HEADER TRANSFERASE 11-OCT-05 2B9E
TITLE HUMAN NSUN5 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOL1/NOP2/SUN DOMAIN FAMILY, MEMBER 5 ISOFORM 2;
COMPND 3 CHAIN: A;
COMPND 4 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 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P28A-LIC
KEYWDS METHYTRANSFERASE, NOL1/NOP2/SUN DOMAIN FAMILY, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.MIN,H.WU,H.ZENG,P.LOPPNAU,M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 A.BOCHKAREV,A.N.PLOTNIKOV,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 23-AUG-23 2B9E 1 REMARK SEQADV
REVDAT 4 24-FEB-09 2B9E 1 VERSN
REVDAT 3 10-JUL-07 2B9E 1 SEQADV SEQRES REMARK MASTER
REVDAT 2 21-MAR-06 2B9E 1 JRNL
REVDAT 1 18-OCT-05 2B9E 0
JRNL AUTH J.R.MIN,H.WU,H.ZENG,P.LOPPNAU,M.SUNDSTROM,C.H.ARROWSMITH,
JRNL AUTH 2 A.M.EDWARDS,A.BOCHKAREV,A.N.PLOTNIKOV
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN NSUN5 PROTEIN IN COMPLEX WITH
JRNL TITL 2 S-ADENOSYL-L-METHIONINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 38415
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2038
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2782
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2127
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 432
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.83000
REMARK 3 B22 (A**2) : 0.83000
REMARK 3 B33 (A**2) : -1.25000
REMARK 3 B12 (A**2) : 0.42000
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): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.638
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2208 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3004 ; 1.326 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 6.529 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;35.119 ;22.887
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 346 ;12.073 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;22.224 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 338 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1689 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1093 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1511 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 335 ; 0.117 ; 0.200
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): 42 ; 0.244 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.151 ; 0.200
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): 1412 ; 0.913 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2219 ; 1.571 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 877 ; 2.135 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 785 ; 3.314 ; 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2B9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034839.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38415
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 59.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
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: AMORE
REMARK 200 STARTING MODEL: 1IXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NSUN5 WAS COMPLEXED WITH S-ADENOSYL-L
