HEADER TRANSFERASE 23-SEP-15 5DX0
TITLE CRYSTAL STRUCTURE OF CARM1, SINEFUNGIN, AND H3 PEPTIDE (R17)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-ARGININE METHYLTRANSFERASE CARM1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 134-479);
COMPND 5 SYNONYM: COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1,PROTEIN
COMPND 6 ARGININE N-METHYLTRANSFERASE 4;
COMPND 7 EC: 2.1.1.-,2.1.1.125;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: H3 PEPTIDE;
COMPND 11 CHAIN: F, G, H, I;
COMPND 12 FRAGMENT: UNP RESIDUES 14-31;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CARM1, PRMT4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606
KEYWDS PROTEIN-SUBSTRATE TERNARY COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.A.BORIACK-SJODIN
REVDAT 2 30-MAR-16 5DX0 1 JRNL
REVDAT 1 25-NOV-15 5DX0 0
JRNL AUTH P.A.BORIACK-SJODIN,L.JIN,S.L.JACQUES,A.DREW,C.SNEERINGER,
JRNL AUTH 2 M.P.SCOTT,M.P.MOYER,S.RIBICH,O.MORADEI,R.A.COPELAND
JRNL TITL STRUCTURAL INSIGHTS INTO TERNARY COMPLEX FORMATION OF HUMAN
JRNL TITL 2 CARM1 WITH VARIOUS SUBSTRATES.
JRNL REF ACS CHEM.BIOL. V. 11 763 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 26551522
JRNL DOI 10.1021/ACSCHEMBIO.5B00773
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 84566
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4324
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5995
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 301
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11274
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 140
REMARK 3 SOLVENT ATOMS : 458
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.39000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -2.39000
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): 0.259
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.213
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.625
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11720 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11015 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15879 ; 1.376 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25313 ; 0.764 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1406 ; 6.312 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 547 ;36.086 ;24.004
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1958 ;13.845 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;16.635 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1744 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13186 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2866 ; 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): 5644 ; 1.829 ; 3.321
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5643 ; 1.828 ; 3.321
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7034 ; 2.734 ; 4.969
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5DX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88915
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.64400
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M TRIS PH
