HEADER TRANSCRIPTION 23-SEP-16 5TF2
TITLE CRYSTAL STRUCTURE OF THE WD40 DOMAIN OF THE HUMAN PROLACTIN REGULATORY
TITLE 2 ELEMENT-BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLACTIN REGULATORY ELEMENT-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WD40 DOMAIN, RESIDUES 1-386;
COMPND 5 SYNONYM: MAMMALIAN GUANINE NUCLEOTIDE EXCHANGE FACTOR MSEC12;
COMPND 6 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: PREB, SEC12;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFBOH-MHL
KEYWDS WD40, ACTIVATOR, PROTEIN TRANSPORT, TRANSCRIPTION, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM (SGC)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,Q.ZHANG,A.DONG,A.WERNIMONT,Y.LI,H.HE,W.TEMPEL,C.BOUNTRA,
AUTHOR 2 A.M.EDWARDS,C.H.ARROWSMITH,Z.CHEN,Y.TONG,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 4 04-OCT-23 5TF2 1 REMARK
REVDAT 3 24-JAN-18 5TF2 1 AUTHOR JRNL
REVDAT 2 16-AUG-17 5TF2 1 SOURCE
REVDAT 1 23-NOV-16 5TF2 0
JRNL AUTH J.R.WALKER,Q.ZHANG,A.DONG,A.WERNIMONT,Y.LI,H.HE,W.TEMPEL,
JRNL AUTH 2 C.BOUNTRA,A.M.EDWARDS,C.H.ARROWSMITH,Z.CHEN,Y.TONG,
JRNL AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL CRYSTAL STRUCTURE OF THE WD40 DOMAIN OF THE HUMAN PROLACTIN
JRNL TITL 2 REGULATORY ELEMENT-BINDING PROTEIN (CASP TARGET)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 15265
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 784
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1102
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2519
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : 0.51000
REMARK 3 B33 (A**2) : -1.64000
REMARK 3 B12 (A**2) : 0.25000
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): 0.384
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.250
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.183
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.049
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2602 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2425 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3553 ; 1.305 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5547 ; 0.849 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 339 ; 6.614 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;31.632 ;23.558
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 380 ;13.107 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.866 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 415 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2989 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 601 ; 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): 1362 ; 0.804 ; 2.976
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1361 ; 0.802 ; 2.975
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1699 ; 1.482 ; 4.453
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 386
REMARK 3 ORIGIN FOR THE GROUP (A): 99.5777 61.3455 8.8601
REMARK 3 T TENSOR
REMARK 3 T11: 0.0371 T22: 0.0915
REMARK 3 T33: 0.0486 T12: -0.0324
REMARK 3 T13: -0.0159 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 3.4355 L22: 2.1240
REMARK 3 L33: 1.6411 L12: -0.1053
REMARK 3 L13: 0.8192 L23: 0.1187
REMARK 3 S TENSOR
REMARK 3 S11: -0.1509 S12: -0.0680 S13: 0.1374
REMARK 3 S21: -0.0578 S22: 0.0503 S23: -0.0212
REMARK 3 S31: -0.1386 S32: 0.0445 S33: 0.1006
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 : WITH TLS ADDED
REMARK 4
REMARK 4 5TF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000222869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92045
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16070
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : 0.77900
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: BALBES
REMARK 200 STARTING MODEL: 1ERJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PREB PROTEIN WAS MIXED WITH ELASTASE
REMARK 280 AT 1:1000 (W/W) RATIO BEFORE SETTING UP CRYSTALLIZATION.
REMARK 280 CRYSTALS WERE GROWN AT 293 K USING THE SITTING DROP METHOD BY
REMARK 280 MIXING 0.5 UL PROTEIN WITH 0.5 UL WELL SOLUTION CONSISTING OF
REMARK 280 1.4M MALONATE, PH 7.0. THE CRYSTALS WERE CRYOPROTECTED BY
REMARK 280 IMMERSION IN PARATONE., VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