REMARK 280 -METHIONINE (SAM) (SIGMA) AT 1:10 MOLAR RATIO OF PROTEIN :SAM
REMARK 280 AND CRYSTALLIZED USING THE SITTING DROP VAPOR DIFFUSION METHOD
REMARK 280 AT 20 C BY MIXING 1 L OF THE PROTEIN SOLUTION WITH 1 L OF THE
REMARK 280 RESERVOIR SOLUTION CONTAINING 10% ISO-PROPANOLE, 20% PEG 4000,
REMARK 280 0.1M NA HEPES PH 7.5. , VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.55533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 119.11067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 119.11067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 59.55533
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1242 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1255 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1595 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 125
REMARK 465 SER A 126
REMARK 465 ARG A 127
REMARK 465 PRO A 128
REMARK 465 GLY A 129
REMARK 465 PRO A 130
REMARK 465 ALA A 131
REMARK 465 SER A 132
REMARK 465 SER A 311
REMARK 465 GLY A 312
REMARK 465 MET A 313
REMARK 465 PRO A 314
REMARK 465 SER A 315
REMARK 465 ARG A 316
REMARK 465 GLN A 317
REMARK 465 LEU A 318
REMARK 465 GLU A 319
REMARK 465 GLU A 320
REMARK 465 PRO A 321
REMARK 465 GLY A 322
REMARK 465 ALA A 323
REMARK 465 GLY A 324
REMARK 465 THR A 325
REMARK 465 PRO A 326
REMARK 465 SER A 327
REMARK 465 PRO A 328
REMARK 465 GLU A 426
REMARK 465 VAL A 427
REMARK 465 PRO A 428
REMARK 465 ARG A 429
REMARK 465 ARG A 430
REMARK 465 ALA A 431
REMARK 465 ARG A 432
REMARK 465 GLY A 433
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1347 O HOH A 1629 6555 2.18
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 GLN A 194 47.16 -96.82
REMARK 500 SER A 309 -92.85 -32.25
REMARK 500 ARG A 330 30.86 -93.46
REMARK 500 ASN A 366 -96.71 -121.84
REMARK 500 LEU A 387 72.32 27.14
REMARK 500 SER A 415 153.02 -47.95
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 ARG A 330 LEU A 331 -146.08
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 SAM A 1201
DBREF 2B9E A 127 429 UNP Q9NW70 Q9NW70_HUMAN 127 429
SEQADV 2B9E GLY A 125 GB 8922322 CLONING ARTIFACT
SEQADV 2B9E SER A 126 GB 8922322 CLONING ARTIFACT
SEQADV 2B9E ARG A 430 GB 8922322 CLONING ARTIFACT
SEQADV 2B9E ALA A 431 GB 8922322 CLONING ARTIFACT
SEQADV 2B9E ARG A 432 GB 8922322 CLONING ARTIFACT
SEQADV 2B9E GLY A 433 GB 8922322 CLONING ARTIFACT
SEQRES 1 A 309 GLY SER ARG PRO GLY PRO ALA SER GLN LEU PRO ARG PHE
SEQRES 2 A 309 VAL ARG VAL ASN THR LEU LYS THR CYS SER ASP ASP VAL
SEQRES 3 A 309 VAL ASP TYR PHE LYS ARG GLN GLY PHE SER TYR GLN GLY
SEQRES 4 A 309 ARG ALA SER SER LEU ASP ASP LEU ARG ALA LEU LYS GLY
SEQRES 5 A 309 LYS HIS PHE LEU LEU ASP PRO LEU MET PRO GLU LEU LEU
SEQRES 6 A 309 VAL PHE PRO ALA GLN THR ASP LEU HIS GLU HIS PRO LEU
SEQRES 7 A 309 TYR ARG ALA GLY HIS LEU ILE LEU GLN ASP ARG ALA SER
SEQRES 8 A 309 CYS LEU PRO ALA MET LEU LEU ASP PRO PRO PRO GLY SER
SEQRES 9 A 309 HIS VAL ILE ASP ALA CYS ALA ALA PRO GLY ASN LYS THR
SEQRES 10 A 309 SER HIS LEU ALA ALA LEU LEU LYS ASN GLN GLY LYS ILE
SEQRES 11 A 309 PHE ALA PHE ASP LEU ASP ALA LYS ARG LEU ALA SER MET
