Header list of 2glh.pdb file
Complete list - r 9 2 Bytes
HEADER HORMONE/GROWTH FACTOR 04-APR-06 2GLH
TITLE SOLUTION CONFORMATION OF SALMON CALCITONIN IN SODIUM DODECYL SULFATE
TITLE 2 MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCITONIN-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: PEPTIDE SYNTHESIS
KEYWDS A-HELIX, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 100
AUTHOR G.ANDREOTTI,B.LOPEZ-MENDEZ,P.AMODEO,M.A.MORELLI,H.NAKAMUTA,A.MOTTA
REVDAT 4 09-MAR-22 2GLH 1 REMARK LINK
REVDAT 3 24-FEB-09 2GLH 1 VERSN
REVDAT 2 05-SEP-06 2GLH 1 JRNL
REVDAT 1 20-JUN-06 2GLH 0
JRNL AUTH G.ANDREOTTI,B.L.MENDEZ,P.AMODEO,M.A.MORELLI,H.NAKAMUTA,
JRNL AUTH 2 A.MOTTA
JRNL TITL STRUCTURAL DETERMINANTS OF SALMON CALCITONIN BIOACTIVITY:
JRNL TITL 2 THE ROLE OF THE LEU-BASED AMPHIPATHIC ALPHA-HELIX.
JRNL REF J.BIOL.CHEM. V. 281 24193 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16766525
JRNL DOI 10.1074/JBC.M603528200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.AMODEO,A.MOTTA,G.STRAZZULLO,M.A.CASTIGLIONE-MORELLI
REMARK 1 TITL CONFORMATIONAL FLEXIBILITY IN CALCITONIN: THE DYNAMIC
REMARK 1 TITL 2 PROPERTIES OF HUMAN AND SALMON CALCITONIN IN SOLUTION
REMARK 1 REF J.BIOMOL.NMR V. 13 161 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008365322148
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.MOTTA,A.PASTORE,N.A.GOUD,M.A.CASTIGLIONE-MORELLI
REMARK 1 TITL SOLUTION CONFORMATION OF SALMON CALCITONIN IN SODIUM DODECYL
REMARK 1 TITL 2 SULFATE MICELLES AS DETERMINED BY TWO-DIMENSIONAL NMR AND
REMARK 1 TITL 3 DISTANCE GEOMETRY CALCULATIONS
REMARK 1 REF BIOCHEMISTRY V. 30 10444 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 6.0
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GLH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037266.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 310
REMARK 210 PH : 4.1; 7.2
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 5 MM SCT; 20 MM PHOSPHATE
REMARK 210 BUFFER; 600 MM SDS; 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA, AMBER 6.0
REMARK 210 METHOD USED : RESTRAINED SIMULATED
REMARK 210 ANNEALING/ENERGY MINIMIZATION
REMARK 210 FOLLOWED BY UNRESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 100
REMARK 210 CONFORMERS, SELECTION CRITERIA : PERIODICALLY SAMPLED
REMARK 210 UNRESTRAINED MOLECULAR DYNAMICS
REMARK 210 STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 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 7 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 8 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 13 TYR A 22 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 14 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 18 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 19 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 20 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 21 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 41 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 44 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 45 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 46 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 54 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 67 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 78 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 85 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 87 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 93 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 00 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.6 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 SER A 2 -75.84 -118.03
