HEADER MEMBRANE PROTEIN 16-APR-09 3H3G
TITLE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE HUMAN PARATHYROID
TITLE 2 HORMONE RECEPTOR (PTH1R) IN COMPLEX WITH PARATHYROID HORMONE-RELATED
TITLE 3 PROTEIN (PTHRP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUSION PROTEIN OF MALTOSE-BINDING PERIPLASMIC DOMAIN AND
COMPND 3 HUMAN PARATHYROID HORMONE RECEPTOR EXTRACELLULAR DOMAIN;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 6 SYNONYM: MALTODEXTRIN-BINDING PROTEIN, MMBP, PTH/PTHR RECEPTOR,
COMPND 7 PTH/PTHRP TYPE I RECEPTOR;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PARATHYROID HORMONE-RELATED PROTEIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RESIDUES 12-34;
COMPND 13 SYNONYM: PTH-RP, PTHRP, PLP, OSTEOSTATIN;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 562, 9606;
SOURCE 4 GENE: B4034, JW3994, MALE, PTHR1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES
KEYWDS GPCR, EXTRACELLULAR DOMAIN, PTHRP, PTH, PTHR1, SUGAR TRANSPORT,
KEYWDS 2 TRANSPORT, HORMONE, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.PIOSZAK,H.E.XU
REVDAT 8 06-SEP-23 3H3G 1 HETSYN
REVDAT 7 29-JUL-20 3H3G 1 COMPND REMARK SEQADV HET
REVDAT 7 2 1 HETNAM FORMUL LINK SITE
REVDAT 7 3 1 ATOM
REVDAT 6 01-NOV-17 3H3G 1 REMARK
REVDAT 5 02-AUG-17 3H3G 1 SOURCE REMARK
REVDAT 4 13-JUL-11 3H3G 1 VERSN
REVDAT 3 20-OCT-09 3H3G 1 JRNL
REVDAT 2 25-AUG-09 3H3G 1 JRNL
REVDAT 1 11-AUG-09 3H3G 0
JRNL AUTH A.A.PIOSZAK,N.R.PARKER,T.J.GARDELLA,H.E.XU
JRNL TITL STRUCTURAL BASIS FOR PARATHYROID HORMONE-RELATED PROTEIN
JRNL TITL 2 BINDING TO THE PARATHYROID HORMONE RECEPTOR AND DESIGN OF
JRNL TITL 3 CONFORMATION-SELECTIVE PEPTIDES.
JRNL REF J.BIOL.CHEM. V. 284 28382 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19674967
JRNL DOI 10.1074/JBC.M109.022905
REMARK 2
REMARK 2 RESOLUTION. 1.94 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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 40693
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2065
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) : 1.94
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1654
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 54.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3889
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 237
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.48000
REMARK 3 B22 (A**2) : 1.48000
REMARK 3 B33 (A**2) : -2.95000
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): 0.170
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.784
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4016 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5452 ; 1.264 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 489 ; 5.664 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;32.870 ;24.728
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 663 ;16.060 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;18.828 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 588 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3059 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1805 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2723 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 255 ; 0.149 ; 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): 59 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.228 ; 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): 2529 ; 0.713 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3934 ; 1.097 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1731 ; 1.855 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1518 ; 2.858 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -344 A 26
REMARK 3 RESIDUE RANGE : A 194 A 194
