Header list of 1l3h.pdb file
Complete list - b 23 2 Bytes
HEADER IMMUNE SYSTEM 27-FEB-02 1L3H
TITLE NMR STRUCTURE OF P41ICF, A POTENT INHIBITOR OF HUMAN CATHEPSIN L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS II-ASSOCIATED P41 INVARIANT CHAIN FRAGMENT
COMPND 3 (P41ICF);
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: THYROGLOBULIN-LIKE DOMAIN;
COMPND 6 SYNONYM: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, GAMMA CHAIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS ALPHA HELIX, BETA SHEET, DISULFIDE BONDS, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR C.CHIVA,P.BARTHE,A.CODINA,E.GIRALT
REVDAT 3 23-FEB-22 1L3H 1 REMARK
REVDAT 2 24-FEB-09 1L3H 1 VERSN
REVDAT 1 04-MAR-03 1L3H 0
JRNL AUTH C.CHIVA,P.BARTHE,A.CODINA,M.GAIRI,F.MOLINA,C.GRANIER,
JRNL AUTH 2 M.PUGNIERE,T.INUI,H.NISHIO,Y.NISHIUCHI,T.KIMURA,
JRNL AUTH 3 S.SAKAKIBARA,F.ALBERICIO,E.GIRALT
JRNL TITL SYNTHESIS AND NMR STRUCTURE OF P41ICF, A POTENT INHIBITOR OF
JRNL TITL 2 HUMAN CATHEPSIN L
JRNL REF J.AM.CHEM.SOC. V. 125 1508 2003
JRNL REFN ISSN 0002-7863
JRNL PMID 12568610
JRNL DOI 10.1021/JA0207908
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, AMBER 5.0
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 981 RESTRAINTS, 925 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 56
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1L3H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015607.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM P41ICF; 20MM PHOSPHATE
REMARK 210 BUFFER, 0.01MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING WITH
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 600
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: CLOSE CONTACTS
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 HG1 THR A 2 O GLY A 27 1.49
REMARK 500 O GLN A 5 HG SER A 9 1.54
REMARK 500 O SER A 18 HG SER A 37 1.56
REMARK 500 OD1 ASN A 47 HG1 THR A 49 1.57
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 57 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 TYR A 35 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 9 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 11 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 14 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 15 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 17 TYR A 35 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 19 ARG A 55 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 20 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 22 TYR A 35 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 22 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 24 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 25 TYR A 40 CB - CG - CD2 ANGL. DEV. = -4.0 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 1 VAL A 14 47.62 -73.92
REMARK 500 1 PRO A 31 -8.53 -51.25
REMARK 500 1 ARG A 55 103.81 -51.69
REMARK 500 1 SER A 63 33.17 -65.81
REMARK 500 1 GLU A 64 4.08 -61.64
REMARK 500 2 PRO A 52 18.82 -69.15
REMARK 500 2 ARG A 55 94.27 -56.77
REMARK 500 2 ARG A 57 1.13 -63.56
REMARK 500 2 SER A 63 62.99 -167.58
REMARK 500 3 PRO A 52 23.20 -70.15
REMARK 500 3 ARG A 55 102.84 -45.54
REMARK 500 3 ASN A 61 49.55 -76.29
REMARK 500 3 CYS A 62 107.87 -56.10
REMARK 500 3 GLU A 64 23.69 -69.63
REMARK 500 4 LYS A 3 -62.14 -21.62
REMARK 500 4 HIS A 15 61.79 -116.40
REMARK 500 4 ASN A 53 -5.02 65.11
REMARK 500 4 ARG A 55 91.89 -60.95
REMARK 500 4 ASN A 61 61.68 -112.11
REMARK 500 4 CYS A 62 106.66 -52.24
REMARK 500 4 SER A 63 25.39 47.22
REMARK 500 5 ARG A 55 106.08 -59.89
REMARK 500 5 ARG A 57 1.50 -65.50
REMARK 500 6 PRO A 31 -9.09 -54.45
REMARK 500 6 ASN A 53 6.63 59.73
REMARK 500 6 ARG A 55 109.21 -42.42
REMARK 500 6 GLU A 64 68.90 -62.63
REMARK 500 7 PRO A 31 -18.76 -48.21
REMARK 500 7 ASN A 53 -0.47 61.22
REMARK 500 7 ARG A 55 95.22 -43.57
REMARK 500 7 SER A 63 18.30 -64.96
REMARK 500 8 HIS A 15 70.87 -111.03
REMARK 500 8 ASN A 53 -0.82 65.18
REMARK 500 8 ARG A 55 98.82 -56.44
REMARK 500 8 CYS A 62 -172.64 -65.32
REMARK 500 8 SER A 63 51.63 -64.70
REMARK 500 8 GLU A 64 32.84 -69.65
REMARK 500 9 HIS A 15 63.68 -111.41
REMARK 500 9 ASN A 53 -2.55 59.44
REMARK 500 9 ARG A 55 99.02 -46.16
REMARK 500 9 ARG A 57 23.33 -79.27
REMARK 500 9 GLU A 64 26.10 -75.34
REMARK 500 10 HIS A 15 53.62 -114.86
REMARK 500 10 GLU A 25 0.15 -64.64
REMARK 500 10 ARG A 55 94.17 -62.83
REMARK 500 10 CYS A 62 105.73 -57.16
REMARK 500 10 SER A 63 19.31 54.29
REMARK 500 11 ARG A 55 103.02 -43.80
REMARK 500 11 ARG A 57 13.72 -69.07
REMARK 500 12 HIS A 15 63.19 -114.36
REMARK 500
REMARK 500 THIS ENTRY HAS 129 RAMACHANDRAN OUTLIERS.
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 14 TYR A 35 0.07 SIDE CHAIN
REMARK 500 18 ARG A 20 0.08 SIDE CHAIN
REMARK 500 23 TYR A 35 0.11 SIDE CHAIN
REMARK 500 27 TYR A 29 0.08 SIDE CHAIN
REMARK 500 29 ARG A 55 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ICF RELATED DB: PDB
REMARK 900 1ICF CONTAINS THE SAME PROTEIN COMPLEXED WITH CATHEPSIN L.
DBREF 1L3H A 1 65 UNP P04233 HG2A_HUMAN 210 274
SEQRES 1 A 65 LEU THR LYS CYS GLN GLU GLU VAL SER HIS ILE PRO ALA
SEQRES 2 A 65 VAL HIS PRO GLY SER PHE ARG PRO LYS CYS ASP GLU ASN
SEQRES 3 A 65 GLY ASN TYR LEU PRO LEU GLN CYS TYR GLY SER ILE GLY
SEQRES 4 A 65 TYR CYS TRP CYS VAL PHE PRO ASN GLY THR GLU VAL PRO
SEQRES 5 A 65 ASN THR ARG SER ARG GLY HIS HIS ASN CYS SER GLU SER
HELIX 1 1 THR A 2 ILE A 11 1 10
SHEET 1 A 2 LEU A 32 TYR A 35 0
SHEET 2 A 2 TYR A 40 CYS A 43 -1 O TRP A 42 N GLN A 33
SSBOND 1 CYS A 4 CYS A 23 1555 1555 2.03
SSBOND 2 CYS A 34 CYS A 41 1555 1555 2.05
SSBOND 3 CYS A 43 CYS A 62 1555 1555 2.03
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 23 2 Bytes