HEADER HORMONE/HORMONE RECEPTOR 14-MAY-08 3D48
TITLE CRYSTAL STRUCTURE OF A PROLACTIN RECEPTOR ANTAGONIST BOUND TO THE
TITLE 2 EXTRACELLULAR DOMAIN OF THE PROLACTIN RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLACTIN;
COMPND 3 CHAIN: P;
COMPND 4 FRAGMENT: RESIDUES 12-199;
COMPND 5 SYNONYM: PRL;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROLACTIN RECEPTOR;
COMPND 10 CHAIN: R;
COMPND 11 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 12 SYNONYM: PRL-R;
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: PRL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32-A(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: PRLR;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PET39-B(+)
KEYWDS CYTOKINE-CYTOKINE RECEPTOR COMPLEX, FOUR-HELIX BUNDLE, GLYCOPROTEIN,
KEYWDS 2 HORMONE, LACTATION, SECRETED, ALTERNATIVE SPLICING, MEMBRANE,
KEYWDS 3 RECEPTOR, TRANSMEMBRANE, HORMONE-HORMONE RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.A.SVENSSON,J.BREINHOLT
REVDAT 6 01-NOV-23 3D48 1 REMARK
REVDAT 5 10-NOV-21 3D48 1 REMARK SEQADV
REVDAT 4 23-MAY-18 3D48 1 REMARK
REVDAT 3 24-FEB-09 3D48 1 VERSN
REVDAT 2 28-OCT-08 3D48 1 JRNL
REVDAT 1 03-JUN-08 3D48 0
JRNL AUTH L.A.SVENSSON,K.BONDENSGAARD,L.NORSKOV-LAURITSEN,
JRNL AUTH 2 L.CHRISTENSEN,P.BECKER,M.D.ANDERSEN,M.J.MALTESEN,K.D.RAND,
JRNL AUTH 3 J.BREINHOLT
JRNL TITL CRYSTAL STRUCTURE OF A PROLACTIN RECEPTOR ANTAGONIST BOUND
JRNL TITL 2 TO THE EXTRACELLULAR DOMAIN OF THE PROLACTIN RECEPTOR
JRNL REF J.BIOL.CHEM. V. 283 19085 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18467331
JRNL DOI 10.1074/JBC.M801202200
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.4.0066
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20629
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1088
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1501
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2945
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.48000
REMARK 3 B22 (A**2) : -2.48000
REMARK 3 B33 (A**2) : 3.73000
REMARK 3 B12 (A**2) : -1.24000
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): 0.335
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.289
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.222
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.863
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3040 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4121 ; 2.013 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 353 ; 8.690 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 139 ;35.912 ;23.885
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 522 ;22.244 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.394 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 446 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2281 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1813 ; 0.964 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2929 ; 1.782 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1227 ; 2.465 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1192 ; 4.035 ; 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: NULL
REMARK 4
REMARK 4 3D48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047571.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21797
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
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: FOR THE R CHAIN, PDB ENTRY 1BP3. FOR THE P CHAIN,
REMARK 200 A CORE OF A MODELER HOMOLOGY MODEL BASED ON PDB ENTRIES 1BP3,
REMARK 200 1F6F, 1RW5 AND 1N9D.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM CHLORIDE, 0.1M HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 46.54667