REMARK 280 8.5, 18% W/V PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 37.86100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.42350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.86100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.42350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F, G
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, I
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 SER A 131
REMARK 465 ILE A 132
REMARK 465 ALA A 133
REMARK 465 ARG A 134
REMARK 465 GLY A 478
REMARK 465 THR A 479
REMARK 465 SER B 131
REMARK 465 ILE B 132
REMARK 465 ALA B 133
REMARK 465 ARG B 134
REMARK 465 GLY B 478
REMARK 465 THR B 479
REMARK 465 SER C 131
REMARK 465 ILE C 132
REMARK 465 ALA C 133
REMARK 465 ARG C 134
REMARK 465 GLY C 478
REMARK 465 THR C 479
REMARK 465 SER D 131
REMARK 465 ILE D 132
REMARK 465 ALA D 133
REMARK 465 ARG D 134
REMARK 465 GLY D 478
REMARK 465 THR D 479
REMARK 465 ALA F 9
REMARK 465 THR F 10
REMARK 465 LYS F 11
REMARK 465 ALA F 12
REMARK 465 ALA F 13
REMARK 465 ARG F 14
REMARK 465 LYS F 15
REMARK 465 SER F 16
REMARK 465 ALA F 17
REMARK 465 PRO F 18
REMARK 465 NH2 F 19
REMARK 465 THR G 10
REMARK 465 LYS G 11
REMARK 465 ALA G 12
REMARK 465 ALA G 13
REMARK 465 ARG G 14
REMARK 465 LYS G 15
REMARK 465 SER G 16
REMARK 465 ALA G 17
REMARK 465 PRO G 18
REMARK 465 NH2 G 19
REMARK 465 ALA H 9
REMARK 465 THR H 10
REMARK 465 LYS H 11
REMARK 465 ALA H 12
REMARK 465 ALA H 13
REMARK 465 ARG H 14
REMARK 465 LYS H 15
REMARK 465 SER H 16
REMARK 465 ALA H 17
REMARK 465 PRO H 18
REMARK 465 NH2 H 19
REMARK 465 THR I 10
REMARK 465 LYS I 11
REMARK 465 ALA I 12
REMARK 465 ALA I 13
REMARK 465 ARG I 14
REMARK 465 LYS I 15
REMARK 465 SER I 16
REMARK 465 ALA I 17
REMARK 465 PRO I 18
REMARK 465 NH2 I 19
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 OD1 ASP B 468 O HOH B 601 1.82
REMARK 500 O HOH B 652 O HOH B 696 2.04
REMARK 500 OH TYR D 272 O PRO D 287 2.09
REMARK 500 OE1 GLU A 364 O HOH A 601 2.14
REMARK 500 O TYR D 476 O HOH D 601 2.16
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 ASN A 179 56.43 -102.92
REMARK 500 LYS A 184 109.72 -52.40
REMARK 500 LEU A 263 -54.01 75.97
REMARK 500 GLU A 266 -18.88 94.28
REMARK 500 ARG A 267 17.59 59.45
REMARK 500 ASP A 299 90.75 -160.23
REMARK 500 SER A 317 52.44 -155.29
REMARK 500 ASP A 341 -173.23 -176.93
REMARK 500 ALA A 350 146.03 -172.34
REMARK 500 TYR A 416 -138.18 45.03
REMARK 500 ASN A 471 63.92 -119.10
REMARK 500 ASN B 179 52.46 -109.34
REMARK 500 LEU B 263 -53.38 68.39
REMARK 500 GLU B 266 -23.30 91.39
REMARK 500 ASP B 299 84.33 -151.88
REMARK 500 TYR B 416 -135.24 47.19
REMARK 500 ASP B 432 175.45 -57.31
REMARK 500 SER B 447 -158.86 -152.82
REMARK 500 ASP C 165 98.91 -64.55
REMARK 500 ASN C 179 45.59 -106.00
REMARK 500 LEU C 263 -45.51 67.27
REMARK 500 GLU C 266 -20.90 88.45
REMARK 500 ASP C 299 90.93 -164.81
REMARK 500 SER C 317 54.63 -147.33
REMARK 500 ASP C 341 -167.17 -173.63
REMARK 500 TYR C 416 -137.69 49.12
REMARK 500 ARG C 445 30.06 -98.00
REMARK 500 ASP D 165 93.69 -69.88
REMARK 500 ASN D 179 50.09 -113.80
REMARK 500 ASP D 185 18.67 57.45
REMARK 500 LEU D 263 -52.07 61.43
REMARK 500 GLU D 266 -24.32 88.71
REMARK 500 SER D 282 -0.21 62.86
REMARK 500 ASP D 299 80.50 -164.68