REMARK 500 1 LEU A 4 -76.91 -32.76
REMARK 500 1 THR A 25 113.75 166.70
REMARK 500 1 SER A 29 48.13 -154.05
REMARK 500 2 LEU A 4 -73.76 -38.23
REMARK 500 2 THR A 25 132.46 149.83
REMARK 500 2 SER A 29 18.69 -61.80
REMARK 500 4 ASN A 26 -30.60 -147.39
REMARK 500 5 SER A 2 -60.31 -100.38
REMARK 500 5 PRO A 23 3.79 -64.30
REMARK 500 5 THR A 25 143.14 -177.94
REMARK 500 5 ASN A 26 -45.39 -148.18
REMARK 500 6 SER A 2 -80.43 -99.73
REMARK 500 6 TYR A 22 -56.53 -29.67
REMARK 500 6 ASN A 26 -47.84 -149.48
REMARK 500 7 SER A 2 -77.56 -91.06
REMARK 500 7 TYR A 22 -70.14 -25.82
REMARK 500 7 PRO A 23 1.55 -60.80
REMARK 500 7 THR A 25 136.13 -171.16
REMARK 500 7 ASN A 26 -12.26 -141.90
REMARK 500 7 SER A 29 101.35 -59.33
REMARK 500 8 SER A 2 -79.78 -102.92
REMARK 500 8 TYR A 22 -69.83 -23.51
REMARK 500 8 PRO A 23 -7.44 -56.95
REMARK 500 8 THR A 25 146.50 -173.05
REMARK 500 8 ASN A 26 -44.69 -146.55
REMARK 500 9 LEU A 4 -77.11 -31.66
REMARK 500 9 TYR A 22 -65.32 -23.81
REMARK 500 9 ASN A 26 -14.23 -152.13
REMARK 500 9 THR A 27 -58.48 -134.13
REMARK 500 10 ASN A 26 -36.10 -149.68
REMARK 500 11 SER A 2 -95.57 -129.26
REMARK 500 11 THR A 25 110.54 -167.48
REMARK 500 11 THR A 27 -1.91 -149.85
REMARK 500 12 ARG A 24 -37.39 -137.06
REMARK 500 12 THR A 25 125.80 -178.17
REMARK 500 12 THR A 27 -41.52 -150.22
REMARK 500 13 ARG A 24 -37.85 -140.69
REMARK 500 13 THR A 25 98.87 172.55
REMARK 500 13 THR A 27 -60.25 -144.90
REMARK 500 14 SER A 2 -91.98 -111.21
REMARK 500 14 ARG A 24 -57.19 -125.36
REMARK 500 14 THR A 25 90.27 -171.44
REMARK 500 15 PRO A 23 4.54 -64.16
REMARK 500 15 ARG A 24 -35.14 -137.67
REMARK 500 15 THR A 25 98.63 155.31
REMARK 500 16 PRO A 23 7.06 -64.84
REMARK 500 16 ARG A 24 -37.14 -141.07
REMARK 500 16 THR A 25 98.45 163.21
REMARK 500 17 PRO A 23 0.19 -65.74
REMARK 500
REMARK 500 THIS ENTRY HAS 138 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 11 TYR A 22 0.07 SIDE CHAIN
REMARK 500 31 TYR A 22 0.07 SIDE CHAIN
REMARK 500 58 TYR A 22 0.07 SIDE CHAIN
REMARK 500 66 TYR A 22 0.06 SIDE CHAIN
REMARK 500 77 ARG A 24 0.09 SIDE CHAIN
REMARK 500 95 ARG A 24 0.09 SIDE CHAIN
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 NH2 A 33
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GLG RELATED DB: PDB
REMARK 900 [L23,A24]-SALMON CALCITONIN MUTANT
DBREF 2GLH A 1 32 UNP P01263 CALC1_ONCKE 83 114
SEQRES 1 A 33 CYS SER ASN LEU SER THR CYS VAL LEU GLY LYS LEU SER
SEQRES 2 A 33 GLN GLU LEU HIS LYS LEU GLN THR TYR PRO ARG THR ASN
SEQRES 3 A 33 THR GLY SER GLY THR PRO NH2
HET NH2 A 33 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 ASN A 3 TYR A 22 1 20
SSBOND 1 CYS A 1 CYS A 7 1555 1555 2.04
LINK C PRO A 32 N NH2 A 33 1555 1555 1.33
SITE 1 AC1 1 PRO A 32
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 2
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 - r 9 2 Bytes