Header list of 1df3.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSPORT PROTEIN 17-NOV-99 1DF3
TITLE SOLUTION STRUCTURE OF A RECOMBINANT MOUSE MAJOR URINARY PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR URINARY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MUP;
COMPND 5 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 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PHIL-D2
KEYWDS LIPOCALIN, CARRIER PROTEIN, PHEROMONE, 8-STRANDED BETA-BARREL,
KEYWDS 2 BINDING POCKET, DISULFIDE BRIDGE (64-157), SIGNALING PROTEIN,
KEYWDS 3 TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.LUECKE,L.FRANZONI,F.ABBATE,F.LOEHR,E.FERRARI,R.T.SORBI,
AUTHOR 2 H.RUETERJANS,A.SPISNI
REVDAT 4 16-FEB-22 1DF3 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1DF3 1 VERSN
REVDAT 2 01-APR-03 1DF3 1 JRNL
REVDAT 1 10-MAY-00 1DF3 0
JRNL AUTH C.LUCKE,L.FRANZONI,F.ABBATE,F.LOHR,E.FERRARI,R.T.SORBI,
JRNL AUTH 2 H.RUTERJANS,A.SPISNI
JRNL TITL SOLUTION STRUCTURE OF A RECOMBINANT MOUSE MAJOR URINARY
JRNL TITL 2 PROTEIN.
JRNL REF EUR.J.BIOCHEM. V. 266 1210 1999
JRNL REFN ISSN 0014-2956
JRNL PMID 10583419
JRNL DOI 10.1046/J.1432-1327.1999.00984.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.ABBATE,L.FRANZONI,F.LOEHR,C.LUECKE,E.FERRARI,R.T.SORBI,
REMARK 1 AUTH 2 H.RUETERJANS,A.SPISNI
REMARK 1 TITL LETTER TO THE EDITOR: COMPLETE 1H, 15N AND 13C ASSIGNMENT OF
REMARK 1 TITL 2 A RECOMBINANT MOUSE MAJOR URINARY PROTEIN
REMARK 1 REF J.BIOMOL.NMR V. 15 187 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008328813017
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.FERRARI,T.LODI,R.T.SORBI,R.TIRINDELLI,A.CAVAGGIONI,
REMARK 1 AUTH 2 A.SPISNI
REMARK 1 TITL EXPRESSION OF A LIPOCALIN IN PICHIA PASTORIS: SECRETION,
REMARK 1 TITL 2 PURIFICATION AND BINDING ACTIVITY OF A RECOMBINANT MOUSE
REMARK 1 TITL 3 MAJOR URINARY PROTEIN
REMARK 1 REF FEBS LETT. V. 401 73 1997
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(96)01436-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, DISCOVER 97
REMARK 3 AUTHORS : BRUKER (XWINNMR), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2432 DISTANCE RESTRAINTS (481 INTRARESIDUAL, 580 SEQUENTIAL, 410
REMARK 3 MEDIUM RANGE, 891 LONG RANGE AND 70 HYDROGEN BOND)
REMARK 4
REMARK 4 1DF3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000010030.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 10MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : UNIFORMLY 15N- AND 13C/15N
REMARK 210 -LABELLED RECOMBINANT MUP FROM
REMARK 210 MOUSE; 10MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HN(CO)CA, HNCO,
REMARK 210 (HCA)CO(CA)NH, HCACO; H(N)CA,CO,
REMARK 210 HNCACB, HBHA(CC)(CO)NH, CC(CO)NH-