REMARK 500 ASP D 341 -168.44 -160.52
REMARK 500 TYR D 416 -139.79 53.52
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 SFG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SFG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SFG C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SFG D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DWQ RELATED DB: PDB
REMARK 900 5DWQ CONTAINS THE SAME PROTEIN WITH A METHYLATED H3 PEPTIDE
REMARK 900 RELATED ID: 5DX1 RELATED DB: PDB
REMARK 900 RELATED ID: 5DX8 RELATED DB: PDB
REMARK 900 RELATED ID: 5DXA RELATED DB: PDB
REMARK 900 RELATED ID: 5DXJ RELATED DB: PDB
DBREF 5DX0 A 134 479 UNP Q86X55 CARM1_HUMAN 134 479
DBREF 5DX0 B 134 479 UNP Q86X55 CARM1_HUMAN 134 479
DBREF 5DX0 C 134 479 UNP Q86X55 CARM1_HUMAN 134 479
DBREF 5DX0 D 134 479 UNP Q86X55 CARM1_HUMAN 134 479
DBREF 5DX0 F 1 18 UNP P84243 H33_HUMAN 14 31
DBREF 5DX0 G 1 18 UNP P84243 H33_HUMAN 14 31
DBREF 5DX0 H 1 18 UNP P84243 H33_HUMAN 14 31
DBREF 5DX0 I 1 18 UNP P84243 H33_HUMAN 14 31
SEQADV 5DX0 SER A 131 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ILE A 132 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ALA A 133 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 SER B 131 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ILE B 132 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ALA B 133 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 SER C 131 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ILE C 132 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ALA C 133 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 SER D 131 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ILE D 132 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ALA D 133 UNP Q86X55 EXPRESSION TAG
SEQADV 5DX0 ACE F 0 UNP P84243 ACETYLATION
SEQADV 5DX0 NH2 F 19 UNP P84243 AMIDATION
SEQADV 5DX0 ACE G 0 UNP P84243 ACETYLATION
SEQADV 5DX0 NH2 G 19 UNP P84243 AMIDATION
SEQADV 5DX0 ACE H 0 UNP P84243 ACETYLATION
SEQADV 5DX0 NH2 H 19 UNP P84243 AMIDATION
SEQADV 5DX0 ACE I 0 UNP P84243 ACETYLATION
SEQADV 5DX0 NH2 I 19 UNP P84243 AMIDATION
SEQRES 1 A 349 SER ILE ALA ARG SER VAL PHE SER GLU ARG THR GLU GLU
SEQRES 2 A 349 SER SER ALA VAL GLN TYR PHE GLN PHE TYR GLY TYR LEU
SEQRES 3 A 349 SER GLN GLN GLN ASN MET MET GLN ASP TYR VAL ARG THR
SEQRES 4 A 349 GLY THR TYR GLN ARG ALA ILE LEU GLN ASN HIS THR ASP
SEQRES 5 A 349 PHE LYS ASP LYS ILE VAL LEU ASP VAL GLY CYS GLY SER
SEQRES 6 A 349 GLY ILE LEU SER PHE PHE ALA ALA GLN ALA GLY ALA ARG
SEQRES 7 A 349 LYS ILE TYR ALA VAL GLU ALA SER THR MET ALA GLN HIS
SEQRES 8 A 349 ALA GLU VAL LEU VAL LYS SER ASN ASN LEU THR ASP ARG
SEQRES 9 A 349 ILE VAL VAL ILE PRO GLY LYS VAL GLU GLU VAL SER LEU
SEQRES 10 A 349 PRO GLU GLN VAL ASP ILE ILE ILE SER GLU PRO MET GLY
SEQRES 11 A 349 TYR MET LEU PHE ASN GLU ARG MET LEU GLU SER TYR LEU
SEQRES 12 A 349 HIS ALA LYS LYS TYR LEU LYS PRO SER GLY ASN MET PHE
SEQRES 13 A 349 PRO THR ILE GLY ASP VAL HIS LEU ALA PRO PHE THR ASP
SEQRES 14 A 349 GLU GLN LEU TYR MET GLU GLN PHE THR LYS ALA ASN PHE
SEQRES 15 A 349 TRP TYR GLN PRO SER PHE HIS GLY VAL ASP LEU SER ALA
SEQRES 16 A 349 LEU ARG GLY ALA ALA VAL ASP GLU TYR PHE ARG GLN PRO
