ID: 2XAF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH PARA-BROMO-(+)-CIS-
REMARK 900 2-PHENYLCYCLOPROPYL-1-AMINE
REMARK 900 RELATED ID: 2IW5 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR COREST-DEPENDENT DEMETHYLATION OF NUCLEOSOMES
REMARK 900 BY THE HUMAN LSD1 HISTONE DEMETHYLASE
REMARK 900 RELATED ID: 2COM RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF THE 33RD FIBRONECTIN TYPE IIIDOMAIN OF
REMARK 900 HUMAN TENASCIN-X
REMARK 900 RELATED ID: 2XAJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH (-)-TRANS-2-
REMARK 900 PHENYLCYCLOPROPYL-1-AMINE
REMARK 900 RELATED ID: 2XAG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH PARA-BROMO-(-)-
REMARK 900 TRANS-2- PHENYLCYCLOPROPYL-1-AMINE
REMARK 900 RELATED ID: 2V1D RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF LSD1-COREST SELECTIVITY IN HISTONE H3
REMARK 900 RECOGNITION
REMARK 900 RELATED ID: 2XAH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH (+)-TRANS-2-
REMARK 900 PHENYLCYCLOPROPYL-1-AMINE
REMARK 900 RELATED ID: 2UXN RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS OF HISTONE DEMETHYLATION BY LSD1 REVEALED BY
REMARK 900 SUICIDE INACTIVATION
REMARK 900 RELATED ID: 2XAS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LSD1-COREST IN COMPLEX WITH A TRANYLCYPROMINE
REMARK 900 DERIVATIVE (MC2580, 14E)
REMARK 900 RELATED ID: 2H94 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE AND MECHANISM OF HUMAN LYSINE-SPECIFICDEMETHYLASE-
REMARK 900 1
DBREF 2Y48 A 123 852 UNP O60341 KDM1A_HUMAN 123 852
DBREF 2Y48 B 305 482 UNP Q9UKL0 RCOR1_HUMAN 305 482
DBREF 2Y48 C 1 20 UNP O95863 SNAI1_HUMAN 2 21
SEQRES 1 A 730 MET ASP GLU SER LEU ALA ASN LEU SER GLU ASP GLU TYR
SEQRES 2 A 730 TYR SER GLU GLU GLU ARG ASN ALA LYS ALA GLU LYS GLU
SEQRES 3 A 730 LYS LYS LEU PRO PRO PRO PRO PRO GLN ALA PRO PRO GLU
SEQRES 4 A 730 GLU GLU ASN GLU SER GLU PRO GLU GLU PRO SER GLY VAL
SEQRES 5 A 730 GLU GLY ALA ALA PHE GLN SER ARG LEU PRO HIS ASP ARG
SEQRES 6 A 730 MET THR SER GLN GLU ALA ALA CYS PHE PRO ASP ILE ILE
SEQRES 7 A 730 SER GLY PRO GLN GLN THR GLN LYS VAL PHE LEU PHE ILE
SEQRES 8 A 730 ARG ASN ARG THR LEU GLN LEU TRP LEU ASP ASN PRO LYS
SEQRES 9 A 730 ILE GLN LEU THR PHE GLU ALA THR LEU GLN GLN LEU GLU
SEQRES 10 A 730 ALA PRO TYR ASN SER ASP THR VAL LEU VAL HIS ARG VAL