REMARK 210 TOCSY; H(C)CH-TOCSY, (H)CB(CGC)
REMARK 210 CH-TOCSY, 3D_15N_EDITED_NOESY_
REMARK 210 HSQC; 3D_13C_EDITED_NOESY_HSQC,
REMARK 210 1H_15N_HSQC, 1H_13C_HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.5.9, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND RESTRAINED
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: SPIN-SYSTEM HETEROGENEITIES DETECTED
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 1 GLU A 1 CD GLU A 1 OE2 0.117
REMARK 500 1 GLU A 2 CD GLU A 2 OE2 0.116
REMARK 500 1 GLU A 13 CD GLU A 13 OE2 0.118
REMARK 500 1 GLU A 18 CD GLU A 18 OE2 0.118
REMARK 500 1 GLU A 30 CD GLU A 30 OE2 0.118
REMARK 500 1 GLU A 33 CD GLU A 33 OE2 0.117
REMARK 500 1 GLU A 43 CD GLU A 43 OE2 0.116
REMARK 500 1 GLU A 49 CD GLU A 49 OE2 0.116
REMARK 500 1 GLU A 62 CD GLU A 62 OE2 0.117
REMARK 500 1 GLU A 63 CD GLU A 63 OE2 0.117
REMARK 500 1 GLU A 66 CD GLU A 66 OE2 0.117
REMARK 500 1 GLU A 75 CD GLU A 75 OE2 0.117
REMARK 500 1 GLU A 79 CD GLU A 79 OE2 0.113
REMARK 500 1 GLU A 108 CD GLU A 108 OE2 0.117
REMARK 500 1 GLU A 112 CD GLU A 112 OE2 0.117
REMARK 500 1 GLU A 123 CD GLU A 123 OE2 0.117
REMARK 500 1 GLU A 132 CD GLU A 132 OE2 0.117
REMARK 500 1 GLU A 139 CD GLU A 139 OE2 0.117
REMARK 500 1 GLU A 140 CD GLU A 140 OE2 0.117
REMARK 500 1 GLU A 146 CD GLU A 146 OE2 0.116
REMARK 500 1 GLU A 162 CD GLU A 162 OE2 0.116
REMARK 500 1 GLU A 162 C GLU A 162 OXT 0.150
REMARK 500 2 GLU A 1 CD GLU A 1 OE2 0.117
REMARK 500 2 GLU A 2 CD GLU A 2 OE2 0.116
REMARK 500 2 GLU A 13 CD GLU A 13 OE2 0.116
REMARK 500 2 GLU A 18 CD GLU A 18 OE2 0.116
REMARK 500 2 GLU A 30 CD GLU A 30 OE2 0.117
REMARK 500 2 GLU A 33 CD GLU A 33 OE2 0.115
REMARK 500 2 GLU A 43 CD GLU A 43 OE2 0.117
REMARK 500 2 GLU A 49 CD GLU A 49 OE2 0.117
REMARK 500 2 GLU A 62 CD GLU A 62 OE2 0.116
REMARK 500 2 GLU A 63 CD GLU A 63 OE2 0.116
REMARK 500 2 GLU A 66 CD GLU A 66 OE2 0.117
REMARK 500 2 GLU A 75 CD GLU A 75 OE2 0.118
REMARK 500 2 GLU A 79 CD GLU A 79 OE2 0.118
REMARK 500 2 GLU A 108 CD GLU A 108 OE2 0.115
REMARK 500 2 GLU A 112 CD GLU A 112 OE2 0.116
REMARK 500 2 GLU A 123 CD GLU A 123 OE2 0.117
REMARK 500 2 GLU A 132 CD GLU A 132 OE2 0.116
REMARK 500 2 GLU A 139 CD GLU A 139 OE2 0.117
REMARK 500 2 GLU A 140 CD GLU A 140 OE2 0.117
REMARK 500 2 GLU A 146 CD GLU A 146 OE2 0.118
REMARK 500 2 GLU A 162 CD GLU A 162 OE2 0.117
REMARK 500 2 GLU A 162 C GLU A 162 OXT 0.151
REMARK 500 3 GLU A 1 CD GLU A 1 OE2 0.117
REMARK 500 3 GLU A 2 CD GLU A 2 OE2 0.117
REMARK 500 3 GLU A 13 CD GLU A 13 OE2 0.118
REMARK 500 3 GLU A 18 CD GLU A 18 OE2 0.117
REMARK 500 3 HIS A 20 CG HIS A 20 CD2 0.054
REMARK 500 3 GLU A 30 CD GLU A 30 OE2 0.117
REMARK 500
REMARK 500 THIS ENTRY HAS 227 BOND DEVIATIONS.