SEQRES 17 A 349 VAL VAL ASP THR PHE ASP ILE ARG ILE LEU MET ALA LYS
SEQRES 18 A 349 SER VAL LYS TYR THR VAL ASN PHE LEU GLU ALA LYS GLU
SEQRES 19 A 349 GLY ASP LEU HIS ARG ILE GLU ILE PRO PHE LYS PHE HIS
SEQRES 20 A 349 MET LEU HIS SER GLY LEU VAL HIS GLY LEU ALA PHE TRP
SEQRES 21 A 349 PHE ASP VAL ALA PHE ILE GLY SER ILE MET THR VAL TRP
SEQRES 22 A 349 LEU SER THR ALA PRO THR GLU PRO LEU THR HIS TRP TYR
SEQRES 23 A 349 GLN VAL ARG CYS LEU PHE GLN SER PRO LEU PHE ALA LYS
SEQRES 24 A 349 ALA GLY ASP THR LEU SER GLY THR CYS LEU LEU ILE ALA
SEQRES 25 A 349 ASN LYS ARG GLN SER TYR ASP ILE SER ILE VAL ALA GLN
SEQRES 26 A 349 VAL ASP GLN THR GLY SER LYS SER SER ASN LEU LEU ASP
SEQRES 27 A 349 LEU LYS ASN PRO PHE PHE ARG TYR THR GLY THR
SEQRES 1 B 349 SER ILE ALA ARG SER VAL PHE SER GLU ARG THR GLU GLU
SEQRES 2 B 349 SER SER ALA VAL GLN TYR PHE GLN PHE TYR GLY TYR LEU
SEQRES 3 B 349 SER GLN GLN GLN ASN MET MET GLN ASP TYR VAL ARG THR
SEQRES 4 B 349 GLY THR TYR GLN ARG ALA ILE LEU GLN ASN HIS THR ASP
SEQRES 5 B 349 PHE LYS ASP LYS ILE VAL LEU ASP VAL GLY CYS GLY SER
SEQRES 6 B 349 GLY ILE LEU SER PHE PHE ALA ALA GLN ALA GLY ALA ARG
SEQRES 7 B 349 LYS ILE TYR ALA VAL GLU ALA SER THR MET ALA GLN HIS
SEQRES 8 B 349 ALA GLU VAL LEU VAL LYS SER ASN ASN LEU THR ASP ARG
SEQRES 9 B 349 ILE VAL VAL ILE PRO GLY LYS VAL GLU GLU VAL SER LEU
SEQRES 10 B 349 PRO GLU GLN VAL ASP ILE ILE ILE SER GLU PRO MET GLY
SEQRES 11 B 349 TYR MET LEU PHE ASN GLU ARG MET LEU GLU SER TYR LEU
SEQRES 12 B 349 HIS ALA LYS LYS TYR LEU LYS PRO SER GLY ASN MET PHE
SEQRES 13 B 349 PRO THR ILE GLY ASP VAL HIS LEU ALA PRO PHE THR ASP
SEQRES 14 B 349 GLU GLN LEU TYR MET GLU GLN PHE THR LYS ALA ASN PHE
SEQRES 15 B 349 TRP TYR GLN PRO SER PHE HIS GLY VAL ASP LEU SER ALA
SEQRES 16 B 349 LEU ARG GLY ALA ALA VAL ASP GLU TYR PHE ARG GLN PRO
SEQRES 17 B 349 VAL VAL ASP THR PHE ASP ILE ARG ILE LEU MET ALA LYS
SEQRES 18 B 349 SER VAL LYS TYR THR VAL ASN PHE LEU GLU ALA LYS GLU
SEQRES 19 B 349 GLY ASP LEU HIS ARG ILE GLU ILE PRO PHE LYS PHE HIS
SEQRES 20 B 349 MET LEU HIS SER GLY LEU VAL HIS GLY LEU ALA PHE TRP
SEQRES 21 B 349 PHE ASP VAL ALA PHE ILE GLY SER ILE MET THR VAL TRP
SEQRES 22 B 349 LEU SER THR ALA PRO THR GLU PRO LEU THR HIS TRP TYR
SEQRES 23 B 349 GLN VAL ARG CYS LEU PHE GLN SER PRO LEU PHE ALA LYS
SEQRES 24 B 349 ALA GLY ASP THR LEU SER GLY THR CYS LEU LEU ILE ALA
SEQRES 25 B 349 ASN LYS ARG GLN SER TYR ASP ILE SER ILE VAL ALA GLN
SEQRES 26 B 349 VAL ASP GLN THR GLY SER LYS SER SER ASN LEU LEU ASP
SEQRES 27 B 349 LEU LYS ASN PRO PHE PHE ARG TYR THR GLY THR
SEQRES 1 C 349 SER ILE ALA ARG SER VAL PHE SER GLU ARG THR GLU GLU
SEQRES 2 C 349 SER SER ALA VAL GLN TYR PHE GLN PHE TYR GLY TYR LEU
SEQRES 3 C 349 SER GLN GLN GLN ASN MET MET GLN ASP TYR VAL ARG THR
SEQRES 4 C 349 GLY THR TYR GLN ARG ALA ILE LEU GLN ASN HIS THR ASP
SEQRES 5 C 349 PHE LYS ASP LYS ILE VAL LEU ASP VAL GLY CYS GLY SER
SEQRES 6 C 349 GLY ILE LEU SER PHE PHE ALA ALA GLN ALA GLY ALA ARG
SEQRES 7 C 349 LYS ILE TYR ALA VAL GLU ALA SER THR MET ALA GLN HIS
SEQRES 8 C 349 ALA GLU VAL LEU VAL LYS SER ASN ASN LEU THR ASP ARG
SEQRES 9 C 349 ILE VAL VAL ILE PRO GLY LYS VAL GLU GLU VAL SER LEU
