HEADER TRANSFERASE 29-SEP-08 3EP0
TITLE METHYLTRANSFERASE DOMAIN OF HUMAN PR DOMAIN-CONTAINING PROTEIN 12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PR DOMAIN ZINC FINGER PROTEIN 12;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PR DOMAIN-CONTAINING PROTEIN 12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: MAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PRDM12, PFM9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PR DOMAIN-CONTAINING PROTEIN 12, PR DOMAIN ZINC FINGER PROTEIN 12,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, DNA-
KEYWDS 3 BINDING, METAL-BINDING, NUCLEUS, TRANSCRIPTION, TRANSCRIPTION
KEYWDS 4 REGULATION, ZINC, ZINC-FINGER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.AMAYA,H.ZENG,P.LOPPNAU,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,A.BOTCHKAREV,J.MIN,A.N.PLOTNIKOV,H.WU,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 4 06-SEP-23 3EP0 1 REMARK
REVDAT 3 25-AUG-09 3EP0 1 REMARK
REVDAT 2 24-FEB-09 3EP0 1 VERSN
REVDAT 1 04-NOV-08 3EP0 0
JRNL AUTH H.ZENG,M.F.AMAYA,P.LOPPNAU,J.MIN,A.N.PLOTNIKOV,H.WU
JRNL TITL THE CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN
JRNL TITL 2 PR DOMAIN-CONTAINING PROTEIN 12.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 21829
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) : 0.259
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1124
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1363
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1741
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 68
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.76000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : -0.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.202
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.916
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.908
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1781 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2419 ; 1.287 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 220 ; 6.784 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;32.861 ;25.211
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 286 ;14.024 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;25.198 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 271 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1326 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 721 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1202 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 100 ; 0.136 ; 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): 60 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.166 ; 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): 1148 ; 0.848 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1792 ; 1.388 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 759 ; 1.696 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 627 ; 2.526 ; 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 3EP0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049595.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21829
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 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: PDB ENTRY 3DAL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PURIFIED PRDM12 WAS CRYSTALLIZED USING
REMARK 280 HANGING DROP VAPOR DIFFUSION METHOD AT 293K BY MIXING THE
REMARK 280 PROTEIN SOLUTION WITH THE RESERVOIR SOLUTION CONTAINING 19% PEG