SEQRES 11 A 730 HIS SER TYR LEU GLU ARG HIS GLY LEU ILE ASN PHE GLY
SEQRES 12 A 730 ILE TYR LYS ARG ILE LYS PRO LEU PRO THR LYS LYS THR
SEQRES 13 A 730 GLY LYS VAL ILE ILE ILE GLY SER GLY VAL SER GLY LEU
SEQRES 14 A 730 ALA ALA ALA ARG GLN LEU GLN SER PHE GLY MET ASP VAL
SEQRES 15 A 730 THR LEU LEU GLU ALA ARG ASP ARG VAL GLY GLY ARG VAL
SEQRES 16 A 730 ALA THR PHE ARG LYS GLY ASN TYR VAL ALA ASP LEU GLY
SEQRES 17 A 730 ALA MET VAL VAL THR GLY LEU GLY GLY ASN PRO MET ALA
SEQRES 18 A 730 VAL VAL SER LYS GLN VAL ASN MET GLU LEU ALA LYS ILE
SEQRES 19 A 730 LYS GLN LYS CYS PRO LEU TYR GLU ALA ASN GLY GLN ALA
SEQRES 20 A 730 VAL PRO LYS GLU LYS ASP GLU MET VAL GLU GLN GLU PHE
SEQRES 21 A 730 ASN ARG LEU LEU GLU ALA THR SER TYR LEU SER HIS GLN
SEQRES 22 A 730 LEU ASP PHE ASN VAL LEU ASN ASN LYS PRO VAL SER LEU
SEQRES 23 A 730 GLY GLN ALA LEU GLU VAL VAL ILE GLN LEU GLN GLU LYS
SEQRES 24 A 730 HIS VAL LYS ASP GLU GLN ILE GLU HIS TRP LYS LYS ILE
SEQRES 25 A 730 VAL LYS THR GLN GLU GLU LEU LYS GLU LEU LEU ASN LYS
SEQRES 26 A 730 MET VAL ASN LEU LYS GLU LYS ILE LYS GLU LEU HIS GLN
SEQRES 27 A 730 GLN TYR LYS GLU ALA SER GLU VAL LYS PRO PRO ARG ASP
SEQRES 28 A 730 ILE THR ALA GLU PHE LEU VAL LYS SER LYS HIS ARG ASP
SEQRES 29 A 730 LEU THR ALA LEU CYS LYS GLU TYR ASP GLU LEU ALA GLU
SEQRES 30 A 730 THR GLN GLY LYS LEU GLU GLU LYS LEU GLN GLU LEU GLU
SEQRES 31 A 730 ALA ASN PRO PRO SER ASP VAL TYR LEU SER SER ARG ASP
SEQRES 32 A 730 ARG GLN ILE LEU ASP TRP HIS PHE ALA ASN LEU GLU PHE
SEQRES 33 A 730 ALA ASN ALA THR PRO LEU SER THR LEU SER LEU LYS HIS
SEQRES 34 A 730 TRP ASP GLN ASP ASP ASP PHE GLU PHE THR GLY SER HIS
SEQRES 35 A 730 LEU THR VAL ARG ASN GLY TYR SER CYS VAL PRO VAL ALA
SEQRES 36 A 730 LEU ALA GLU GLY LEU ASP ILE LYS LEU ASN THR ALA VAL
SEQRES 37 A 730 ARG GLN VAL ARG TYR THR ALA SER GLY CYS GLU VAL ILE
SEQRES 38 A 730 ALA VAL ASN THR ARG SER THR SER GLN THR PHE ILE TYR
SEQRES 39 A 730 LYS CYS ASP ALA VAL LEU CYS THR LEU PRO LEU GLY VAL
SEQRES 40 A 730 LEU LYS GLN GLN PRO PRO ALA VAL GLN PHE VAL PRO PRO
SEQRES 41 A 730 LEU PRO GLU TRP LYS THR SER ALA VAL GLN ARG MET GLY
SEQRES 42 A 730 PHE GLY ASN LEU ASN LYS VAL VAL LEU CYS PHE ASP ARG
SEQRES 43 A 730 VAL PHE TRP ASP PRO SER VAL ASN LEU PHE GLY HIS VAL
