HEADER HORMONE/HORMONE RECEPTOR 13-MAY-10 3N06
TITLE A MUTANT HUMAN PROLACTIN RECEPTOR ANTAGONIST H27A IN COMPLEX WITH THE
TITLE 2 EXTRACELLULAR DOMAIN OF THE HUMAN PROLACTIN RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLACTIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 43-227;
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: B;
COMPND 11 FRAGMENT: EXTRACELLULAR DOMAIN RESIDUES 26-234;
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: HPRL, PRL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7L;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: HPRLR, PRLR;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PH DEPENDENCE, HEMATOPOIETIC CYTOKINE, HORMONE-HORMONE RECEPTOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.V.KULKARNI,M.C.TETTAMANZI,J.W.MURPHY,C.KEELER,D.G.MYSZKA,
AUTHOR 2 N.E.CHAYEN,E.J.LOLIS,M.E.HODSDON
REVDAT 5 06-SEP-23 3N06 1 REMARK SEQADV LINK
REVDAT 4 08-NOV-17 3N06 1 REMARK
REVDAT 3 15-DEC-10 3N06 1 JRNL
REVDAT 2 20-OCT-10 3N06 1 JRNL
REVDAT 1 29-SEP-10 3N06 0
JRNL AUTH M.V.KULKARNI,M.C.TETTAMANZI,J.W.MURPHY,C.KEELER,D.G.MYSZKA,
JRNL AUTH 2 N.E.CHAYEN,E.J.LOLIS,M.E.HODSDON
JRNL TITL TWO INDEPENDENT HISTIDINES, ONE IN HUMAN PROLACTIN AND ONE
JRNL TITL 2 IN ITS RECEPTOR, ARE CRITICAL FOR PH-DEPENDENT RECEPTOR
JRNL TITL 3 RECOGNITION AND ACTIVATION.
JRNL REF J.BIOL.CHEM. V. 285 38524 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20889499
JRNL DOI 10.1074/JBC.M110.172072
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 40533
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2155
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2953
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 166
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3197
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.43000
REMARK 3 B22 (A**2) : -2.43000
REMARK 3 B33 (A**2) : 3.65000
REMARK 3 B12 (A**2) : -1.22000
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): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.004
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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 3N06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059213.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-09
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42787
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 17.50
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.30
REMARK 200 R MERGE FOR SHELL (I) : 0.94000
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: 3MZG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.6M NACL, 0.1 M HEPES 7.5,
REMARK 280 TEMPERATURE 291K, VAPOR DIFFUSION, HANGING DROP, PH 7.5
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 48.44333
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 24.22167
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 36.33250
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 12.11083
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 60.55417
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: 2900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 THR B 207
REMARK 465 MET B 208
REMARK 465 ASN B 209
REMARK 465 ASP B 210
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 142 CG CD CE NZ
REMARK 470 ASP B 118 CG OD1 OD2