REMARK 280 2,000 MME, 0.1 M KSCN., VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 69.44100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.17900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 69.44100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 17.17900
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 LYS A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 PHE A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 GLN A 11
REMARK 465 SER A 12
REMARK 465 PHE A 13
REMARK 465 SER A 14
REMARK 465 GLY A 15
REMARK 465 GLU A 16
REMARK 465 GLU A 66
REMARK 465 HIS A 67
REMARK 465 VAL A 68
REMARK 465 ASP A 69
REMARK 465 ILE A 70
REMARK 465 CYS A 71
REMARK 465 LYS A 72
REMARK 465 ASN A 73
REMARK 465 ASN A 74
REMARK 465 ASN A 75
REMARK 465 SER A 94
REMARK 465 GLN A 95
REMARK 465 GLU A 96
REMARK 465 ASP A 97
REMARK 465 HIS A 98
REMARK 465 ARG A 99
REMARK 465 SER A 146
REMARK 465 HIS A 147
REMARK 465 ASN A 148
REMARK 465 THR A 149
REMARK 465 PHE A 150
REMARK 465 LEU A 151
REMARK 465 GLY A 152
REMARK 465 ILE A 153
REMARK 465 PRO A 154
REMARK 465 GLY A 155
REMARK 465 VAL A 156
REMARK 465 PRO A 157
REMARK 465 GLY A 158
REMARK 465 LEU A 159
REMARK 465 GLU A 160
REMARK 465 GLU A 161
REMARK 465 ASP A 162
REMARK 465 GLN A 163
REMARK 465 LYS A 164
REMARK 465 LYS A 165
REMARK 465 ASN A 166
REMARK 465 LYS A 167
REMARK 465 HIS A 168
REMARK 465 GLU A 169
REMARK 465 ASP A 170
REMARK 465 LYS B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 PHE B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 GLU B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 GLN B 11
REMARK 465 SER B 12
REMARK 465 PHE B 13
REMARK 465 SER B 14
REMARK 465 GLY B 15
REMARK 465 GLU B 16
REMARK 465 GLU B 66
REMARK 465 HIS B 67
REMARK 465 VAL B 68
REMARK 465 ASP B 69
REMARK 465 ILE B 70
REMARK 465 CYS B 71
REMARK 465 LYS B 72
REMARK 465 ASN B 73
REMARK 465 ASN B 74
REMARK 465 ASN B 75
REMARK 465 SER B 94
REMARK 465 GLN B 95
REMARK 465 GLU B 96
REMARK 465 ASP B 97
REMARK 465 HIS B 98
REMARK 465 ARG B 99
REMARK 465 SER B 146
REMARK 465 HIS B 147
REMARK 465 ASN B 148
REMARK 465 THR B 149
REMARK 465 PHE B 150
REMARK 465 LEU B 151
REMARK 465 GLY B 152
REMARK 465 ILE B 153
REMARK 465 PRO B 154
REMARK 465 GLY B 155
REMARK 465 VAL B 156
REMARK 465 PRO B 157
REMARK 465 GLY B 158
REMARK 465 LEU B 159
REMARK 465 GLU B 160
REMARK 465 GLU B 161
REMARK 465 ASP B 162
REMARK 465 GLN B 163
REMARK 465 LYS B 164
REMARK 465 LYS B 165
REMARK 465 ASN B 166
REMARK 465 LYS B 167
REMARK 465 HIS B 168
REMARK 465 GLU B 169
REMARK 465 ASP B 170
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 17 CG1 CG2
REMARK 470 LEU A 23 CD1 CD2
REMARK 470 ILE A 36 CB CG1 CG2 CD1
REMARK 470 LYS A 50 CG CD CE NZ
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 ALA A 64 CB
REMARK 470 GLU A 131 CD OE1 OE2
REMARK 470 MET A 132 CG SD CE
REMARK 470 ASN A 145 CG OD1 ND2
REMARK 470 VAL B 17 CG1 CG2
REMARK 470 GLN B 18 CG CD OE1 NE2
REMARK 470 GLU B 39 CG CD OE1 OE2
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 ALA B 64 CB
REMARK 470 GLU B 83 CG CD OE1 OE2
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 37 C - N - CA ANGL. DEV. = 9.6 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 PRO A 37 -58.61 -29.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3EP0 A 1 170 UNP Q9H4Q4 PRD12_HUMAN 60 229
DBREF 3EP0 B 1 170 UNP Q9H4Q4 PRD12_HUMAN 60 229
SEQRES 1 A 170 LYS THR ALA PHE THR ALA GLU VAL LEU ALA GLN SER PHE
SEQRES 2 A 170 SER GLY GLU VAL GLN LYS LEU SER SER LEU VAL LEU PRO