SEQRES 44 A 730 GLY SER THR THR ALA SER ARG GLY GLU LEU PHE LEU PHE
SEQRES 45 A 730 TRP ASN LEU TYR LYS ALA PRO ILE LEU LEU ALA LEU VAL
SEQRES 46 A 730 ALA GLY GLU ALA ALA GLY ILE MET GLU ASN ILE SER ASP
SEQRES 47 A 730 ASP VAL ILE VAL GLY ARG CYS LEU ALA ILE LEU LYS GLY
SEQRES 48 A 730 ILE PHE GLY SER SER ALA VAL PRO GLN PRO LYS GLU THR
SEQRES 49 A 730 VAL VAL SER ARG TRP ARG ALA ASP PRO TRP ALA ARG GLY
SEQRES 50 A 730 SER TYR SER TYR VAL ALA ALA GLY SER SER GLY ASN ASP
SEQRES 51 A 730 TYR ASP LEU MET ALA GLN PRO ILE THR PRO GLY PRO SER
SEQRES 52 A 730 ILE PRO GLY ALA PRO GLN PRO ILE PRO ARG LEU PHE PHE
SEQRES 53 A 730 ALA GLY GLU HIS THR ILE ARG ASN TYR PRO ALA THR VAL
SEQRES 54 A 730 HIS GLY ALA LEU LEU SER GLY LEU ARG GLU ALA GLY ARG
SEQRES 55 A 730 ILE ALA ASP GLN PHE LEU GLY ALA MET TYR THR LEU PRO
SEQRES 56 A 730 ARG GLN ALA THR PRO GLY VAL PRO ALA GLN GLN SER PRO
SEQRES 57 A 730 SER MET
SEQRES 1 B 178 ARG ALA LYS ARG LYS PRO PRO LYS GLY MET PHE LEU SER
SEQRES 2 B 178 GLN GLU ASP VAL GLU ALA VAL SER ALA ASN ALA THR ALA
SEQRES 3 B 178 ALA THR THR VAL LEU ARG GLN LEU ASP MET GLU LEU VAL
SEQRES 4 B 178 SER VAL LYS ARG GLN ILE GLN ASN ILE LYS GLN THR ASN
SEQRES 5 B 178 SER ALA LEU LYS GLU LYS LEU ASP GLY GLY ILE GLU PRO
SEQRES 6 B 178 TYR ARG LEU PRO GLU VAL ILE GLN LYS CYS ASN ALA ARG
SEQRES 7 B 178 TRP THR THR GLU GLU GLN LEU LEU ALA VAL GLN ALA ILE
SEQRES 8 B 178 ARG LYS TYR GLY ARG ASP PHE GLN ALA ILE SER ASP VAL
SEQRES 9 B 178 ILE GLY ASN LYS SER VAL VAL GLN VAL LYS ASN PHE PHE
SEQRES 10 B 178 VAL ASN TYR ARG ARG ARG PHE ASN ILE ASP GLU VAL LEU
SEQRES 11 B 178 GLN GLU TRP GLU ALA GLU HIS GLY LYS GLU GLU THR ASN
SEQRES 12 B 178 GLY PRO SER ASN GLN LYS PRO VAL LYS SER PRO ASP ASN
SEQRES 13 B 178 SER ILE LYS MET PRO GLU GLU GLU ASP GLU ALA PRO VAL
SEQRES 14 B 178 LEU ASP VAL ARG TYR ALA SER ALA SER
SEQRES 1 C 20 PRO ARG SER PHE LEU VAL ARG LYS PRO SER ASP PRO ASN
SEQRES 2 C 20 ARG LYS PRO ASN TYR SER GLU
HET FAD A 900 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 4 FAD C27 H33 N9 O15 P2
HELIX 1 1 GLY A 173 SER A 181 1 9
HELIX 2 2 THR A 189 PHE A 196 1 8
HELIX 3 3 PHE A 196 SER A 201 1 6
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 PRO A 241 SER A 244 5 4
HELIX 7 7 ASP A 245 HIS A 259 1 15
HELIX 8 8 GLY A 287 PHE A 300 1 14