REMARK 470 ARG B 119 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 120 CD CE NZ
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 45 -5.89 -140.07
REMARK 500 ARG A 48 176.44 173.20
REMARK 500 GLU A 107 46.64 -106.51
REMARK 500 THR A 141 125.59 -31.03
REMARK 500 ASN A 144 111.06 -166.84
REMARK 500 ASP A 160 104.92 -58.72
REMARK 500 ASN B 16 14.02 -148.69
REMARK 500 LYS B 17 15.12 59.36
REMARK 500 ASP B 29 43.07 73.84
REMARK 500 CYS B 51 127.12 -33.33
REMARK 500 ASP B 118 12.02 38.24
REMARK 500 LYS B 152 -9.85 77.89
REMARK 500 SER B 171 78.08 53.62
REMARK 500 ASP B 205 26.46 -71.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 211 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 276 O
REMARK 620 2 LYS B 66 O 100.4
REMARK 620 3 THR B 69 O 156.6 102.8
REMARK 620 4 HOH B 328 O 97.0 84.0 82.3
REMARK 620 5 HOH B 332 O 90.6 97.9 89.4 171.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 212 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 19 OG1
REMARK 620 2 THR B 21 OG1 140.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 214 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 54 O
REMARK 620 2 SER B 61 O 76.5
REMARK 620 3 HOH B 323 O 44.6 116.8
REMARK 620 4 HOH B 340 O 96.0 163.1 52.2
REMARK 620 5 HOH B 359 O 117.3 125.4 104.0 71.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 214
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MZG RELATED DB: PDB
REMARK 900 RELATED ID: 3N0P RELATED DB: PDB
DBREF 3N06 A 15 199 UNP P01236 PRL_HUMAN 43 227
DBREF 3N06 B 2 210 UNP P16471 PRLR_HUMAN 26 234
SEQADV 3N06 MET A 14 UNP P01236 INITIATING METHIONINE
SEQADV 3N06 ALA A 27 UNP P01236 HIS 55 ENGINEERED MUTATION
SEQADV 3N06 ARG A 129 UNP P01236 GLY 157 ENGINEERED MUTATION
SEQADV 3N06 MET B 1 UNP P16471 INITIATING METHIONINE
SEQRES 1 A 186 MET LEU ARG ASP LEU PHE ASP ARG ALA VAL VAL LEU SER
SEQRES 2 A 186 ALA TYR ILE HIS ASN LEU SER SER GLU MET PHE SER GLU
SEQRES 3 A 186 PHE ASP LYS ARG TYR THR HIS GLY ARG GLY PHE ILE THR
SEQRES 4 A 186 LYS ALA ILE ASN SER CYS HIS THR SER SER LEU ALA THR
SEQRES 5 A 186 PRO GLU ASP LYS GLU GLN ALA GLN GLN MET ASN GLN LYS
SEQRES 6 A 186 ASP PHE LEU SER LEU ILE VAL SER ILE LEU ARG SER TRP
SEQRES 7 A 186 ASN GLU PRO LEU TYR HIS LEU VAL THR GLU VAL ARG GLY
SEQRES 8 A 186 MET GLN GLU ALA PRO GLU ALA ILE LEU SER LYS ALA VAL
SEQRES 9 A 186 GLU ILE GLU GLU GLN THR LYS ARG LEU LEU GLU ARG MET
SEQRES 10 A 186 GLU LEU ILE VAL SER GLN VAL HIS PRO GLU THR LYS GLU
SEQRES 11 A 186 ASN GLU ILE TYR PRO VAL TRP SER GLY LEU PRO SER LEU
SEQRES 12 A 186 GLN MET ALA ASP GLU GLU SER ARG LEU SER ALA TYR TYR
SEQRES 13 A 186 ASN LEU LEU HIS CYS LEU ARG ARG ASP SER HIS LYS ILE
SEQRES 14 A 186 ASP ASN TYR LEU LYS LEU LEU LYS CYS ARG ILE ILE HIS
SEQRES 15 A 186 ASN ASN ASN CYS
SEQRES 1 B 210 MET LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS ARG
SEQRES 2 B 210 SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG PRO
SEQRES 3 B 210 GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU THR
SEQRES 4 B 210 TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS PRO
SEQRES 5 B 210 ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE GLY
SEQRES 6 B 210 LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET MET
SEQRES 7 B 210 VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER ASP
