Header list of 2h4b.pdb file
Complete list - r 9 2 Bytes
HEADER DE NOVO PROTEIN 24-MAY-06 2H4B
TITLE CIS-4-AMINOMETHYLPHENYLAZOBENZOIC ACID-AVIAN PANCREATIC POLYPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC HORMONE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PANCREATIC HORMONE, RESIDUES 1-9;
COMPND 5 SYNONYM: PANCREATIC POLYPEPTIDE, APP;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PANCREATIC HORMONE;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: PANCREATIC HORMONE, RESIDUES 11-34;
COMPND 11 SYNONYM: PANCREATIC POLYPEPTIDE, APP;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: PRODUCED BY SOLID PHASE PEPTIDE SYNTHESIS, DERIVED
SOURCE 4 FROM AVIAN PANCREATIC POLYPEPTIDE WITH 4-AMINOMETHYL-
SOURCE 5 PHENYLAZOBENZOIC ACID REPLACING RESIDUES 10-12;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: PRODUCED BY SOLID PHASE PEPTIDE SYNTHESIS, DERIVED
SOURCE 9 FROM AVIAN PANCREATIC POLYPEPTIDE
KEYWDS PHOTOSWITCH, FOLDING, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.JURT,A.AEMISSEGGER,P.GUENTERT,O.ZERBE,D.HILVERT
REVDAT 4 09-MAR-22 2H4B 1 REMARK LINK
REVDAT 3 24-FEB-09 2H4B 1 VERSN
REVDAT 2 03-OCT-06 2H4B 1 JRNL
REVDAT 1 12-SEP-06 2H4B 0
JRNL AUTH S.JURT,A.AEMISSEGGER,P.GUENTERT,O.ZERBE,D.HILVERT
JRNL TITL A PHOTOSWITCHABLE MINIPROTEIN BASED ON THE SEQUENCE OF AVIAN
JRNL TITL 2 PANCREATIC POLYPEPTIDE
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 45 6297 2006
JRNL REFN ESSN 0570-0833
JRNL PMID 16933352
JRNL DOI 10.1002/ANIE.200602084
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.2.2
REMARK 3 AUTHORS : GUENTERT, P. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H4B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037912.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 4.1
REMARK 210 IONIC STRENGTH : 0.0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE; 20MM ACETATE
REMARK 210 BUFFER(PH 4.1); 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.2.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
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
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 PRO A 2 -178.62 -65.60
REMARK 500 1 ARG D 33 46.45 -81.78
REMARK 500 2 SER A 3 -25.67 -149.66
REMARK 500 2 PRO A 5 40.63 -79.40
REMARK 500 2 THR A 6 4.73 -69.66
REMARK 500 2 HIS C 32 16.39 59.77
REMARK 500 2 SER B 3 -64.75 -123.66
REMARK 500 2 THR B 6 59.26 -141.09
REMARK 500 2 VAL D 29 -71.29 -54.14
REMARK 500 3 SER A 3 -62.60 -98.82
REMARK 500 3 SER B 3 -33.26 -133.36
REMARK 500 3 THR B 6 108.60 -57.91
REMARK 500 3 TYR D 25 -70.24 -55.06
REMARK 500 4 SER A 3 -70.41 -99.25
REMARK 500 4 HIS D 32 62.81 61.09
REMARK 500 5 SER A 3 -56.55 -141.58
REMARK 500 5 THR A 6 80.48 50.34
REMARK 500 5 HIS C 32 19.49 56.33
REMARK 500 5 SER B 3 -73.25 -150.53
REMARK 500 5 THR B 6 91.48 63.83
REMARK 500 6 SER A 3 -59.23 -130.58
REMARK 500 6 GLN A 4 50.88 -148.14
REMARK 500 6 GLN B 4 55.34 -155.18
REMARK 500 6 PRO B 5 -172.51 -66.20
REMARK 500 7 TYR A 7 78.62 48.03
REMARK 500 7 ARG C 31 49.49 38.49
REMARK 500 7 SER B 3 -55.04 -125.65
REMARK 500 7 TYR B 7 71.75 34.95
REMARK 500 8 GLN A 4 79.65 -163.96
REMARK 500 8 GLN B 4 74.64 -165.03
REMARK 500 8 THR B 6 97.89 -66.52
REMARK 500 8 ARG D 33 30.18 -73.18
REMARK 500 9 GLN A 4 82.03 179.85
REMARK 500 9 ARG C 33 74.78 -153.89
REMARK 500 9 SER B 3 -74.79 -107.46
REMARK 500 9 GLN B 4 62.19 -155.63
REMARK 500 10 ARG C 33 66.29 -103.56
REMARK 500 10 LEU D 15 5.35 -66.49