HELIX 9 9 ASN A 340 VAL A 349 1 10
HELIX 10 10 PRO A 371 GLN A 395 1 25
HELIX 11 11 SER A 407 VAL A 468 1 62
HELIX 12 12 ASP A 473 GLU A 512 1 40
HELIX 13 13 SER A 522 ASN A 540 1 19
HELIX 14 14 ASP A 555 GLU A 559 5 5
HELIX 15 15 SER A 572 GLU A 580 1 9
HELIX 16 16 PRO A 626 LYS A 631 1 6
HELIX 17 17 PRO A 644 MET A 654 1 11
HELIX 18 18 THR A 684 ARG A 688 5 5
HELIX 19 19 ALA A 708 MET A 715 1 8
HELIX 20 20 GLU A 716 ILE A 718 5 3
HELIX 21 21 SER A 719 GLY A 736 1 18
HELIX 22 22 SER A 769 GLN A 778 1 10
HELIX 23 23 GLY A 800 ILE A 804 5 5
HELIX 24 24 THR A 810 LEU A 830 1 21
HELIX 25 25 ALA A 832 LEU A 836 5 5
HELIX 26 26 SER B 317 VAL B 324 1 8
HELIX 27 27 THR B 329 LEU B 363 1 35
HELIX 28 28 ILE B 367 ARG B 371 5 5
HELIX 29 29 THR B 384 GLY B 399 1 16
HELIX 30 30 ASP B 401 GLY B 410 1 10
HELIX 31 31 SER B 413 TYR B 424 1 12
HELIX 32 32 ASN B 429 ALA B 439 1 11
HELIX 33 33 PRO C 1 LEU C 5 5 5
SHEET 1 AA 5 ILE A 584 LYS A 585 0
SHEET 2 AA 5 ASP A 303 LEU A 307 1 O LEU A 306 N LYS A 585
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 THR A 319 LYS A 322 0
SHEET 2 AB 2 TYR A 325 ASP A 328 -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 2 GLY A 655 PHE A 656 0
SHEET 2 AF 2 SER A 762 TYR A 763 -1 O TYR A 763 N GLY A 655
SHEET 1 AG 5 LEU A 677 GLY A 679 0
SHEET 2 AG 5 GLU A 690 TRP A 695 -1 O PHE A 694 N PHE A 678
SHEET 3 AG 5 ILE A 702 VAL A 707 -1 O LEU A 704 N TRP A 695
SHEET 4 AG 5 ASN A 660 CYS A 665 -1 O ASN A 660 N VAL A 707
SHEET 5 AG 5 GLU A 745 VAL A 748 -1 O GLU A 745 N CYS A 665
CISPEP 1 ALA A 240 PRO A 241 0 -1.14
CISPEP 2 PRO A 470 PRO A 471 0 0.13
CISPEP 3 GLN A 633 PRO A 634 0 6.84
CISPEP 4 VAL A 640 PRO A 641 0 -1.72
SITE 1 AC1 32 GLY A 285 GLY A 287 VAL A 288 SER A 289
SITE 2 AC1 32 LEU A 307 GLU A 308 ALA A 309 ARG A 310
SITE 3 AC1 32 GLY A 314 GLY A 315 ARG A 316 LEU A 329
SITE 4 AC1 32 GLY A 330 ALA A 331 MET A 332 VAL A 333
SITE 5 AC1 32 THR A 588 ALA A 589 VAL A 590 THR A 624
SITE 6 AC1 32 LEU A 625 PRO A 626 TRP A 756 SER A 760
SITE 7 AC1 32 TYR A 761 GLY A 800 GLU A 801 ALA A 809
SITE 8 AC1 32 THR A 810 VAL A 811 ALA A 814 PHE C 4
CRYST1 119.170 181.460 234.440 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 0.008391 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004265 0.00000
(ATOM LINES ARE NOT SHOWN.)
END