SEQRES 10 C 349 PRO GLU GLN VAL ASP ILE ILE ILE SER GLU PRO MET GLY
SEQRES 11 C 349 TYR MET LEU PHE ASN GLU ARG MET LEU GLU SER TYR LEU
SEQRES 12 C 349 HIS ALA LYS LYS TYR LEU LYS PRO SER GLY ASN MET PHE
SEQRES 13 C 349 PRO THR ILE GLY ASP VAL HIS LEU ALA PRO PHE THR ASP
SEQRES 14 C 349 GLU GLN LEU TYR MET GLU GLN PHE THR LYS ALA ASN PHE
SEQRES 15 C 349 TRP TYR GLN PRO SER PHE HIS GLY VAL ASP LEU SER ALA
SEQRES 16 C 349 LEU ARG GLY ALA ALA VAL ASP GLU TYR PHE ARG GLN PRO
SEQRES 17 C 349 VAL VAL ASP THR PHE ASP ILE ARG ILE LEU MET ALA LYS
SEQRES 18 C 349 SER VAL LYS TYR THR VAL ASN PHE LEU GLU ALA LYS GLU
SEQRES 19 C 349 GLY ASP LEU HIS ARG ILE GLU ILE PRO PHE LYS PHE HIS
SEQRES 20 C 349 MET LEU HIS SER GLY LEU VAL HIS GLY LEU ALA PHE TRP
SEQRES 21 C 349 PHE ASP VAL ALA PHE ILE GLY SER ILE MET THR VAL TRP
SEQRES 22 C 349 LEU SER THR ALA PRO THR GLU PRO LEU THR HIS TRP TYR
SEQRES 23 C 349 GLN VAL ARG CYS LEU PHE GLN SER PRO LEU PHE ALA LYS
SEQRES 24 C 349 ALA GLY ASP THR LEU SER GLY THR CYS LEU LEU ILE ALA
SEQRES 25 C 349 ASN LYS ARG GLN SER TYR ASP ILE SER ILE VAL ALA GLN
SEQRES 26 C 349 VAL ASP GLN THR GLY SER LYS SER SER ASN LEU LEU ASP
SEQRES 27 C 349 LEU LYS ASN PRO PHE PHE ARG TYR THR GLY THR
SEQRES 1 D 349 SER ILE ALA ARG SER VAL PHE SER GLU ARG THR GLU GLU
SEQRES 2 D 349 SER SER ALA VAL GLN TYR PHE GLN PHE TYR GLY TYR LEU
SEQRES 3 D 349 SER GLN GLN GLN ASN MET MET GLN ASP TYR VAL ARG THR
SEQRES 4 D 349 GLY THR TYR GLN ARG ALA ILE LEU GLN ASN HIS THR ASP
SEQRES 5 D 349 PHE LYS ASP LYS ILE VAL LEU ASP VAL GLY CYS GLY SER
SEQRES 6 D 349 GLY ILE LEU SER PHE PHE ALA ALA GLN ALA GLY ALA ARG
SEQRES 7 D 349 LYS ILE TYR ALA VAL GLU ALA SER THR MET ALA GLN HIS
SEQRES 8 D 349 ALA GLU VAL LEU VAL LYS SER ASN ASN LEU THR ASP ARG
SEQRES 9 D 349 ILE VAL VAL ILE PRO GLY LYS VAL GLU GLU VAL SER LEU
SEQRES 10 D 349 PRO GLU GLN VAL ASP ILE ILE ILE SER GLU PRO MET GLY
SEQRES 11 D 349 TYR MET LEU PHE ASN GLU ARG MET LEU GLU SER TYR LEU
SEQRES 12 D 349 HIS ALA LYS LYS TYR LEU LYS PRO SER GLY ASN MET PHE
SEQRES 13 D 349 PRO THR ILE GLY ASP VAL HIS LEU ALA PRO PHE THR ASP
SEQRES 14 D 349 GLU GLN LEU TYR MET GLU GLN PHE THR LYS ALA ASN PHE
SEQRES 15 D 349 TRP TYR GLN PRO SER PHE HIS GLY VAL ASP LEU SER ALA
SEQRES 16 D 349 LEU ARG GLY ALA ALA VAL ASP GLU TYR PHE ARG GLN PRO
SEQRES 17 D 349 VAL VAL ASP THR PHE ASP ILE ARG ILE LEU MET ALA LYS
SEQRES 18 D 349 SER VAL LYS TYR THR VAL ASN PHE LEU GLU ALA LYS GLU
SEQRES 19 D 349 GLY ASP LEU HIS ARG ILE GLU ILE PRO PHE LYS PHE HIS
SEQRES 20 D 349 MET LEU HIS SER GLY LEU VAL HIS GLY LEU ALA PHE TRP
SEQRES 21 D 349 PHE ASP VAL ALA PHE ILE GLY SER ILE MET THR VAL TRP
SEQRES 22 D 349 LEU SER THR ALA PRO THR GLU PRO LEU THR HIS TRP TYR
SEQRES 23 D 349 GLN VAL ARG CYS LEU PHE GLN SER PRO LEU PHE ALA LYS
SEQRES 24 D 349 ALA GLY ASP THR LEU SER GLY THR CYS LEU LEU ILE ALA
SEQRES 25 D 349 ASN LYS ARG GLN SER TYR ASP ILE SER ILE VAL ALA GLN
SEQRES 26 D 349 VAL ASP GLN THR GLY SER LYS SER SER ASN LEU LEU ASP
SEQRES 27 D 349 LEU LYS ASN PRO PHE PHE ARG TYR THR GLY THR
SEQRES 1 F 20 ACE GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA