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8866 -1.8562 -20.4937
REMARK 3 T TENSOR
REMARK 3 T11: -0.1622 T22: -0.1217
REMARK 3 T33: -0.2136 T12: 0.0221
REMARK 3 T13: -0.0591 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 1.6121 L22: 1.5924
REMARK 3 L33: 2.4972 L12: 0.5824
REMARK 3 L13: -1.0510 L23: -1.1657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.0930 S13: 0.0149
REMARK 3 S21: 0.0901 S22: 0.0290 S23: -0.0224
REMARK 3 S31: -0.1442 S32: -0.1058 S33: -0.0055
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 31 A 175
REMARK 3 RESIDUE RANGE : B 13 B 35
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0258 -27.7314 -58.2677
REMARK 3 T TENSOR
REMARK 3 T11: -0.1159 T22: -0.0253
REMARK 3 T33: -0.0063 T12: -0.0965
REMARK 3 T13: -0.0253 T23: 0.1466
REMARK 3 L TENSOR
REMARK 3 L11: 6.5769 L22: 2.8771
REMARK 3 L33: 9.0959 L12: 1.1465
REMARK 3 L13: 3.8690 L23: -0.3609
REMARK 3 S TENSOR
REMARK 3 S11: 0.3881 S12: -0.6622 S13: -0.5537
REMARK 3 S21: 0.1994 S22: -0.3967 S23: -0.3820
REMARK 3 S31: 0.2073 S32: -0.0523 S33: 0.0085
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 3H3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052643.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40884
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 17.00
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.44300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3C4M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.5% PEG 2000, 13% PEG 400, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.22750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.02050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.02050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.11375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.02050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.02050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 123.34125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.02050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.02050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.11375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.02050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.02050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 123.34125
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.22750
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -345
REMARK 465 GLU A 27
REMARK 465 PHE A 28
REMARK 465 ASP A 29
REMARK 465 ASP A 30
REMARK 465 GLN A 57
REMARK 465 ARG A 58
REMARK 465 PRO A 59
REMARK 465 ALA A 60
REMARK 465 SER A 61
REMARK 465 ILE A 62
REMARK 465 MET A 63
REMARK 465 GLU A 64
REMARK 465 SER A 65
REMARK 465 ASP A 66
REMARK 465 LYS A 67
REMARK 465 GLY A 68
REMARK 465 TRP A 69
REMARK 465 THR A 70
REMARK 465 SER A 71
REMARK 465 ALA A 72
REMARK 465 SER A 73
REMARK 465 THR A 74
REMARK 465 SER A 75
REMARK 465 GLY A 76
REMARK 465 LYS A 77
REMARK 465 PRO A 78
REMARK 465 ARG A 79
REMARK 465 LYS A 80
REMARK 465 ASP A 81
REMARK 465 LYS A 82
REMARK 465 ALA A 83
REMARK 465 SER A 84
REMARK 465 GLY A 85
REMARK 465 LYS A 86
REMARK 465 LEU A 87
REMARK 465 TYR A 88
REMARK 465 PRO A 89
REMARK 465 GLU A 90
REMARK 465 SER A 91
REMARK 465 GLU A 92
REMARK 465 GLU A 93
REMARK 465 ASP A 94
REMARK 465 LYS A 95
REMARK 465 GLU A 96
REMARK 465 ALA A 97
REMARK 465 PRO A 98
REMARK 465 THR A 99
REMARK 465 GLY A 100
REMARK 465 SER A 101
REMARK 465 ASN A 176
REMARK 465 GLU A 177
REMARK 465 THR A 178
REMARK 465 ARG A 179
REMARK 465 GLU A 180
REMARK 465 ARG A 181
REMARK 465 GLU A 182
REMARK 465 VAL A 183
REMARK 465 PHE A 184
REMARK 465 ASP A 185
REMARK 465 ARG A 186
REMARK 465 LEU A 187
REMARK 465 HIS A 188
REMARK 465 HIS A 189
REMARK 465 HIS A 190
