HEADER TRANSPORT PROTEIN 09-SEP-03 1QY0
TITLE THERMODYNAMICS OF BINDING OF 2-METHOXY-3-ISOPROPYLPYRAZINE AND 2-
TITLE 2 METHOXY-3-ISOBUTYLPYRAZINE TO THE MAJOR URINARY PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR URINARY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: SWISS;
SOURCE 6 GENE: MUP1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SG13009;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS LIPOCALIN, BETA-BARREL, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.BINGHAM,J.B.C.FINDLAY,S.-Y.HSIEH,A.P.KALVERDA,A.KJELLBERG,
AUTHOR 2 C.PERAZZOLO,S.E.V.PHILLIPS,K.SESHADRI,C.H.TRINH,W.B.TURNBULL,
AUTHOR 3 G.BODENHAUSEN,S.W.HOMANS
REVDAT 5 23-AUG-23 1QY0 1 REMARK SEQADV LINK
REVDAT 4 16-NOV-11 1QY0 1 HETATM
REVDAT 3 13-JUL-11 1QY0 1 VERSN
REVDAT 2 24-FEB-09 1QY0 1 VERSN
REVDAT 1 24-FEB-04 1QY0 0
JRNL AUTH R.J.BINGHAM,J.B.C.FINDLAY,S.-Y.HSIEH,A.P.KALVERDA,
JRNL AUTH 2 A.KJELLBERG,C.PERAZZOLO,S.E.V.PHILLIPS,K.SESHADRI,C.H.TRINH,
JRNL AUTH 3 W.B.TURNBULL,G.BODENHAUSEN,S.W.HOMANS
JRNL TITL THERMODYNAMICS OF BINDING OF 2-METHOXY-3-ISOPROPYLPYRAZINE
JRNL TITL 2 AND 2-METHOXY-3-ISOBUTYLPYRAZINE TO THE MAJOR URINARY
JRNL TITL 3 PROTEIN.
JRNL REF J.AM.CHEM.SOC. V. 126 1675 2004
JRNL REFN ISSN 0002-7863
JRNL PMID 14871097
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 18006
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 SET) : 0.177
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 921
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 97
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1272
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 208
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.80000
REMARK 3 B22 (A**2) : -3.80000
REMARK 3 B33 (A**2) : 7.60000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 1.760
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.060
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QY0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.49
REMARK 200 MONOCHROMATOR : LIQUID GALLIUM COOLED, BENT,
REMARK 200 TRIANGULAR, SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18006
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.23000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1I06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CADMIUM CHLORIDE, MALATE/HCL, PH 4.9,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 68.50400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 26.81350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 26.81350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 102.75600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 26.81350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 26.81350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.25200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 26.81350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.81350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 102.75600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 26.81350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.81350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.25200
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 68.50400
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 611 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 612 LIES ON A SPECIAL POSITION.