SEQRES 2 F 20 ALA ARG LYS SER ALA PRO NH2
SEQRES 1 G 20 ACE GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA
SEQRES 2 G 20 ALA ARG LYS SER ALA PRO NH2
SEQRES 1 H 20 ACE GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA
SEQRES 2 H 20 ALA ARG LYS SER ALA PRO NH2
SEQRES 1 I 20 ACE GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA
SEQRES 2 I 20 ALA ARG LYS SER ALA PRO NH2
HET ACE F 0 3
HET ACE G 0 3
HET ACE H 0 3
HET ACE I 0 3
HET SFG A 501 27
HET GOL A 502 6
HET SO4 A 503 5
HET SFG B 501 27
HET SO4 B 502 5
HET SFG C 501 27
HET GOL C 502 6
HET SO4 C 503 5
HET SFG D 501 27
HET SO4 D 502 5
HETNAM ACE ACETYL GROUP
HETNAM SFG SINEFUNGIN
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN SFG ADENOSYL-ORNITHINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ACE 4(C2 H4 O)
FORMUL 9 SFG 4(C15 H23 N7 O5)
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 11 SO4 4(O4 S 2-)
FORMUL 19 HOH *458(H2 O)
HELIX 1 AA1 SER A 135 THR A 141 1 7
HELIX 2 AA2 GLU A 142 GLY A 154 1 13
HELIX 3 AA3 TYR A 155 GLN A 164 1 10
HELIX 4 AA4 ASP A 165 ASN A 179 1 15
HELIX 5 AA5 HIS A 180 PHE A 183 5 4
HELIX 6 AA6 GLY A 196 ALA A 205 1 10
HELIX 7 AA7 THR A 217 ASN A 229 1 13
HELIX 8 AA8 ARG A 267 ALA A 275 1 9
HELIX 9 AA9 ASP A 299 ASN A 311 1 13
HELIX 10 AB1 PHE A 312 GLN A 315 5 4
HELIX 11 AB2 SER A 317 VAL A 321 5 5
HELIX 12 AB3 LEU A 323 ALA A 325 5 3
HELIX 13 AB4 LEU A 326 GLN A 337 1 12
HELIX 14 AB5 ASP A 344 LEU A 348 5 5
HELIX 15 AB6 LYS A 363 LEU A 367 5 5
HELIX 16 AB7 VAL B 136 ARG B 140 1 5
HELIX 17 AB8 GLU B 142 GLY B 154 1 13
HELIX 18 AB9 TYR B 155 GLN B 164 1 10
HELIX 19 AC1 ASP B 165 ASN B 179 1 15
HELIX 20 AC2 HIS B 180 PHE B 183 5 4
HELIX 21 AC3 GLY B 196 ALA B 205 1 10
HELIX 22 AC4 THR B 217 ASN B 229 1 13
HELIX 23 AC5 MET B 268 ALA B 275 1 8
HELIX 24 AC6 ASP B 299 ASN B 311 1 13
HELIX 25 AC7 PHE B 312 TYR B 314 5 3
HELIX 26 AC8 LEU B 323 ALA B 325 5 3
HELIX 27 AC9 LEU B 326 ARG B 336 1 11
HELIX 28 AD1 ASP B 344 LEU B 348 5 5
HELIX 29 AD2 LYS B 363 LEU B 367 5 5
HELIX 30 AD3 VAL C 136 THR C 141 1 6
HELIX 31 AD4 GLU C 142 TYR C 153 1 12
HELIX 32 AD5 TYR C 155 ASP C 165 1 11
HELIX 33 AD6 ASP C 165 ASN C 179 1 15
HELIX 34 AD7 HIS C 180 PHE C 183 5 4
HELIX 35 AD8 GLY C 196 ALA C 205 1 10
HELIX 36 AD9 THR C 217 ASN C 229 1 13
HELIX 37 AE1 ARG C 267 ALA C 275 1 9
HELIX 38 AE2 ASP C 299 ASN C 311 1 13
HELIX 39 AE3 PHE C 312 GLN C 315 5 4
HELIX 40 AE4 SER C 317 VAL C 321 5 5
HELIX 41 AE5 LEU C 323 ALA C 325 5 3
HELIX 42 AE6 LEU C 326 ARG C 336 1 11
HELIX 43 AE7 ASP C 344 LEU C 348 5 5
HELIX 44 AE8 LYS C 363 LEU C 367 5 5
HELIX 45 AE9 VAL D 136 THR D 141 1 6
HELIX 46 AF1 GLU D 142 GLY D 154 1 13
HELIX 47 AF2 TYR D 155 GLN D 164 1 10
HELIX 48 AF3 ASP D 165 ASN D 179 1 15
HELIX 49 AF4 HIS D 180 PHE D 183 5 4
HELIX 50 AF5 GLY D 196 GLY D 206 1 11
HELIX 51 AF6 THR D 217 ASN D 229 1 13
HELIX 52 AF7 ARG D 267 ALA D 275 1 9
HELIX 53 AF8 ASP D 299 ASN D 311 1 13
HELIX 54 AF9 PHE D 312 TYR D 314 5 3
HELIX 55 AG1 LEU D 323 ALA D 325 5 3
HELIX 56 AG2 LEU D 326 ARG D 336 1 11
HELIX 57 AG3 ASP D 344 LEU D 348 5 5
HELIX 58 AG4 LYS D 363 LEU D 367 5 5
SHEET 1 AA1 5 ILE A 235 PRO A 239 0