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 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+2/3
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 27.67133
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 55.34267
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.67133
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 55.34267
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 27.67133
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 55.34267
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 27.67133
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 55.34267
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 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 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 -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 ARG A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 GLY A 55
REMARK 465 GLN A 99
REMARK 465 GLN A 100
REMARK 465 GLN A 101
REMARK 465 GLY A 102
REMARK 465 ASN A 103
REMARK 465 LYS A 104
REMARK 465 ALA A 105
REMARK 465 GLU A 106
REMARK 465 LYS A 107
REMARK 465 ALA A 108
REMARK 465 GLY A 109
REMARK 465 SER A 110
REMARK 465 LYS A 111
REMARK 465 GLU A 112
REMARK 465 GLN A 113
REMARK 465 GLY A 114
REMARK 465 PRO A 115
REMARK 465 ARG A 116
REMARK 465 GLN A 117
REMARK 465 ARG A 118
REMARK 465 LYS A 119
REMARK 465 GLY A 120
REMARK 465 ALA A 121
REMARK 465 ALA A 122
REMARK 465 PRO A 123
REMARK 465 ALA A 124
REMARK 465 GLU A 125
REMARK 465 LYS A 126
REMARK 465 LYS A 127
REMARK 465 CYS A 128
REMARK 465 GLY A 129
REMARK 465 ALA A 130
REMARK 465 GLU A 131
REMARK 465 THR A 132
REMARK 465 GLN A 133
REMARK 465 HIS A 134
REMARK 465 GLU A 135
REMARK 465 GLY A 136
REMARK 465 ASN A 236
REMARK 465 GLY A 237
REMARK 465 ARG A 387
REMARK 465 SER A 388
REMARK 465 VAL A 389
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 LYS A 38 CG CD CE NZ
REMARK 470 THR A 39 OG1 CG2
REMARK 470 LYS A 42 NZ
REMARK 470 GLN A 49 OE1 NE2
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 ILE A 53 CD1
REMARK 470 ASN A 54 CG OD1 ND2
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 68 CG CD OE1 OE2
REMARK 470 HIS A 98 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 138 CG CD OE1 OE2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 182 NZ
REMARK 470 LYS A 193 NZ
REMARK 470 ASP A 207 OD1 OD2
REMARK 470 LYS A 209 CE NZ
REMARK 470 LYS A 218 CE NZ
REMARK 470 LYS A 224 CD CE NZ
REMARK 470 GLN A 234 CG CD OE1 NE2
REMARK 470 PRO A 238 CG CD
REMARK 470 THR A 239 OG1 CG2
REMARK 470 SER A 241 OG
REMARK 470 SER A 242 OG
REMARK 470 LEU A 262 CG CD1 CD2
REMARK 470 LYS A 272 CD CE NZ
REMARK 470 GLU A 310 CG CD OE1 OE2
REMARK 470 LYS A 355 CD CE NZ
REMARK 470 ARG A 357 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 360 CG CD OE1 OE2
REMARK 470 ARG A 386 CG CD NE CZ NH1 NH2
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 GLU A 68 -118.40 61.34
REMARK 500 ASP A 87 -124.67 46.89
REMARK 500 LEU A 144 -150.94 -117.16
REMARK 500 PHE A 151 45.01 -140.59
REMARK 500 LYS A 224 -118.21 51.24
REMARK 500 PHE A 240 42.57 -94.19
REMARK 500 ASP A 375 1.48 -68.90
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5TF2 A 1 389 UNP Q9HCU5 PREB_HUMAN 1 389
SEQADV 5TF2 MET A -17 UNP Q9HCU5 INITIATING METHIONINE
SEQADV 5TF2 HIS A -16 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 HIS A -15 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 HIS A -14 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 HIS A -13 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 HIS A -12 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 HIS A -11 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 SER A -10 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 SER A -9 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 GLY A -8 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 ARG A -7 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 GLU A -6 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 ASN A -5 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 LEU A -4 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 TYR A -3 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 PHE A -2 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 GLN A -1 UNP Q9HCU5 EXPRESSION TAG