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 1 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 HIS A 20 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 1 ASP A 27 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ASP A 34 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 HIS A 46 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 HIS A 57 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 ARG A 60 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ASP A 72 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 ASP A 85 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 ASP A 96 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 1 ASP A 98 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 HIS A 104 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 1 ASP A 110 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ASP A 125 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ASP A 129 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 HIS A 141 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ASP A 150 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 ASP A 150 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 161 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 HIS A 20 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 2 ASP A 27 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ASP A 34 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 HIS A 46 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 2 HIS A 57 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 2 ARG A 60 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ASP A 72 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ASP A 85 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ASP A 96 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ASP A 98 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 HIS A 104 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ASP A 110 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ARG A 122 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ASP A 125 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ASP A 129 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 HIS A 141 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 2 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 161 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 260 ANGLE DEVIATIONS.
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 1 ARG A 8 -65.63 76.02
REMARK 500 1 ILE A 15 26.31 -79.37
REMARK 500 1 GLU A 30 -36.09 -142.13
REMARK 500 1 PHE A 38 49.59 -104.84
REMARK 500 1 LYS A 50 -59.71 157.49
REMARK 500 1 GLU A 62 -14.62 74.28
REMARK 500 1 LYS A 76 168.83 69.15
REMARK 500 1 ALA A 77 95.46 -64.50
REMARK 500 1 ASP A 98 -51.85 -168.33
REMARK 500 1 ASN A 153 -45.88 -178.57
REMARK 500 2 THR A 6 -41.37 -162.13
REMARK 500 2 ARG A 8 64.52 -110.42
REMARK 500 2 ASN A 9 66.71 -156.10
REMARK 500 2 ARG A 29 -54.04 81.57
REMARK 500 2 PHE A 38 67.35 -119.34
REMARK 500 2 GLU A 43 -62.96 -92.87
REMARK 500 2 LYS A 50 -43.59 102.93
REMARK 500 2 ARG A 60 78.58 -115.89
REMARK 500 2 GLU A 62 -21.24 78.91
REMARK 500 2 LYS A 76 83.52 -155.62
REMARK 500 2 ALA A 77 -93.84 63.79
REMARK 500 2 THR A 83 -109.08 -84.32
REMARK 500 2 TYR A 84 93.14 55.94
REMARK 500 2 ASP A 98 -56.69 -172.01
REMARK 500 2 ASN A 99 -68.74 -94.79
REMARK 500 2 LYS A 109 -148.15 -136.96
REMARK 500 2 ASN A 153 -41.50 -179.24
REMARK 500 2 LEU A 158 -79.68 -156.03
REMARK 500 2 GLN A 159 103.02 65.13
REMARK 500 2 ALA A 160 -70.67 -137.13
REMARK 500 3 ASN A 9 -36.89 -160.67
REMARK 500 3 ARG A 29 -64.75 80.76
REMARK 500 3 PHE A 38 64.37 -114.66
REMARK 500 3 LEU A 42 115.12 67.75
REMARK 500 3 LYS A 50 -51.43 160.92
REMARK 500 3 ASP A 61 73.73 53.85
REMARK 500 3 GLU A 62 -22.61 77.55
REMARK 500 3 ALA A 77 -86.73 68.28
REMARK 500 3 TYR A 97 76.17 -62.59
REMARK 500 3 ASP A 98 -51.28 158.76
REMARK 500 3 SER A 152 56.05 35.81
REMARK 500 3 ALA A 154 -71.37 -77.83
REMARK 500 3 ARG A 156 107.90 -35.06
REMARK 500 3 CYS A 157 111.99 65.28
REMARK 500 4 THR A 6 45.93 -97.00
REMARK 500 4 ARG A 8 70.10 -100.51
REMARK 500 4 ASN A 9 78.45 60.55
REMARK 500 4 ILE A 15 35.47 -89.88
REMARK 500 4 ILE A 22 -61.76 -91.07
REMARK 500 4 ARG A 29 -62.63 81.58
REMARK 500
REMARK 500 THIS ENTRY HAS 157 RAMACHANDRAN OUTLIERS.