SHEET 2 AA1 5 LYS A 209 GLU A 214 1 N ILE A 210 O VAL A 236
SHEET 3 AA1 5 ILE A 187 VAL A 191 1 N VAL A 188 O TYR A 211
SHEET 4 AA1 5 VAL A 251 SER A 256 1 O ILE A 255 N LEU A 189
SHEET 5 AA1 5 LEU A 279 PHE A 286 1 O LYS A 280 N VAL A 251
SHEET 1 AA2 4 VAL A 353 ASN A 358 0
SHEET 2 AA2 4 ILE A 289 PHE A 297 -1 N VAL A 292 O TYR A 355
SHEET 3 AA2 4 GLY A 382 ILE A 396 -1 O ALA A 388 N ALA A 295
SHEET 4 AA2 4 THR A 401 SER A 405 -1 O VAL A 402 N PHE A 395
SHEET 1 AA3 6 VAL A 353 ASN A 358 0
SHEET 2 AA3 6 ILE A 289 PHE A 297 -1 N VAL A 292 O TYR A 355
SHEET 3 AA3 6 GLY A 382 ILE A 396 -1 O ALA A 388 N ALA A 295
SHEET 4 AA3 6 GLN A 417 ALA A 428 -1 O LEU A 426 N VAL A 384
SHEET 5 AA3 6 VAL A 339 ASP A 341 -1 N VAL A 339 O ARG A 419
SHEET 6 AA3 6 PHE A 473 PHE A 474 1 O PHE A 473 N VAL A 340
SHEET 1 AA4 4 ARG A 369 HIS A 377 0
SHEET 2 AA4 4 THR A 433 ALA A 442 -1 O LEU A 434 N PHE A 376
SHEET 3 AA4 4 TYR A 448 VAL A 456 -1 O SER A 451 N LEU A 439
SHEET 4 AA4 4 LYS A 462 ASP A 468 -1 O LEU A 467 N ILE A 450
SHEET 1 AA5 5 ILE B 235 PRO B 239 0
SHEET 2 AA5 5 LYS B 209 GLU B 214 1 N ALA B 212 O ILE B 238
SHEET 3 AA5 5 ILE B 187 VAL B 191 1 N ASP B 190 O TYR B 211
SHEET 4 AA5 5 VAL B 251 SER B 256 1 O ILE B 255 N LEU B 189
SHEET 5 AA5 5 LEU B 279 PHE B 286 1 O PHE B 286 N ILE B 254
SHEET 1 AA6 4 VAL B 353 ASN B 358 0
SHEET 2 AA6 4 ILE B 289 PHE B 297 -1 N VAL B 292 O TYR B 355
SHEET 3 AA6 4 GLY B 382 ILE B 396 -1 O ALA B 388 N ALA B 295
SHEET 4 AA6 4 THR B 401 SER B 405 -1 O VAL B 402 N PHE B 395
SHEET 1 AA7 6 VAL B 353 ASN B 358 0
SHEET 2 AA7 6 ILE B 289 PHE B 297 -1 N VAL B 292 O TYR B 355
SHEET 3 AA7 6 GLY B 382 ILE B 396 -1 O ALA B 388 N ALA B 295
SHEET 4 AA7 6 GLN B 417 ALA B 428 -1 O LEU B 426 N VAL B 384
SHEET 5 AA7 6 VAL B 339 ASP B 341 -1 N VAL B 339 O ARG B 419
SHEET 6 AA7 6 PHE B 473 PHE B 474 1 O PHE B 473 N VAL B 340
SHEET 1 AA8 4 ARG B 369 HIS B 377 0
SHEET 2 AA8 4 THR B 433 ASN B 443 -1 O CYS B 438 N ILE B 372
SHEET 3 AA8 4 SER B 447 VAL B 456 -1 O SER B 451 N LEU B 439
SHEET 4 AA8 4 SER B 461 ASP B 468 -1 O SER B 463 N ALA B 454
SHEET 1 AA9 5 ILE C 235 PRO C 239 0
SHEET 2 AA9 5 LYS C 209 GLU C 214 1 N ILE C 210 O VAL C 236
SHEET 3 AA9 5 ILE C 187 VAL C 191 1 N ASP C 190 O TYR C 211
SHEET 4 AA9 5 VAL C 251 SER C 256 1 O ILE C 255 N LEU C 189
SHEET 5 AA9 5 LEU C 279 PHE C 286 1 O LYS C 280 N VAL C 251
SHEET 1 AB1 4 VAL C 353 ASN C 358 0
SHEET 2 AB1 4 ILE C 289 PHE C 297 -1 N GLY C 290 O VAL C 357
SHEET 3 AB1 4 GLY C 382 ILE C 396 -1 O ALA C 388 N ALA C 295
SHEET 4 AB1 4 THR C 401 SER C 405 -1 O LEU C 404 N VAL C 393
SHEET 1 AB2 6 VAL C 353 ASN C 358 0
SHEET 2 AB2 6 ILE C 289 PHE C 297 -1 N GLY C 290 O VAL C 357
SHEET 3 AB2 6 GLY C 382 ILE C 396 -1 O ALA C 388 N ALA C 295
SHEET 4 AB2 6 GLN C 417 ALA C 428 -1 O LEU C 426 N VAL C 384
SHEET 5 AB2 6 VAL C 339 ASP C 341 -1 N VAL C 339 O ARG C 419
SHEET 6 AB2 6 PHE C 473 PHE C 474 1 O PHE C 473 N VAL C 340
SHEET 1 AB3 4 ARG C 369 HIS C 377 0
SHEET 2 AB3 4 THR C 433 ALA C 442 -1 O LEU C 434 N PHE C 376
SHEET 3 AB3 4 TYR C 448 VAL C 456 -1 O ASP C 449 N ILE C 441
SHEET 4 AB3 4 LYS C 462 ASP C 468 -1 O LEU C 467 N ILE C 450
SHEET 1 AB4 5 ILE D 235 PRO D 239 0