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 -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 LEU A 158
REMARK 465 GLN A 159
REMARK 465 ALA A 160
REMARK 465 ARG A 161
REMARK 465 GLU A 162
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 74 -168.04 -105.13
REMARK 500 TYR A 84 116.12 -166.18
REMARK 500 TYR A 97 -43.17 67.19
REMARK 500 ASN A 99 -54.78 -125.46
REMARK 500 ALA A 154 18.02 -155.30
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 CD A 201 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 13 OE2
REMARK 620 2 GLU A 13 OE1 55.0
REMARK 620 3 ASP A 110 OD2 82.3 118.3
REMARK 620 4 HOH A 438 O 115.4 84.3 76.1
REMARK 620 5 HOH A 494 O 132.9 84.8 143.5 78.9
REMARK 620 6 HOH A 517 O 154.8 142.4 95.1 87.9 57.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 200 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 18 OE2
REMARK 620 2 GLU A 18 OE1 54.7
REMARK 620 3 GLU A 139 OE1 164.0 140.3
REMARK 620 4 GLU A 139 OE2 141.8 87.2 53.2
REMARK 620 5 HOH A 423 O 92.1 89.0 83.7 83.6
REMARK 620 6 HOH A 516 O 82.2 136.9 82.5 135.8 92.0
REMARK 620 7 HOH A 542 O 91.4 80.7 96.7 84.2 164.4 103.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 30 OE1
REMARK 620 2 GLU A 30 OE2 46.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 204 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 125 OD2
REMARK 620 2 HOH A 463 O 104.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 203 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 140 OE2
REMARK 620 2 HOH A 459 O 106.0
REMARK 620 3 HOH A 512 O 151.9 89.6
REMARK 620 4 HOH A 555 O 86.3 74.8 120.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QY1 RELATED DB: PDB
REMARK 900 RELATED ID: 1QY2 RELATED DB: PDB
DBREF 1QY0 A 1 162 UNP P11588 MUP1_MOUSE 19 180
SEQADV 1QY0 MET A -11 UNP P11588 CLONING ARTIFACT
SEQADV 1QY0 ARG A -10 UNP P11588 CLONING ARTIFACT
SEQADV 1QY0 GLY A -9 UNP P11588 CLONING ARTIFACT
SEQADV 1QY0 SER A 4 UNP P11588 CLONING ARTIFACT
SEQADV 1QY0 HIS A -7 UNP P11588 EXPRESSION TAG
SEQADV 1QY0 HIS A -6 UNP P11588 EXPRESSION TAG
SEQADV 1QY0 HIS A -5 UNP P11588 EXPRESSION TAG
SEQADV 1QY0 HIS A -4 UNP P11588 EXPRESSION TAG
SEQADV 1QY0 HIS A -3 UNP P11588 EXPRESSION TAG
SEQADV 1QY0 HIS A -2 UNP P11588 EXPRESSION TAG
SEQADV 1QY0 GLY A -1 UNP P11588 CLONING ARTIFACT
SEQADV 1QY0 SER A 0 UNP P11588 CLONING ARTIFACT
SEQRES 1 A 174 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU
SEQRES 2 A 174 GLU ALA SER SER THR GLY ARG ASN PHE ASN VAL GLU LYS
SEQRES 3 A 174 ILE ASN GLY GLU TRP HIS THR ILE ILE LEU ALA SER ASP
SEQRES 4 A 174 LYS ARG GLU LYS ILE GLU ASP ASN GLY ASN PHE ARG LEU
SEQRES 5 A 174 PHE LEU GLU GLN ILE HIS VAL LEU GLU LYS SER LEU VAL
SEQRES 6 A 174 LEU LYS PHE HIS THR VAL ARG ASP GLU GLU CYS SER GLU
SEQRES 7 A 174 LEU SER MET VAL ALA ASP LYS THR GLU LYS ALA GLY GLU
SEQRES 8 A 174 TYR SER VAL THR TYR ASP GLY PHE ASN THR PHE THR ILE