SEQRES 3 A 170 ALA GLU VAL ILE ILE ALA GLN SER SER ILE PRO GLY GLU
SEQRES 4 A 170 GLY LEU GLY ILE PHE SER LYS THR TRP ILE LYS ALA GLY
SEQRES 5 A 170 THR GLU MET GLY PRO PHE THR GLY ARG VAL ILE ALA PRO
SEQRES 6 A 170 GLU HIS VAL ASP ILE CYS LYS ASN ASN ASN LEU MET TRP
SEQRES 7 A 170 GLU VAL PHE ASN GLU ASP GLY THR VAL ARG TYR PHE ILE
SEQRES 8 A 170 ASP ALA SER GLN GLU ASP HIS ARG SER TRP MET THR TYR
SEQRES 9 A 170 ILE LYS CYS ALA ARG ASN GLU GLN GLU GLN ASN LEU GLU
SEQRES 10 A 170 VAL VAL GLN ILE GLY THR SER ILE PHE TYR LYS ALA ILE
SEQRES 11 A 170 GLU MET ILE PRO PRO ASP GLN GLU LEU LEU VAL TRP TYR
SEQRES 12 A 170 GLY ASN SER HIS ASN THR PHE LEU GLY ILE PRO GLY VAL
SEQRES 13 A 170 PRO GLY LEU GLU GLU ASP GLN LYS LYS ASN LYS HIS GLU
SEQRES 14 A 170 ASP
SEQRES 1 B 170 LYS THR ALA PHE THR ALA GLU VAL LEU ALA GLN SER PHE
SEQRES 2 B 170 SER GLY GLU VAL GLN LYS LEU SER SER LEU VAL LEU PRO
SEQRES 3 B 170 ALA GLU VAL ILE ILE ALA GLN SER SER ILE PRO GLY GLU
SEQRES 4 B 170 GLY LEU GLY ILE PHE SER LYS THR TRP ILE LYS ALA GLY
SEQRES 5 B 170 THR GLU MET GLY PRO PHE THR GLY ARG VAL ILE ALA PRO
SEQRES 6 B 170 GLU HIS VAL ASP ILE CYS LYS ASN ASN ASN LEU MET TRP
SEQRES 7 B 170 GLU VAL PHE ASN GLU ASP GLY THR VAL ARG TYR PHE ILE
SEQRES 8 B 170 ASP ALA SER GLN GLU ASP HIS ARG SER TRP MET THR TYR
SEQRES 9 B 170 ILE LYS CYS ALA ARG ASN GLU GLN GLU GLN ASN LEU GLU
SEQRES 10 B 170 VAL VAL GLN ILE GLY THR SER ILE PHE TYR LYS ALA ILE
SEQRES 11 B 170 GLU MET ILE PRO PRO ASP GLN GLU LEU LEU VAL TRP TYR
SEQRES 12 B 170 GLY ASN SER HIS ASN THR PHE LEU GLY ILE PRO GLY VAL
SEQRES 13 B 170 PRO GLY LEU GLU GLU ASP GLN LYS LYS ASN LYS HIS GLU
SEQRES 14 B 170 ASP
FORMUL 3 HOH *68(H2 O)
HELIX 1 1 SER A 100 ILE A 105 5 6
HELIX 2 2 SER B 100 ILE B 105 5 6
SHEET 1 A 6 LYS A 19 SER A 21 0
SHEET 2 A 6 GLU A 54 PHE A 58 1 O GLU A 54 N LEU A 20
SHEET 3 A 6 SER A 124 ALA A 129 -1 O TYR A 127 N MET A 55
SHEET 4 A 6 LEU A 116 ILE A 121 -1 N ILE A 121 O SER A 124
SHEET 5 A 6 LEU A 140 TYR A 143 1 O TRP A 142 N VAL A 118
SHEET 6 A 6 LYS A 106 CYS A 107 1 N LYS A 106 O VAL A 141
SHEET 1 B 2 VAL A 29 GLN A 33 0
SHEET 2 B 2 LEU A 41 SER A 45 -1 O PHE A 44 N ILE A 30
SHEET 1 C 3 ARG A 61 ILE A 63 0
SHEET 2 C 3 VAL A 87 ASP A 92 -1 O ASP A 92 N ARG A 61
SHEET 3 C 3 MET A 77 PHE A 81 -1 N VAL A 80 O TYR A 89
SHEET 1 D 7 LYS B 19 SER B 21 0
SHEET 2 D 7 GLU B 54 PHE B 58 1 O GLU B 54 N LEU B 20
SHEET 3 D 7 SER B 124 ALA B 129 -1 O ILE B 125 N PHE B 58
SHEET 4 D 7 LEU B 116 ILE B 121 -1 N ILE B 121 O SER B 124
SHEET 5 D 7 GLU B 138 TYR B 143 1 O LEU B 140 N LEU B 116
SHEET 6 D 7 LEU B 41 SER B 45 -1 N ILE B 43 O LEU B 139
SHEET 7 D 7 VAL B 29 GLN B 33 -1 N ILE B 30 O PHE B 44
SHEET 1 E 6 LYS B 19 SER B 21 0
SHEET 2 E 6 GLU B 54 PHE B 58 1 O GLU B 54 N LEU B 20
SHEET 3 E 6 SER B 124 ALA B 129 -1 O ILE B 125 N PHE B 58
SHEET 4 E 6 LEU B 116 ILE B 121 -1 N ILE B 121 O SER B 124
SHEET 5 E 6 GLU B 138 TYR B 143 1 O LEU B 140 N LEU B 116
SHEET 6 E 6 LYS B 106 CYS B 107 1 N LYS B 106 O VAL B 141
SHEET 1 F 3 ARG B 61 ILE B 63 0
SHEET 2 F 3 VAL B 87 ASP B 92 -1 O PHE B 90 N ILE B 63
SHEET 3 F 3 MET B 77 PHE B 81 -1 N VAL B 80 O TYR B 89
CISPEP 1 GLY A 56 PRO A 57 0 -1.57
CISPEP 2 GLY B 56 PRO B 57 0 -0.14
CRYST1 138.882 34.358 103.739 90.00 131.09 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007200 0.000000 0.006279 0.00000
SCALE2 0.000000 0.029105 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012790 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