REMARK 465 HIS A 191
REMARK 465 HIS A 192
REMARK 465 HIS A 193
REMARK 465 GLY B 12
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 B 13 CG CD CE NZ
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 A -303 O HOH A 224 1.87
REMARK 500 OE2 GLU A -16 O HOH A 381 2.11
REMARK 500
REMARK 500 REMARK: NULL
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 223 O HOH A 233 3545 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 19 NE ARG B 19 CZ 0.206
REMARK 500 ARG B 19 CZ ARG B 19 NH1 0.090
REMARK 500
REMARK 500 REMARK: NULL
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 ARG B 19 NE - CZ - NH2 ANGL. DEV. = -4.6 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 THR A-264 54.57 -117.84
REMARK 500 ALA A-176 -81.82 -82.23
REMARK 500 ASN A-171 113.67 -31.73
REMARK 500 HIS A 114 -5.65 85.46
REMARK 500 ILE A 115 -46.71 -130.69
REMARK 500 PHE A 173 30.62 -98.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C4M RELATED DB: PDB
REMARK 900 PTH1R ECD BOUND TO PTH
DBREF 3H3G A -344 22 UNP P0AEX9 MALE_ECOLI 26 392
DBREF 3H3G A 29 187 UNP Q03431 PTH1R_HUMAN 29 187
DBREF 3H3G B 12 34 UNP P12272 PTHR_HUMAN 48 70
SEQADV 3H3G MET A -345 UNP P0AEX9 INITIATING METHIONINE
SEQADV 3H3G ASN A 23 UNP P0AEX9 LINKER
SEQADV 3H3G ALA A 24 UNP P0AEX9 LINKER
SEQADV 3H3G ALA A 25 UNP P0AEX9 LINKER
SEQADV 3H3G ALA A 26 UNP P0AEX9 LINKER
SEQADV 3H3G GLU A 27 UNP P0AEX9 LINKER
SEQADV 3H3G PHE A 28 UNP P0AEX9 LINKER
SEQADV 3H3G HIS A 188 UNP Q03431 EXPRESSION TAG
SEQADV 3H3G HIS A 189 UNP Q03431 EXPRESSION TAG
SEQADV 3H3G HIS A 190 UNP Q03431 EXPRESSION TAG
SEQADV 3H3G HIS A 191 UNP Q03431 EXPRESSION TAG
SEQADV 3H3G HIS A 192 UNP Q03431 EXPRESSION TAG
SEQADV 3H3G HIS A 193 UNP Q03431 EXPRESSION TAG
SEQADV 3H3G NH2 B 35 UNP P12272 AMIDATION
SEQRES 1 A 539 MET ALA LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE
SEQRES 2 A 539 ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY
SEQRES 3 A 539 LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL
SEQRES 4 A 539 GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL
SEQRES 5 A 539 ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA
SEQRES 6 A 539 HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU
SEQRES 7 A 539 ALA GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU
SEQRES 8 A 539 TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS
SEQRES 9 A 539 LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU
SEQRES 10 A 539 ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR
SEQRES 11 A 539 TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA
SEQRES 12 A 539 LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO
SEQRES 13 A 539 TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR
SEQRES 14 A 539 ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP
SEQRES 15 A 539 VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR
SEQRES 16 A 539 PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA
SEQRES 17 A 539 ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS
SEQRES 18 A 539 GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP
SEQRES 19 A 539 SER ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR
SEQRES 20 A 539 VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE
SEQRES 21 A 539 VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO
SEQRES 22 A 539 ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU
SEQRES 23 A 539 LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS
SEQRES 24 A 539 PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU
SEQRES 25 A 539 LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN
SEQRES 26 A 539 ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET
SEQRES 27 A 539 SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN
SEQRES 28 A 539 ALA ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS
SEQRES 29 A 539 ASP ALA GLN THR ASN ALA ALA ALA GLU PHE ASP ASP VAL
SEQRES 30 A 539 MET THR LYS GLU GLU GLN ILE PHE LEU LEU HIS ARG ALA
SEQRES 31 A 539 GLN ALA GLN CYS GLU LYS ARG LEU LYS GLU VAL LEU GLN
SEQRES 32 A 539 ARG PRO ALA SER ILE MET GLU SER ASP LYS GLY TRP THR
SEQRES 33 A 539 SER ALA SER THR SER GLY LYS PRO ARG LYS ASP LYS ALA
SEQRES 34 A 539 SER GLY LYS LEU TYR PRO GLU SER GLU GLU ASP LYS GLU
SEQRES 35 A 539 ALA PRO THR GLY SER ARG TYR ARG GLY ARG PRO CYS LEU
SEQRES 36 A 539 PRO GLU TRP ASP HIS ILE LEU CYS TRP PRO LEU GLY ALA
SEQRES 37 A 539 PRO GLY GLU VAL VAL ALA VAL PRO CYS PRO ASP TYR ILE
SEQRES 38 A 539 TYR ASP PHE ASN HIS LYS GLY HIS ALA TYR ARG ARG CYS
SEQRES 39 A 539 ASP ARG ASN GLY SER TRP GLU LEU VAL PRO GLY HIS ASN
SEQRES 40 A 539 ARG THR TRP ALA ASN TYR SER GLU CYS VAL LYS PHE LEU
SEQRES 41 A 539 THR ASN GLU THR ARG GLU ARG GLU VAL PHE ASP ARG LEU
SEQRES 42 A 539 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 24 GLY LYS SER ILE GLN ASP LEU ARG ARG ARG PHE PHE LEU
SEQRES 2 B 24 HIS HIS LEU ILE ALA GLU ILE HIS THR ALA NH2
HET NH2 B 35 1
HET GLC C 1 12
HET GLC C 2 11
HETNAM NH2 AMINO GROUP
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 NH2 H2 N
FORMUL 3 GLC 2(C6 H12 O6)
FORMUL 4 HOH *237(H2 O)
HELIX 1 1 GLY A -328 GLY A -312 1 17
HELIX 2 2 LYS A -302 ALA A -293 1 10
HELIX 3 3 ARG A -278 SER A -271 1 8
HELIX 4 4 ASP A -262 ASP A -257 1 6
HELIX 5 5 TYR A -254 VAL A -247 1 8
HELIX 6 6 THR A -216 GLU A -214 5 3
HELIX 7 7 GLU A -213 ALA A -203 1 11
HELIX 8 8 GLU A -191 ASP A -180 1 12
HELIX 9 9 ASN A -159 ASN A -143 1 17
HELIX 10 10 ASP A -135 LYS A -125 1 11
HELIX 11 11 GLY A -116 TRP A -114 5 3
HELIX 12 12 ALA A -113 LYS A -105 1 9
HELIX 13 13 ASN A -72 TYR A -61 1 12
HELIX 14 14 THR A -58 LYS A -47 1 12
HELIX 15 15 LEU A -40 ALA A -32 1 9
HELIX 16 16 ASP A -30 GLY A -17 1 14
HELIX 17 17 GLN A -9 SER A 8 1 18
HELIX 18 18 THR A 12 ALA A 25 1 14
HELIX 19 19 THR A 33 LEU A 56 1 24
HELIX 20 20 SER B 14 HIS B 32 1 19
SHEET 1 A 6 VAL A-309 GLU A-306 0
SHEET 2 A 6 LEU A-337 TRP A-334 1 N ILE A-335 O GLU A-306
SHEET 3 A 6 ILE A-285 ALA A-281 1 O ILE A-285 N TRP A-334
SHEET 4 A 6 PHE A -86 ILE A -78 -1 O SER A -81 N TRP A-282
SHEET 5 A 6 TYR A-238 GLU A-233 -1 N ILE A-236 O LEU A -82
SHEET 6 A 6 ALA A -43 VAL A -42 -1 O ALA A -43 N VAL A-234
SHEET 1 B 5 VAL A-309 GLU A-306 0
SHEET 2 B 5 LEU A-337 TRP A-334 1 N ILE A-335 O GLU A-306
SHEET 3 B 5 ILE A-285 ALA A-281 1 O ILE A-285 N TRP A-334
SHEET 4 B 5 PHE A -86 ILE A -78 -1 O SER A -81 N TRP A-282
SHEET 5 B 5 GLU A -16 ILE A -15 1 O GLU A -16 N VAL A -85
SHEET 1 C 2 ARG A-246 TYR A-245 0
SHEET 2 C 2 LYS A-242 LEU A-241 -1 O LYS A-242 N TYR A-245
SHEET 1 D 4 SER A-199 LEU A-197 0
SHEET 2 D 4 THR A-122 ASN A-117 1 O ALA A-121 N SER A-199
SHEET 3 D 4 SER A-230 ASN A-226 -1 N ASN A-226 O ALA A-121
SHEET 4 D 4 TYR A-102 THR A -99 -1 O THR A -99 N LEU A-229
SHEET 1 E 2 TYR A-177 GLU A-172 0
SHEET 2 E 2 LYS A-169 GLY A-162 -1 O LYS A-169 N GLU A-172
SHEET 1 F 2 GLU A 111 TRP A 112 0
SHEET 2 F 2 CYS A 117 TRP A 118 -1 O TRP A 118 N GLU A 111
SHEET 1 G 2 VAL A 126 PRO A 130 0
SHEET 2 G 2 HIS A 143 ARG A 147 -1 O ALA A 144 N VAL A 129
SSBOND 1 CYS A 48 CYS A 117 1555 1555 2.09
SSBOND 2 CYS A 108 CYS A 148 1555 1555 2.05
SSBOND 3 CYS A 131 CYS A 170 1555 1555 2.05
LINK C ALA B 34 N NH2 B 35 1555 1555 1.33
LINK O4 GLC C 1 C1 GLC C 2 1555 1555 1.42
CRYST1 84.041 84.041 164.455 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011899 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011899 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006081 0.00000
(ATOM LINES ARE NOT SHOWN.)
END