SEQRES 9 A 174 PRO LYS THR ASP TYR ASP ASN PHE LEU MET ALA HIS LEU
SEQRES 10 A 174 ILE ASN GLU LYS ASP GLY GLU THR PHE GLN LEU MET GLY
SEQRES 11 A 174 LEU TYR GLY ARG GLU PRO ASP LEU SER SER ASP ILE LYS
SEQRES 12 A 174 GLU ARG PHE ALA GLN LEU CYS GLU GLU HIS GLY ILE LEU
SEQRES 13 A 174 ARG GLU ASN ILE ILE ASP LEU SER ASN ALA ASN ARG CYS
SEQRES 14 A 174 LEU GLN ALA ARG GLU
HET CD A 200 1
HET CD A 201 1
HET NA A 202 1
HET NA A 203 1
HET NA A 204 1
HET GOL A 300 6
HETNAM CD CADMIUM ION
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CD 2(CD 2+)
FORMUL 4 NA 3(NA 1+)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *208(H2 O)
HELIX 1 1 ASN A 11 ASN A 16 5 6
HELIX 2 2 LYS A 28 GLU A 33 5 6
HELIX 3 3 SER A 127 GLU A 140 1 14
HELIX 4 4 LEU A 144 GLU A 146 5 3
SHEET 1 A10 GLY A 17 GLU A 18 0
SHEET 2 A10 PHE A 41 VAL A 47 -1 O ILE A 45 N GLY A 17
SHEET 3 A10 SER A 51 ARG A 60 -1 O VAL A 53 N HIS A 46
SHEET 4 A10 GLU A 63 LYS A 73 -1 O LEU A 67 N PHE A 56
SHEET 5 A10 TYR A 80 THR A 83 -1 O SER A 81 N ASP A 72
SHEET 6 A10 PHE A 87 THR A 95 -1 O PHE A 90 N TYR A 80
SHEET 7 A10 PHE A 100 LYS A 109 -1 O GLU A 108 N PHE A 87
SHEET 8 A10 GLU A 112 GLY A 121 -1 O LEU A 116 N LEU A 105
SHEET 9 A10 HIS A 20 SER A 26 -1 N ALA A 25 O MET A 117
SHEET 10 A10 ILE A 148 ASP A 150 -1 O ILE A 149 N LEU A 24
SSBOND 1 CYS A 64 CYS A 157 1555 1555 2.05
LINK OE2 GLU A 13 CD CD A 201 1555 1555 2.50
LINK OE1 GLU A 13 CD CD A 201 1555 1555 2.34
LINK OE2 GLU A 18 CD CD A 200 5645 1555 2.30
LINK OE1 GLU A 18 CD CD A 200 5645 1555 2.52
LINK OE1 GLU A 30 NA NA A 202 1555 1555 2.53
LINK OE2 GLU A 30 NA NA A 202 1555 1555 2.95
LINK OD2 ASP A 110 CD CD A 201 8675 1555 2.33
LINK OD2 ASP A 125 NA NA A 204 1555 1555 2.52
LINK OE1 GLU A 139 CD CD A 200 1555 1555 2.30
LINK OE2 GLU A 139 CD CD A 200 1555 1555 2.52
LINK OE2 GLU A 140 NA NA A 203 1555 1555 2.59
LINK CD CD A 200 O HOH A 423 1555 5645 2.38
LINK CD CD A 200 O HOH A 516 1555 1555 2.37
LINK CD CD A 200 O HOH A 542 1555 1555 2.44
LINK CD CD A 201 O HOH A 438 1555 8675 2.33
LINK CD CD A 201 O HOH A 494 1555 8675 3.08
LINK CD CD A 201 O HOH A 517 1555 8675 2.44
LINK NA NA A 203 O HOH A 459 1555 1555 2.53
LINK NA NA A 203 O HOH A 512 1555 1555 2.41
LINK NA NA A 203 O HOH A 555 1555 1555 2.37
LINK NA NA A 204 O HOH A 463 1555 1555 2.80
SITE 1 AC1 5 GLU A 18 GLU A 139 HOH A 423 HOH A 516
SITE 2 AC1 5 HOH A 542
SITE 1 AC2 5 GLU A 13 ASP A 110 HOH A 438 HOH A 494
SITE 2 AC2 5 HOH A 517
SITE 1 AC3 2 GLU A 30 GLU A 49
SITE 1 AC4 5 LYS A 76 GLU A 140 HOH A 459 HOH A 512
SITE 2 AC4 5 HOH A 555
SITE 1 AC5 5 LYS A 109 ASP A 110 ASP A 125 HOH A 463
SITE 2 AC5 5 HOH A 517
SITE 1 AC6 3 ALA A 103 LEU A 105 TYR A 120
CRYST1 53.627 53.627 137.008 90.00 90.00 90.00 P 43 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 0.018647 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018647 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007299 0.00000
(ATOM LINES ARE NOT SHOWN.)
END