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 23.27333
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 34.91000
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 11.63667
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 58.18333
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: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, R
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 P 12
REMARK 465 ARG P 43
REMARK 465 TYR P 44
REMARK 465 THR P 45
REMARK 465 HIS P 46
REMARK 465 GLY P 47
REMARK 465 ARG P 48
REMARK 465 GLY P 104
REMARK 465 MET P 105
REMARK 465 GLN P 106
REMARK 465 GLU P 107
REMARK 465 ALA P 108
REMARK 465 PRO P 109
REMARK 465 GLU P 110
REMARK 465 HIS P 138
REMARK 465 PRO P 139
REMARK 465 GLU P 140
REMARK 465 THR P 141
REMARK 465 LYS P 142
REMARK 465 GLU P 143
REMARK 465 ASN P 144
REMARK 465 GLU P 145
REMARK 465 CYS P 199
REMARK 465 SER R 0
REMARK 465 GLN R 1
REMARK 465 GLN R 115
REMARK 465 PRO R 116
REMARK 465 GLU R 117
REMARK 465 ASP R 118
REMARK 465 ARG R 119
REMARK 465 LYS R 120
REMARK 465 LEU R 172
REMARK 465 HIS R 173
REMARK 465 ASP R 205
REMARK 465 PHE R 206
REMARK 465 THR R 207
REMARK 465 MET R 208
REMARK 465 ASN R 209
REMARK 465 ASP R 210
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 O ARG P 16 N LEU P 18 1.89
REMARK 500 O LEU R 2 ND2 ASN R 83 2.15
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 CYS R 184 CB CYS R 184 SG -0.113
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 LEU R 179 CA - CB - CG ANGL. DEV. = 14.2 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 ARG P 16 -118.27 -64.80
REMARK 500 ASP P 17 -43.33 12.77
REMARK 500 ASP P 41 93.74 -66.85
REMARK 500 SER P 90 -19.46 -48.07
REMARK 500 GLU P 93 -73.77 -57.04
REMARK 500 ASN P 197 60.97 62.55
REMARK 500 ASN R 16 22.09 -158.28
REMARK 500 LYS R 17 14.55 53.05
REMARK 500 THR R 28 125.36 -37.41
REMARK 500 ASP R 29 128.14 -28.45
REMARK 500 GLU R 45 136.58 158.45
REMARK 500 CYS R 51 124.37 -33.19
REMARK 500 ASP R 53 102.41 -166.11
REMARK 500 PRO R 59 132.21 -36.84
REMARK 500 ASP R 104 172.46 -54.41
REMARK 500 LEU R 109 107.24 -56.63
REMARK 500 PRO R 203 -168.93 -60.05
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 PRO R 4 GLY R 5 45.06
REMARK 500 GLY R 175 GLN R 176 -146.15
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 CO3 P 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 R 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 R 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 R 213
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BP3 RELATED DB: PDB
REMARK 900 RELATED ID: 1F6F RELATED DB: PDB
REMARK 900 RELATED ID: 1RW5 RELATED DB: PDB
REMARK 900 RELATED ID: 1N9D RELATED DB: PDB
REMARK 900 RELATED ID: 2Q98 RELATED DB: PDB
DBREF 3D48 P 12 199 UNP P01236 PRL_HUMAN 40 227
DBREF 3D48 R 1 210 UNP P16471 PRLR_HUMAN 25 234
SEQADV 3D48 SER P 12 UNP P01236 GLN 40 ENGINEERED MUTATION
SEQADV 3D48 ARG P 129 UNP P01236 GLY 157 ENGINEERED MUTATION
SEQADV 3D48 SER R 0 UNP P16471 EXPRESSION TAG
SEQRES 1 P 188 SER VAL THR LEU ARG ASP LEU PHE ASP ARG ALA VAL VAL
SEQRES 2 P 188 LEU SER HIS TYR ILE HIS ASN LEU SER SER GLU MET PHE
SEQRES 3 P 188 SER GLU PHE ASP LYS ARG TYR THR HIS GLY ARG GLY PHE
SEQRES 4 P 188 ILE THR LYS ALA ILE ASN SER CYS HIS THR SER SER LEU
SEQRES 5 P 188 ALA THR PRO GLU ASP LYS GLU GLN ALA GLN GLN MET ASN
SEQRES 6 P 188 GLN LYS ASP PHE LEU SER LEU ILE VAL SER ILE LEU ARG
SEQRES 7 P 188 SER TRP ASN GLU PRO LEU TYR HIS LEU VAL THR GLU VAL
SEQRES 8 P 188 ARG GLY MET GLN GLU ALA PRO GLU ALA ILE LEU SER LYS