REMARK 500 11 SER A 3 -63.28 -94.44
REMARK 500 11 SER B 3 -66.18 -100.67
REMARK 500 11 GLN B 4 64.57 -162.88
REMARK 500 12 THR A 6 -2.32 -152.45
REMARK 500 12 ARG D 31 53.69 39.34
REMARK 500 13 SER A 3 -70.13 -110.15
REMARK 500 13 SER B 3 -70.88 -136.75
REMARK 500 14 SER A 3 -68.49 -162.99
REMARK 500 14 SER B 3 -67.58 -154.07
REMARK 500 15 SER A 3 -69.14 -152.01
REMARK 500 15 THR A 6 -50.21 -157.44
REMARK 500 15 LEU C 15 4.19 -63.76
REMARK 500
REMARK 500 THIS ENTRY HAS 65 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 1 TYR B 7 0.08 SIDE CHAIN
REMARK 500 1 TYR D 19 0.08 SIDE CHAIN
REMARK 500 2 TYR C 19 0.10 SIDE CHAIN
REMARK 500 2 TYR D 25 0.08 SIDE CHAIN
REMARK 500 3 ASP C 21 0.10 SIDE CHAIN
REMARK 500 4 ASP C 21 0.08 SIDE CHAIN
REMARK 500 4 TYR D 25 0.07 SIDE CHAIN
REMARK 500 4 TYR D 34 0.14 SIDE CHAIN
REMARK 500 5 TYR A 7 0.07 SIDE CHAIN
REMARK 500 6 ARG D 31 0.10 SIDE CHAIN
REMARK 500 7 TYR A 7 0.08 SIDE CHAIN
REMARK 500 7 ASP C 21 0.08 SIDE CHAIN
REMARK 500 8 TYR D 25 0.08 SIDE CHAIN
REMARK 500 8 TYR D 34 0.10 SIDE CHAIN
REMARK 500 9 ASP C 14 0.09 SIDE CHAIN
REMARK 500 9 GLU D 13 0.09 SIDE CHAIN
REMARK 500 10 ASP D 14 0.08 SIDE CHAIN
REMARK 500 10 ARG D 33 0.08 SIDE CHAIN
REMARK 500 11 TYR A 7 0.13 SIDE CHAIN
REMARK 500 11 ASP D 14 0.11 SIDE CHAIN
REMARK 500 12 ARG C 17 0.08 SIDE CHAIN
REMARK 500 13 TYR C 25 0.10 SIDE CHAIN
REMARK 500 13 ARG C 33 0.12 SIDE CHAIN
REMARK 500 14 ASP C 14 0.07 SIDE CHAIN
REMARK 500 14 ARG D 17 0.08 SIDE CHAIN
REMARK 500 14 ARG D 33 0.08 SIDE CHAIN
REMARK 500 15 TYR D 25 0.08 SIDE CHAIN
REMARK 500 16 TYR A 7 0.07 SIDE CHAIN
REMARK 500 16 ARG D 33 0.10 SIDE CHAIN
REMARK 500 17 ASP C 14 0.07 SIDE CHAIN
REMARK 500 18 ASP D 14 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 ZAB A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZAB B 110
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H3S RELATED DB: PDB
REMARK 900 THE SAME PEPTIDE IN PRESENCE OF DPC MICELLES
REMARK 900 RELATED ID: 2H3T RELATED DB: PDB
REMARK 900 THE SAME PEPTIDE CONTAINING TRANS INSTEAD OF CIS-4-
REMARK 900 AMINOMETHYLPHENYLAZOBENZOIC ACID IN PRESENCE OF DPC MICELLES
DBREF 2H4B A 1 9 UNP P68249 PAHO_MELGA 1 9
DBREF 2H4B B 1 9 UNP P68249 PAHO_MELGA 1 9
DBREF 2H4B C 11 34 UNP P68249 PAHO_MELGA 13 36
DBREF 2H4B D 11 34 UNP P68249 PAHO_MELGA 13 36
SEQRES 1 A 9 GLY PRO SER GLN PRO THR TYR PRO GLY
SEQRES 1 C 25 PRO VAL GLU ASP LEU ILE ARG PHE TYR ASN ASP LEU GLN
SEQRES 2 C 25 GLN TYR LEU ASN VAL VAL THR ARG HIS ARG TYR NH2
SEQRES 1 B 9 GLY PRO SER GLN PRO THR TYR PRO GLY
SEQRES 1 D 25 PRO VAL GLU ASP LEU ILE ARG PHE TYR ASN ASP LEU GLN
SEQRES 2 D 25 GLN TYR LEU ASN VAL VAL THR ARG HIS ARG TYR NH2
HET NH2 C 35 3
HET NH2 D 35 3
HET ZAB A 10 32
HET ZAB B 110 32
HETNAM NH2 AMINO GROUP
HETNAM ZAB (3-{(Z)-[3-(AMINOMETHYL)PHENYL]DIAZENYL}PHENYL)ACETIC
HETNAM 2 ZAB ACID
FORMUL 2 NH2 2(H2 N)
FORMUL 5 ZAB 2(C15 H15 N3 O2)
HELIX 1 1 PRO C 11 THR C 30 1 20
HELIX 2 2 PRO D 11 ARG D 31 1 21
LINK C GLY A 9 N ZAB A 10 1555 1555 1.34
LINK C ZAB A 10 N PRO C 11 1555 1555 1.34
LINK C TYR C 34 N NH2 C 35 1555 1555 1.32
LINK C GLY B 9 N ZAB B 110 1555 1555 1.34
LINK C ZAB B 110 N PRO D 11 1555 1555 1.34
LINK C TYR D 34 N NH2 D 35 1555 1555 1.33
SITE 1 AC1 5 GLY A 9 ZAB B 110 PRO C 11 LEU C 15
SITE 2 AC1 5 PHE C 18
SITE 1 AC2 7 ZAB A 10 PRO B 8 GLY B 9 PRO D 11
SITE 2 AC2 7 LEU D 15 PHE D 18 LEU D 22
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 - r 9 2 Bytes