SEQRES 12 A 309 ALA THR LEU LEU ALA ARG ALA GLY VAL SER CYS CYS GLU
SEQRES 13 A 309 LEU ALA GLU GLU ASP PHE LEU ALA VAL SER PRO SER ASP
SEQRES 14 A 309 PRO ARG TYR HIS GLU VAL HIS TYR ILE LEU LEU ASP PRO
SEQRES 15 A 309 SER CYS SER GLY SER GLY MET PRO SER ARG GLN LEU GLU
SEQRES 16 A 309 GLU PRO GLY ALA GLY THR PRO SER PRO VAL ARG LEU HIS
SEQRES 17 A 309 ALA LEU ALA GLY PHE GLN GLN ARG ALA LEU CYS HIS ALA
SEQRES 18 A 309 LEU THR PHE PRO SER LEU GLN ARG LEU VAL TYR SER THR
SEQRES 19 A 309 CYS SER LEU CYS GLN GLU GLU ASN GLU ASP VAL VAL ARG
SEQRES 20 A 309 ASP ALA LEU GLN GLN ASN PRO GLY ALA PHE ARG LEU ALA
SEQRES 21 A 309 PRO ALA LEU PRO ALA TRP PRO HIS ARG GLY LEU SER THR
SEQRES 22 A 309 PHE PRO GLY ALA GLU HIS CYS LEU ARG ALA SER PRO GLU
SEQRES 23 A 309 THR THR LEU SER SER GLY PHE PHE VAL ALA VAL ILE GLU
SEQRES 24 A 309 ARG VAL GLU VAL PRO ARG ARG ALA ARG GLY
HET SAM A1201 27
HETNAM SAM S-ADENOSYLMETHIONINE
FORMUL 2 SAM C15 H22 N6 O5 S
FORMUL 3 HOH *432(H2 O)
HELIX 1 1 CYS A 146 GLN A 157 1 12
HELIX 2 2 SER A 167 ALA A 173 1 7
HELIX 3 3 HIS A 200 ALA A 205 1 6
HELIX 4 4 ARG A 213 SER A 215 5 3
HELIX 5 5 CYS A 216 ASP A 223 1 8
HELIX 6 6 GLY A 238 LYS A 249 1 12
HELIX 7 7 ASP A 260 ALA A 274 1 15
HELIX 8 8 ASP A 285 VAL A 289 5 5
HELIX 9 9 ASP A 293 HIS A 297 5 5
HELIX 10 10 ARG A 330 LEU A 346 1 17
HELIX 11 11 CYS A 362 GLU A 365 5 4
HELIX 12 12 ASN A 366 GLN A 375 1 10
HELIX 13 13 GLY A 400 CYS A 404 5 5
HELIX 14 14 SER A 408 LEU A 413 1 6
SHEET 1 A 5 SER A 160 ARG A 164 0
SHEET 2 A 5 HIS A 178 LEU A 181 1 O PHE A 179 N GLN A 162
SHEET 3 A 5 LEU A 188 PHE A 191 -1 O VAL A 190 N LEU A 180
SHEET 4 A 5 ARG A 136 VAL A 140 -1 N VAL A 138 O LEU A 189
SHEET 5 A 5 LEU A 208 LEU A 210 -1 O ILE A 209 N ARG A 139
SHEET 1 B 7 CYS A 279 GLU A 283 0
SHEET 2 B 7 LYS A 253 ASP A 258 1 N ILE A 254 O GLU A 280
SHEET 3 B 7 HIS A 229 ASP A 232 1 N VAL A 230 O PHE A 255
SHEET 4 B 7 VAL A 299 LEU A 304 1 O LEU A 303 N ILE A 231
SHEET 5 B 7 ARG A 353 THR A 358 1 O VAL A 355 N LEU A 304
SHEET 6 B 7 PHE A 417 ARG A 424 -1 O ILE A 422 N LEU A 354
SHEET 7 B 7 PHE A 381 LEU A 383 -1 N ARG A 382 O GLU A 423
SHEET 1 C 7 CYS A 279 GLU A 283 0
SHEET 2 C 7 LYS A 253 ASP A 258 1 N ILE A 254 O GLU A 280
SHEET 3 C 7 HIS A 229 ASP A 232 1 N VAL A 230 O PHE A 255
SHEET 4 C 7 VAL A 299 LEU A 304 1 O LEU A 303 N ILE A 231
SHEET 5 C 7 ARG A 353 THR A 358 1 O VAL A 355 N LEU A 304
SHEET 6 C 7 PHE A 417 ARG A 424 -1 O ILE A 422 N LEU A 354
SHEET 7 C 7 LEU A 405 ALA A 407 -1 N LEU A 405 O VAL A 419
CISPEP 1 ALA A 236 PRO A 237 0 4.92
SITE 1 AC1 23 ALA A 233 CYS A 234 ALA A 235 ALA A 236
SITE 2 AC1 23 PRO A 237 GLY A 238 ASN A 239 LYS A 240
SITE 3 AC1 23 ASP A 258 LEU A 259 ASP A 260 ARG A 263
SITE 4 AC1 23 GLU A 284 ASP A 285 PHE A 286 ASP A 305
SITE 5 AC1 23 SER A 307 PHE A 337 HOH A1210 HOH A1361
SITE 6 AC1 23 HOH A1376 HOH A1413 HOH A1442
CRYST1 56.289 56.289 178.666 90.00 90.00 120.00 P 31 2 1 6
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 0.017765 0.010257 0.000000 0.00000
SCALE2 0.000000 0.020514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