SEQRES 9 P 188 ALA VAL GLU ILE GLU GLU GLN THR LYS ARG LEU LEU GLU
SEQRES 10 P 188 ARG MET GLU LEU ILE VAL SER GLN VAL HIS PRO GLU THR
SEQRES 11 P 188 LYS GLU ASN GLU ILE TYR PRO VAL TRP SER GLY LEU PRO
SEQRES 12 P 188 SER LEU GLN MET ALA ASP GLU GLU SER ARG LEU SER ALA
SEQRES 13 P 188 TYR TYR ASN LEU LEU HIS CYS LEU ARG ARG ASP SER HIS
SEQRES 14 P 188 LYS ILE ASP ASN TYR LEU LYS LEU LEU LYS CYS ARG ILE
SEQRES 15 P 188 ILE HIS ASN ASN ASN CYS
SEQRES 1 R 211 SER GLN LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS
SEQRES 2 R 211 ARG SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG
SEQRES 3 R 211 PRO GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU
SEQRES 4 R 211 THR TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS
SEQRES 5 R 211 PRO ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE
SEQRES 6 R 211 GLY LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET
SEQRES 7 R 211 MET VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER
SEQRES 8 R 211 ASP GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO
SEQRES 9 R 211 ASP PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO
SEQRES 10 R 211 GLU ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO
SEQRES 11 R 211 PRO THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU
SEQRES 12 R 211 LEU TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU
SEQRES 13 R 211 TRP GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS
SEQRES 14 R 211 ILE LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN
SEQRES 15 R 211 VAL ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP
SEQRES 16 R 211 SER PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR
SEQRES 17 R 211 MET ASN ASP
HET CO3 P 1 4
HET CO3 R 211 4
HET CO3 R 212 4
HET CO3 R 213 4
HETNAM CO3 CARBONATE ION
FORMUL 3 CO3 4(C O3 2-)
FORMUL 7 HOH *103(H2 O)
HELIX 1 1 THR P 14 ASP P 41 1 28
HELIX 2 2 PHE P 50 ILE P 55 1 6
HELIX 3 3 CYS P 58 LEU P 63 5 6
HELIX 4 4 ASP P 68 GLN P 73 1 6
HELIX 5 5 ASN P 76 ARG P 103 1 28
HELIX 6 6 ALA P 111 VAL P 137 1 27
HELIX 7 7 GLY P 152 GLN P 157 1 6
HELIX 8 8 ASP P 160 ILE P 194 1 35
HELIX 9 9 GLY R 65 THR R 69 5 5
HELIX 10 10 THR R 98 ILE R 100 5 3
SHEET 1 A 3 LYS R 6 ARG R 13 0
SHEET 2 A 3 PHE R 20 THR R 28 -1 O THR R 21 N ARG R 13
SHEET 3 A 3 SER R 61 PHE R 64 -1 O PHE R 64 N PHE R 20
SHEET 1 B 4 HIS R 49 GLU R 50 0
SHEET 2 B 4 ASN R 35 ARG R 42 -1 N TYR R 40 O HIS R 49
SHEET 3 B 4 THR R 74 ASN R 83 -1 O ASN R 80 N SER R 37
SHEET 4 B 4 GLY R 86 PHE R 89 -1 O GLY R 86 N ASN R 83
SHEET 1 C 4 HIS R 49 GLU R 50 0
SHEET 2 C 4 ASN R 35 ARG R 42 -1 N TYR R 40 O HIS R 49
SHEET 3 C 4 THR R 74 ASN R 83 -1 O ASN R 80 N SER R 37
SHEET 4 C 4 LEU R 93 ASP R 96 -1 O VAL R 95 N TYR R 75
SHEET 1 D 3 LEU R 107 GLU R 112 0
SHEET 2 D 3 LEU R 123 SER R 128 -1 O LYS R 126 N ALA R 110
SHEET 3 D 3 GLU R 166 ILE R 169 -1 O ILE R 169 N LEU R 123
SHEET 1 E 4 GLU R 157 GLY R 162 0
SHEET 2 E 4 LEU R 142 PRO R 150 -1 N ILE R 146 O HIS R 159
SHEET 3 E 4 LYS R 177 PRO R 186 -1 O GLN R 181 N ARG R 147
SHEET 4 E 4 THR R 198 GLN R 201 -1 O THR R 198 N VAL R 180
SSBOND 1 CYS P 58 CYS P 174 1555 1555 2.05
SSBOND 2 CYS R 12 CYS R 22 1555 1555 2.08
SSBOND 3 CYS R 51 CYS R 62 1555 1555 2.12
SITE 1 AC1 5 SER P 57 CYS P 58 HIS P 59 LEU P 171
SITE 2 AC1 5 CYS P 174
SITE 1 AC2 2 TYR R 190 TRP R 191
SITE 1 AC3 3 CYS R 12 ARG R 13 GLN R 102
SITE 1 AC4 5 THR R 39 TYR R 40 HIS R 41 ILE R 76
SITE 2 AC4 5 MET R 78
CRYST1 125.350 125.350 69.820 90.00 90.00 120.00 P 65 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 0.007980 0.004610 0.000000 0.00000
SCALE2 0.000000 0.009210 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END