SEQRES 8 B 210 GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO ASP
SEQRES 9 B 210 PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO GLU
SEQRES 10 B 210 ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO PRO
SEQRES 11 B 210 THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU LEU
SEQRES 12 B 210 TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU TRP
SEQRES 13 B 210 GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS ILE
SEQRES 14 B 210 LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN VAL
SEQRES 15 B 210 ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP SER
SEQRES 16 B 210 PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR MET
SEQRES 17 B 210 ASN ASP
HET NA B 211 1
HET NA B 212 1
HET CL B 213 1
HET NA B 214 1
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 NA 3(NA 1+)
FORMUL 5 CL CL 1-
FORMUL 7 HOH *273(H2 O)
HELIX 1 1 MET A 14 THR A 45 1 32
HELIX 2 2 GLY A 49 ILE A 55 1 7
HELIX 3 3 ASP A 68 MET A 75 1 8
HELIX 4 4 ASN A 76 TRP A 91 1 16
HELIX 5 5 TRP A 91 GLY A 104 1 14
HELIX 6 6 PRO A 109 HIS A 138 1 30
HELIX 7 7 GLY A 152 MET A 158 1 7
HELIX 8 8 ASP A 160 ASN A 196 1 37
HELIX 9 9 GLY B 65 THR B 69 5 5
HELIX 10 10 ASP B 96 ILE B 100 5 5
SHEET 1 A 3 GLU B 8 ARG B 13 0
SHEET 2 A 3 PHE B 20 ARG B 25 -1 O ARG B 25 N GLU B 8
SHEET 3 A 3 SER B 61 PHE B 64 -1 O PHE B 64 N PHE B 20
SHEET 1 B 4 HIS B 49 GLU B 50 0
SHEET 2 B 4 ASN B 35 ARG B 42 -1 N TYR B 40 O HIS B 49
SHEET 3 B 4 TYR B 75 ASN B 83 -1 O ILE B 76 N HIS B 41
SHEET 4 B 4 GLY B 86 PHE B 89 -1 O SER B 88 N ALA B 81
SHEET 1 C 4 HIS B 49 GLU B 50 0
SHEET 2 C 4 ASN B 35 ARG B 42 -1 N TYR B 40 O HIS B 49
SHEET 3 C 4 TYR B 75 ASN B 83 -1 O ILE B 76 N HIS B 41
SHEET 4 C 4 LEU B 93 VAL B 95 -1 O LEU B 93 N MET B 77
SHEET 1 D 3 LEU B 107 LYS B 114 0
SHEET 2 D 3 TYR B 122 SER B 128 -1 O TYR B 122 N LYS B 114
SHEET 3 D 3 GLU B 166 ILE B 169 -1 O ILE B 169 N LEU B 123
SHEET 1 E 4 GLU B 157 GLY B 162 0
SHEET 2 E 4 LEU B 142 LYS B 149 -1 N ILE B 146 O HIS B 159
SHEET 3 E 4 LYS B 177 PRO B 186 -1 O GLN B 181 N ARG B 147
SHEET 4 E 4 THR B 198 GLN B 201 -1 O THR B 198 N VAL B 180
SSBOND 1 CYS A 58 CYS A 174 1555 1555 2.05
SSBOND 2 CYS A 191 CYS A 199 1555 1555 2.05
SSBOND 3 CYS B 12 CYS B 22 1555 1555 1.98
SSBOND 4 CYS B 51 CYS B 62 1555 1555 2.11
LINK O HOH A 276 NA NA B 211 1555 1555 2.31
LINK OG1 THR B 19 NA NA B 212 1555 1555 3.09
LINK OG1 THR B 21 NA NA B 212 1555 1555 3.11
LINK O TYR B 54 NA NA B 214 1555 1555 3.19
LINK O SER B 61 NA NA B 214 1555 1555 2.86
LINK O LYS B 66 NA NA B 211 1555 1555 2.25
LINK O THR B 69 NA NA B 211 1555 1555 2.22
LINK NA NA B 211 O HOH B 328 1555 1555 2.48
LINK NA NA B 211 O HOH B 332 1555 1555 2.42
LINK NA NA B 214 O HOH B 323 1555 1555 2.01
LINK NA NA B 214 O HOH B 340 1555 1555 3.07
LINK NA NA B 214 O HOH B 359 1555 1555 3.08
SITE 1 AC1 5 HOH A 276 LYS B 66 THR B 69 HOH B 328
SITE 2 AC1 5 HOH B 332
SITE 1 AC2 5 PRO B 15 THR B 19 PHE B 20 THR B 21
SITE 2 AC2 5 HIS B 63
SITE 1 AC3 1 TRP B 191
SITE 1 AC4 8 TRP B 24 TYR B 54 GLY B 58 ASN B 60
SITE 2 AC4 8 SER B 61 HOH B 323 HOH B 340 HOH B 359
CRYST1 123.419 123.419 72.665 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 0.008102 0.004678 0.000000 0.00000
SCALE2 0.000000 0.009356 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013762 0.00000
(ATOM LINES ARE NOT SHOWN.)
END