Header list of 1zuv.pdb file
Complete list - 2 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 01-JUN-05 1ZUV
TITLE 24 NMR STRUCTURES OF ACAMP2-LIKE PEPTIDE WITH PHENYLALANINE 18 MUTATED
TITLE 2 TO TRYPTOPHAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMARANTHUS CAUDATUS ANTIMICROBIAL PEPTIDE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACMP2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE RESIDUE PHE18 WAS CHANGED TO TRYPTOPHAN. THE
SOURCE 4 SEQUENCE BY STANDARD SOLID PHASE SYNTHESIS USING FMOC CHEMISTRY
SOURCE 5 ACCORDING TO STANDARD PROTOCOLS.
KEYWDS ALFA-HELIX, ANTI-PARALLEL BETA-SHEET, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR M.I.CHAVEZ,C.ANDREU,P.VIDAL,F.FREIRE,N.ABOITIZ,P.GROVES,J.L.ASENSIO,
AUTHOR 2 G.ASENSIO,M.MURAKI,F.J.CANADA,J.JIMENEZ-BARBERO
REVDAT 3 02-MAR-22 1ZUV 1 REMARK
REVDAT 2 24-FEB-09 1ZUV 1 VERSN
REVDAT 1 06-DEC-05 1ZUV 0
JRNL AUTH C.ANDREU,P.VIDAL,N.ABOITIZ,F.FREIRE,P.GROVES,J.L.ASENSIO,
JRNL AUTH 2 G.ASENSIO,M.MURAKI
JRNL TITL ON THE IMPORTANCE OF CARBOHYDRATE-AROMATIC INTERACTIONS FOR
JRNL TITL 2 THE MOLECULAR RECOGNITION OF OLIGOSACCHARIDES BY PROTEINS:
JRNL TITL 3 NMR STUDIES OF THE STRUCTURE AND BINDING AFFINITY OF
JRNL TITL 4 ACAMP2-LIKE PEPTIDES WITH NON-NATURAL NAPHTHYL AND
JRNL TITL 5 FLUOROAROMATIC RESIDUES
JRNL REF CHEMISTRY V. 11 7060 2005
JRNL REFN ISSN 0947-6539
JRNL PMID 16220560
JRNL DOI 10.1002/CHEM.200500367
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.C.MARTINS,D.MAES,R.LORIS,H.A.M.PEPERMANS,L.WYNS,R.WILLEM,
REMARK 1 AUTH 2 P.VERHEYDEN
REMARK 1 TITL H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2, A SUGAR
REMARK 1 TITL 2 BINDING ANTIMICROBIAL PROTEIN ISOLATED FROM AMARANTHUS
REMARK 1 TITL 3 CAUDATUS
REMARK 1 REF J.MOL.BIOL. V. 258 322 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 8627629
REMARK 1 DOI 10.1006/JMBI.1996.0253
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.MURAKI
REMARK 1 TITL THE IMPORTANCE OF CH/PI INTERACTIONS TO THE FUNCTION OF
REMARK 1 TITL 2 CARBOHYDRATE BINDING PROTEINS
REMARK 1 REF PROTEIN PEPT.LETT. V. 9 195 2002
REMARK 1 REFN ISSN 0929-8665
REMARK 1 PMID 12144516
REMARK 1 REFERENCE 3
REMARK 1 AUTH N.ABOITIZ,M.VILA-PERELLO,P.GROVES,J.L.ASENSIO,D.ANDREU,
REMARK 1 AUTH 2 F.J.CANADA,J.JIMENEZ-BARBERO
REMARK 1 TITL NMR AND MODELING STUDIES OF PROTEIN-CARBOHYDRATE
REMARK 1 TITL 2 INTERACTIONS: SYNTHESIS, THREE-DIMENSIONAL STRUCTURE, AND
REMARK 1 TITL 3 RECOGNITION PROPERTIES OF A MINIMUM HEVEIN DOMAIN WITH
REMARK 1 TITL 4 BINDING AFFINITY FOR CHITOOLIGOSACCHARIDES
REMARK 1 REF CHEMBIOCHEM V. 5 1245 2004
REMARK 1 REFN ISSN 1439-4227
REMARK 1 PMID 15368576
REMARK 1 DOI 10.1002/CBIC.200400025
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.L.ASENSIO,H.C.SIEBERT,C.W.VON DER LIETH,J.LAYNEZ,M.BRUIX,
REMARK 1 AUTH 2 U.M.SOEDJANAAMADJA,J.J.BEINTEMA,F.J.CANADA,H.J.GABIUS,
REMARK 1 AUTH 3 J.JIMENEZ-BARBERO
REMARK 1 TITL NMR INVESTIGATIONS OF PROTEIN-CARBOHYDRATE INTERACTIONS:
REMARK 1 TITL 2 STUDIES ON THE RELEVANCE OF TRP/TYR VARIATIONS IN LECTIN
REMARK 1 TITL 3 BINDING SITES AS DEDUCED FROM TITRATION MICROCALORIMETRY AND
REMARK 1 TITL 4 NMR STUDIES ON HEVEIN DOMAINS. DETERMINATION OF THE NMR
REMARK 1 TITL 5 STRUCTURE OF THE COMPLEX BETWEEN PSEUDOHEVEIN AND
REMARK 1 TITL 6 N,N',N"-TRIACETYLCHITOTRIOSE
REMARK 1 REF PROTEINS V. 40 218 2000
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 10842338
REMARK 1 DOI 10.1002/(SICI)1097-0134(20000801)40:2<218::AID-PROT50>3.3.CO
REMARK 1 DOI 2 ;2-G
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.L.ASENSIO,F.J.CANADA,H.C.SIEBERT,J.LAYNEZ,A.POVEDA,
REMARK 1 AUTH 2 P.M.NIETO,U.M.SOEDJANAAMADJA,H.J.GABIUS,J.JIMENEZ-BARBERO
REMARK 1 TITL STRUCTURAL BASIS FOR CHITIN RECOGNITION BY DEFENSE PROTEINS:
REMARK 1 TITL 2 GLCNAC RESIDUES ARE BOUND IN A MULTIVALENT FASHION BY
REMARK 1 TITL 3 EXTENDED BINDING SITES IN HEVEIN DOMAINS
REMARK 1 REF CHEM.BIOL. V. 7 529 2000
REMARK 1 REFN ISSN 1074-5521
REMARK 1 PMID 10903932
REMARK 1 DOI 10.1016/S1074-5521(00)00136-8
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.MURAKI,H.MORII,K.HARATA
REMARK 1 TITL CHEMICALLY PREPARED HEVEIN DOMAINS: EFFECT OF C-TERMINAL
REMARK 1 TITL 2 TRUNCATION AND THE MUTAGENESIS OF AROMATIC RESIDUES ON THE
REMARK 1 TITL 3 AFFINITY FOR CHITIN
REMARK 1 REF PROTEIN ENG. V. 13 385 2000
REMARK 1 REFN ISSN 0269-2139
REMARK 1 PMID 10877847
REMARK 1 DOI 10.1093/PROTEIN/13.6.385
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.2, AMBER 5.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZUV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033146.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.76MM ACAMP2F18W; 20MM
REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : THE STRUCTURES ARE BASED ON 331
REMARK 210 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 210 AND 18 COME FROM CYS-CYS
REMARK 210 DISULFIDE BRIDGES
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
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 1 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 4 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 6 ARG A 6 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES
REMARK 500 6 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 6 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 ARG A 6 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 7 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 7 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 8 ARG A 6 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES
REMARK 500 8 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 8 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 ARG A 6 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 11 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 11 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 11 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ARG A 30 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 13 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 14 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 15 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 15 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 16 ARG A 6 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 16 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 16 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 16 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 17 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 17 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 18 ARG A 6 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 18 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 18 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 18 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 19 ARG A 6 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 19 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 20 ARG A 6 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 20 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 20 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 20 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 21 ARG A 6 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 21 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 23 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 24 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 51 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 CYS A 4 127.56 -38.96
REMARK 500 1 VAL A 5 -85.41 1.34
REMARK 500 1 SER A 11 80.06 -68.25
REMARK 500 1 TYR A 27 -53.47 -138.15
REMARK 500 2 ARG A 6 25.31 47.97
REMARK 500 3 ARG A 6 1.32 52.94
REMARK 500 3 SER A 11 93.25 -68.38
REMARK 500 3 MET A 13 176.04 -56.55
REMARK 500 3 TYR A 27 -54.92 -137.32
REMARK 500 4 SER A 11 106.03 -54.69
REMARK 500 4 TYR A 27 -50.78 -138.69
REMARK 500 5 GLU A 3 -176.66 57.45
REMARK 500 5 VAL A 5 -88.36 -4.57
REMARK 500 5 SER A 11 76.27 -69.49
REMARK 500 5 TYR A 27 -48.88 -134.28
REMARK 500 6 VAL A 5 -70.20 -30.44
REMARK 500 6 PRO A 10 177.00 -53.98
REMARK 500 6 SER A 11 90.83 -53.86
REMARK 500 6 PRO A 25 -0.70 -59.19
REMARK 500 6 TYR A 27 -47.07 -136.91
REMARK 500 7 SER A 11 46.99 37.74
REMARK 500 7 TYR A 27 -55.26 -125.37
REMARK 500 8 VAL A 5 -76.37 -19.95
REMARK 500 8 SER A 11 92.71 -56.63
REMARK 500 8 TYR A 27 -51.27 -130.92
REMARK 500 8 CYS A 28 -1.58 -143.95
REMARK 500 9 TYR A 27 -52.40 -133.45
REMARK 500 10 CYS A 4 99.69 -66.58
REMARK 500 10 VAL A 5 -90.53 2.73
REMARK 500 10 SER A 11 76.22 -69.83
REMARK 500 11 VAL A 5 -74.72 -22.47
REMARK 500 11 PRO A 10 -178.00 -58.39
REMARK 500 11 SER A 11 105.18 -43.80
REMARK 500 11 TYR A 27 -52.16 -120.39
REMARK 500 12 PRO A 10 177.97 -55.81
REMARK 500 12 TYR A 27 -53.02 -147.24
REMARK 500 12 CYS A 28 -46.53 -138.76
REMARK 500 13 PRO A 10 178.71 -57.54
REMARK 500 13 SER A 11 109.13 -42.87
REMARK 500 13 TYR A 27 -70.48 -129.96
REMARK 500 14 VAL A 5 -70.89 -49.18
REMARK 500 14 ARG A 6 17.28 -141.92