SHEET 2 AB4 5 LYS D 209 GLU D 214 1 N ALA D 212 O VAL D 236
SHEET 3 AB4 5 ILE D 187 VAL D 191 1 N ASP D 190 O TYR D 211
SHEET 4 AB4 5 VAL D 251 SER D 256 1 O ILE D 255 N LEU D 189
SHEET 5 AB4 5 LEU D 279 PHE D 286 1 O PHE D 286 N ILE D 254
SHEET 1 AB5 4 VAL D 353 ASN D 358 0
SHEET 2 AB5 4 ILE D 289 PHE D 297 -1 N VAL D 292 O TYR D 355
SHEET 3 AB5 4 GLY D 382 ILE D 396 -1 O ALA D 388 N ALA D 295
SHEET 4 AB5 4 THR D 401 SER D 405 -1 O VAL D 402 N PHE D 395
SHEET 1 AB6 6 VAL D 353 ASN D 358 0
SHEET 2 AB6 6 ILE D 289 PHE D 297 -1 N VAL D 292 O TYR D 355
SHEET 3 AB6 6 GLY D 382 ILE D 396 -1 O ALA D 388 N ALA D 295
SHEET 4 AB6 6 GLN D 417 ALA D 428 -1 O VAL D 418 N PHE D 389
SHEET 5 AB6 6 VAL D 339 ASP D 341 -1 N VAL D 339 O ARG D 419
SHEET 6 AB6 6 PHE D 473 PHE D 474 1 O PHE D 473 N VAL D 340
SHEET 1 AB7 4 ARG D 369 HIS D 377 0
SHEET 2 AB7 4 THR D 433 ALA D 442 -1 O LEU D 434 N PHE D 376
SHEET 3 AB7 4 TYR D 448 VAL D 456 -1 O SER D 451 N LEU D 439
SHEET 4 AB7 4 LYS D 462 ASP D 468 -1 O SER D 463 N ALA D 454
LINK C ACE F 0 N GLY F 1 1555 1555 1.33
LINK C ACE G 0 N GLY G 1 1555 1555 1.35
LINK C ACE H 0 N GLY H 1 1555 1555 1.34
LINK C ACE I 0 N GLY I 1 1555 1555 1.35
CISPEP 1 PHE A 286 PRO A 287 0 6.50
CISPEP 2 PHE B 286 PRO B 287 0 8.44
CISPEP 3 PHE C 286 PRO C 287 0 4.46
CISPEP 4 PHE D 286 PRO D 287 0 0.61
SITE 1 AC1 22 TYR A 149 PHE A 150 TYR A 153 GLN A 159
SITE 2 AC1 22 MET A 162 ARG A 168 CYS A 193 ILE A 197
SITE 3 AC1 22 LEU A 198 GLU A 214 ALA A 215 LYS A 241
SITE 4 AC1 22 VAL A 242 GLU A 243 GLU A 257 MET A 268
SITE 5 AC1 22 SER A 271 HOH A 606 HOH A 608 HOH A 610
SITE 6 AC1 22 HOH A 625 ARG F 5
SITE 1 AC2 2 ASP A 392 SER A 405
SITE 1 AC3 4 GLN A 148 LYS A 470 HOH A 672 GLN B 151
SITE 1 AC4 22 TYR B 149 PHE B 150 TYR B 153 GLN B 159
SITE 2 AC4 22 MET B 162 ARG B 168 CYS B 193 ILE B 197
SITE 3 AC4 22 LEU B 198 GLU B 214 ALA B 215 LYS B 241
SITE 4 AC4 22 VAL B 242 GLU B 243 GLU B 257 MET B 268
SITE 5 AC4 22 SER B 271 HOH B 617 HOH B 618 HOH B 643
SITE 6 AC4 22 HOH B 647 ARG G 5
SITE 1 AC5 5 GLN A 151 GLN B 148 ARG B 445 LYS B 470
SITE 2 AC5 5 HOH G 103
SITE 1 AC6 22 TYR C 149 PHE C 150 TYR C 153 GLN C 159
SITE 2 AC6 22 MET C 162 ARG C 168 CYS C 193 ILE C 197
SITE 3 AC6 22 LEU C 198 GLU C 214 ALA C 215 LYS C 241
SITE 4 AC6 22 VAL C 242 GLU C 243 GLU C 257 MET C 268
SITE 5 AC6 22 SER C 271 HOH C 602 HOH C 618 HOH C 623
SITE 6 AC6 22 HOH C 664 ARG H 5
SITE 1 AC7 2 ASP C 392 TRP C 403
SITE 1 AC8 5 GLN C 148 ARG C 445 LYS C 470 GLN D 151
SITE 2 AC8 5 LYS H 2
SITE 1 AC9 22 TYR D 149 PHE D 150 TYR D 153 GLN D 159
SITE 2 AC9 22 MET D 162 ARG D 168 CYS D 193 ILE D 197
SITE 3 AC9 22 LEU D 198 GLU D 214 ALA D 215 LYS D 241
SITE 4 AC9 22 VAL D 242 GLU D 243 GLU D 257 MET D 268
SITE 5 AC9 22 SER D 271 HOH D 612 HOH D 613 HOH D 640
SITE 6 AC9 22 HOH D 655 ARG I 5
SITE 1 AD1 6 GLN C 151 GLN D 148 ARG D 445 LYS D 470
SITE 2 AD1 6 HOH D 628 LYS I 2
CRYST1 75.722 98.847 208.670 90.00 90.00 90.00 P 21 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013206 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010117 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004792 0.00000
(ATOM LINES ARE NOT SHOWN.)
END