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 PHE A 90 THR A 91 2 147.44
REMARK 500 ALA A 154 ASN A 155 3 146.74
REMARK 500 CYS A 157 LEU A 158 5 148.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 4 TYR A 80 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MUP RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE
DBREF 1DF3 A 1 162 UNP P11589 MUP2_MOUSE 19 180
SEQADV 1DF3 GLN A 136 UNP P11589 LYS 154 CONFLICT
SEQRES 1 A 162 GLU GLU ALA SER SER THR GLY ARG ASN PHE ASN VAL GLU
SEQRES 2 A 162 LYS ILE ASN GLY GLU TRP HIS THR ILE ILE LEU ALA SER
SEQRES 3 A 162 ASP LYS ARG GLU LYS ILE GLU ASP ASN GLY ASN PHE ARG
SEQRES 4 A 162 LEU PHE LEU GLU GLN ILE HIS VAL LEU GLU LYS SER LEU
SEQRES 5 A 162 VAL LEU LYS PHE HIS THR VAL ARG ASP GLU GLU CYS SER
SEQRES 6 A 162 GLU LEU SER MET VAL ALA ASP LYS THR GLU LYS ALA GLY
SEQRES 7 A 162 GLU TYR SER VAL THR TYR ASP GLY PHE ASN THR PHE THR
SEQRES 8 A 162 ILE PRO LYS THR ASP TYR ASP ASN PHE LEU MET ALA HIS
SEQRES 9 A 162 LEU ILE ASN GLU LYS ASP GLY GLU THR PHE GLN LEU MET
SEQRES 10 A 162 GLY LEU TYR GLY ARG GLU PRO ASP LEU SER SER ASP ILE
SEQRES 11 A 162 LYS GLU ARG PHE ALA GLN LEU CYS GLU GLU HIS GLY ILE
SEQRES 12 A 162 LEU ARG GLU ASN ILE ILE ASP LEU SER ASN ALA ASN ARG
SEQRES 13 A 162 CYS LEU GLN ALA ARG GLU
HELIX 1 1 VAL A 12 ASN A 16 5 5
HELIX 2 2 SER A 127 GLY A 142 1 16
HELIX 3 3 LEU A 144 ILE A 148 5 5
SHEET 1 A 9 GLY A 17 GLU A 18 0
SHEET 2 A 9 GLN A 44 VAL A 47 -1 N ILE A 45 O GLY A 17
SHEET 3 A 9 SER A 51 ARG A 60 -1 O VAL A 53 N HIS A 46
SHEET 4 A 9 GLU A 63 GLU A 75 -1 O GLU A 63 N ARG A 60
SHEET 5 A 9 GLU A 79 VAL A 82 -1 O GLU A 79 N GLU A 75
SHEET 6 A 9 ASN A 88 THR A 95 -1 N ASN A 88 O VAL A 82
SHEET 7 A 9 PHE A 100 GLU A 108 -1 N MET A 102 O LYS A 94
SHEET 8 A 9 THR A 113 GLY A 121 -1 O PHE A 114 N ASN A 107
SHEET 9 A 9 HIS A 20 SER A 26 -1 N HIS A 20 O GLY A 121
SSBOND 1 CYS A 64 CYS A 157 1555 1555 2.00
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 16 2 Bytes