REMARK 500 14 SER A 11 30.07 -72.12
REMARK 500 14 MET A 13 -179.67 -61.02
REMARK 500 14 TYR A 27 -58.76 -134.08
REMARK 500 15 CYS A 4 119.76 -34.17
REMARK 500 15 VAL A 5 -85.33 0.92
REMARK 500 15 PRO A 10 178.41 -57.39
REMARK 500 16 SER A 11 96.23 -38.68
REMARK 500 16 TYR A 27 -63.34 -130.14
REMARK 500
REMARK 500 THIS ENTRY HAS 72 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 VAL A 5 ARG A 6 1 142.69
REMARK 500 MET A 13 CYS A 14 3 143.03
REMARK 500 VAL A 5 ARG A 6 4 142.26
REMARK 500 VAL A 5 ARG A 6 5 143.43
REMARK 500 VAL A 5 ARG A 6 6 138.45
REMARK 500 VAL A 5 ARG A 6 7 134.93
REMARK 500 VAL A 5 ARG A 6 8 139.65
REMARK 500 TYR A 27 CYS A 28 8 -148.06
REMARK 500 VAL A 5 ARG A 6 9 140.96
REMARK 500 VAL A 5 ARG A 6 10 141.99
REMARK 500 VAL A 5 ARG A 6 11 138.93
REMARK 500 VAL A 5 ARG A 6 13 139.07
REMARK 500 MET A 13 CYS A 14 13 147.90
REMARK 500 VAL A 5 ARG A 6 14 145.41
REMARK 500 MET A 13 CYS A 14 14 146.61
REMARK 500 VAL A 5 ARG A 6 15 140.84
REMARK 500 VAL A 5 ARG A 6 16 138.49
REMARK 500 GLU A 3 CYS A 4 17 148.92
REMARK 500 VAL A 5 ARG A 6 17 147.36
REMARK 500 VAL A 5 ARG A 6 18 140.86
REMARK 500 VAL A 5 ARG A 6 19 140.63
REMARK 500 MET A 13 CYS A 14 19 148.23
REMARK 500 CYS A 28 GLY A 29 19 147.09
REMARK 500 VAL A 5 ARG A 6 20 139.16
REMARK 500 VAL A 5 ARG A 6 21 129.76
REMARK 500 VAL A 5 ARG A 6 22 142.01
REMARK 500 VAL A 5 ARG A 6 23 137.58
REMARK 500 VAL A 5 ARG A 6 24 139.37
REMARK 500 MET A 13 CYS A 14 24 122.50
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 A 20 0.08 SIDE CHAIN
REMARK 500 2 ARG A 30 0.18 SIDE CHAIN
REMARK 500 3 TYR A 20 0.07 SIDE CHAIN
REMARK 500 3 TYR A 27 0.07 SIDE CHAIN
REMARK 500 4 ARG A 30 0.09 SIDE CHAIN
REMARK 500 5 ARG A 6 0.12 SIDE CHAIN
REMARK 500 9 TYR A 20 0.09 SIDE CHAIN
REMARK 500 9 ARG A 30 0.11 SIDE CHAIN
REMARK 500 10 ARG A 6 0.09 SIDE CHAIN
REMARK 500 11 TYR A 27 0.07 SIDE CHAIN
REMARK 500 14 TYR A 27 0.08 SIDE CHAIN
REMARK 500 15 TYR A 20 0.07 SIDE CHAIN
REMARK 500 16 ARG A 30 0.13 SIDE CHAIN
REMARK 500 17 ARG A 30 0.11 SIDE CHAIN
REMARK 500 18 ARG A 30 0.12 SIDE CHAIN
REMARK 500 20 TYR A 20 0.11 SIDE CHAIN
REMARK 500 22 TYR A 20 0.08 SIDE CHAIN
REMARK 500 22 ARG A 30 0.08 SIDE CHAIN
REMARK 500 23 TYR A 20 0.09 SIDE CHAIN
REMARK 500 24 TYR A 20 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MMC RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF ACAMP2 (AMARANTHUS CAUDATUS ANTIMICROBIAL PEPTIDE
REMARK 900 2) IN THE FREE STATE
DBREF 1ZUV A 1 30 PDB 1ZUV 1ZUV 1 30
SEQRES 1 A 30 VAL GLY GLU CYS VAL ARG GLY ARG CYS PRO SER GLY MET
SEQRES 2 A 30 CYS CYS SER GLN TRP GLY TYR CYS GLY LYS GLY PRO LYS
SEQRES 3 A 30 TYR CYS GLY ARG
SHEET 1 A 2 CYS A 14 CYS A 15 0
SHEET 2 A 2 CYS A 21 GLY A 22 -1 O GLY A 22 N CYS A 14
SSBOND 1 CYS A 4 CYS A 15 1555 1555 2.04
SSBOND 2 CYS A 9 CYS A 21 1555 1555 2.03
SSBOND 3 CYS A 14 CYS A 28 1555 1555 2.04
CISPEP 1 VAL A 1 GLY A 2 5 -1.64
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 - 2 20 Bytes