SEQADV 5TF2 GLY A 0 UNP Q9HCU5 EXPRESSION TAG
SEQRES 1 A 407 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 407 LEU TYR PHE GLN GLY MET GLY ARG ARG ARG ALA PRO GLU
SEQRES 3 A 407 LEU TYR ARG ALA PRO PHE PRO LEU TYR ALA LEU GLN VAL
SEQRES 4 A 407 ASP PRO SER THR GLY LEU LEU ILE ALA ALA GLY GLY GLY
SEQRES 5 A 407 GLY ALA ALA LYS THR GLY ILE LYS ASN GLY VAL HIS PHE
SEQRES 6 A 407 LEU GLN LEU GLU LEU ILE ASN GLY ARG LEU SER ALA SER
SEQRES 7 A 407 LEU LEU HIS SER HIS ASP THR GLU THR ARG ALA THR MET
SEQRES 8 A 407 ASN LEU ALA LEU ALA GLY ASP ILE LEU ALA ALA GLY GLN
SEQRES 9 A 407 ASP ALA HIS CYS GLN LEU LEU ARG PHE GLN ALA HIS GLN
SEQRES 10 A 407 GLN GLN GLY ASN LYS ALA GLU LYS ALA GLY SER LYS GLU
SEQRES 11 A 407 GLN GLY PRO ARG GLN ARG LYS GLY ALA ALA PRO ALA GLU
SEQRES 12 A 407 LYS LYS CYS GLY ALA GLU THR GLN HIS GLU GLY LEU GLU
SEQRES 13 A 407 LEU ARG VAL GLU ASN LEU GLN ALA VAL GLN THR ASP PHE
SEQRES 14 A 407 SER SER ASP PRO LEU GLN LYS VAL VAL CYS PHE ASN HIS
SEQRES 15 A 407 ASP ASN THR LEU LEU ALA THR GLY GLY THR ASP GLY TYR
SEQRES 16 A 407 VAL ARG VAL TRP LYS VAL PRO SER LEU GLU LYS VAL LEU
SEQRES 17 A 407 GLU PHE LYS ALA HIS GLU GLY GLU ILE GLU ASP LEU ALA
SEQRES 18 A 407 LEU GLY PRO ASP GLY LYS LEU VAL THR VAL GLY ARG ASP
SEQRES 19 A 407 LEU LYS ALA SER VAL TRP GLN LYS ASP GLN LEU VAL THR
SEQRES 20 A 407 GLN LEU HIS TRP GLN GLU ASN GLY PRO THR PHE SER SER
SEQRES 21 A 407 THR PRO TYR ARG TYR GLN ALA CYS ARG PHE GLY GLN VAL
SEQRES 22 A 407 PRO ASP GLN PRO ALA GLY LEU ARG LEU PHE THR VAL GLN
SEQRES 23 A 407 ILE PRO HIS LYS ARG LEU ARG GLN PRO PRO PRO CYS TYR
SEQRES 24 A 407 LEU THR ALA TRP ASP GLY SER ASN PHE LEU PRO LEU ARG
SEQRES 25 A 407 THR LYS SER CYS GLY HIS GLU VAL VAL SER CYS LEU ASP
SEQRES 26 A 407 VAL SER GLU SER GLY THR PHE LEU GLY LEU GLY THR VAL
SEQRES 27 A 407 THR GLY SER VAL ALA ILE TYR ILE ALA PHE SER LEU GLN
SEQRES 28 A 407 CYS LEU TYR TYR VAL ARG GLU ALA HIS GLY ILE VAL VAL
SEQRES 29 A 407 THR ASP VAL ALA PHE LEU PRO GLU LYS GLY ARG GLY PRO
SEQRES 30 A 407 GLU LEU LEU GLY SER HIS GLU THR ALA LEU PHE SER VAL
SEQRES 31 A 407 ALA VAL ASP SER ARG CYS GLN LEU HIS LEU LEU PRO SER
SEQRES 32 A 407 ARG ARG SER VAL
HET UNX A 401 1
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 2 UNX X
FORMUL 3 HOH *20(H2 O)
HELIX 1 AA1 PRO A 206 GLY A 208 5 3
HELIX 2 AA2 ARG A 357 GLY A 363 1 7
SHEET 1 AA1 4 TYR A 10 ARG A 11 0
SHEET 2 AA1 4 ARG A 377 LEU A 382 -1 O CYS A 378 N TYR A 10
SHEET 3 AA1 4 ALA A 368 ALA A 373 -1 N LEU A 369 O HIS A 381
SHEET 4 AA1 4 VAL A 346 PHE A 351 -1 N ALA A 350 O PHE A 370
SHEET 1 AA2 4 LEU A 16 ASP A 22 0
SHEET 2 AA2 4 LEU A 27 GLY A 33 -1 O ILE A 29 N GLN A 20
SHEET 3 AA2 4 ASN A 43 LEU A 52 -1 O HIS A 46 N ALA A 30
SHEET 4 AA2 4 LEU A 57 ASP A 66 -1 O LEU A 62 N PHE A 47
SHEET 1 AA3 4 THR A 72 ALA A 78 0
SHEET 2 AA3 4 ILE A 81 GLN A 86 -1 O ALA A 83 N ALA A 76
SHEET 3 AA3 4 HIS A 89 ALA A 97 -1 O GLN A 91 N ALA A 84
SHEET 4 AA3 4 LEU A 139 GLN A 148 -1 O ARG A 140 N GLN A 96
SHEET 1 AA4 4 GLN A 157 PHE A 162 0
SHEET 2 AA4 4 LEU A 168 GLY A 173 -1 O ALA A 170 N CYS A 161
SHEET 3 AA4 4 TYR A 177 LYS A 182 -1 O TRP A 181 N LEU A 169
SHEET 4 AA4 4 LYS A 188 LYS A 193 -1 O VAL A 189 N VAL A 180
SHEET 1 AA5 4 ILE A 199 LEU A 204 0
SHEET 2 AA5 4 LEU A 210 GLY A 214 -1 O VAL A 213 N GLU A 200
SHEET 3 AA5 4 ALA A 219 GLN A 223 -1 O TRP A 222 N LEU A 210
SHEET 4 AA5 4 GLN A 226 LEU A 231 -1 O VAL A 228 N VAL A 221
SHEET 1 AA6 4 TYR A 245 GLN A 254 0
SHEET 2 AA6 4 LEU A 262 PRO A 270 -1 O PHE A 265 N ARG A 251
SHEET 3 AA6 4 TYR A 281 ASP A 286 -1 O TRP A 285 N LEU A 264
SHEET 4 AA6 4 PRO A 292 SER A 297 -1 O ARG A 294 N ALA A 284
SHEET 1 AA7 4 VAL A 303 VAL A 308 0
SHEET 2 AA7 4 PHE A 314 THR A 319 -1 O GLY A 318 N SER A 304
SHEET 3 AA7 4 VAL A 324 ILE A 328 -1 O TYR A 327 N LEU A 315
SHEET 4 AA7 4 GLN A 333 VAL A 338 -1 O LEU A 335 N ILE A 326
CISPEP 1 VAL A 183 PRO A 184 0 5.89
CRYST1 160.708 160.708 83.014 90.00 90.00 120.00 P 64 2 2 12
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 0.006222 0.003593 0.000000 0.00000
SCALE2 0.000000 0.007185 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012046 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
