Header list of 1znt.pdb file
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HEADER ANTIMICROBIAL PROTEIN 12-MAY-05 1ZNT TITLE 18 NMR STRUCTURES OF ACAMP2-LIKE PEPTIDE WITH NON NATURAL TITLE 2 FLUOROAROMATIC RESIDUE (ACAMP2F18PFF/Y20PFF) COMPLEX WITH N,N,N- TITLE 3 TRIACETYLCHITOTRIOSE 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 PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN AMARANTHUS CAUDATUS (INCA- SOURCE 5 WHEAT). SEQUENCE PREPARED BY STANDARD SOLID PHASE PEPTIDE SYNTHESIS SOURCE 6 PROTOCOLS USING FMOC CHEMISTRY. PHE18 AND TYR20 HAVE BEEN MUTATED TO SOURCE 7 THE NON PROTEINOGENIC AMINOACID 4-FLUOROPHENYALANINE. KEYWDS ALFA-HELIX, ANTI-PARALLEL BETA-SHEET, ANTIMICROBIAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR M.I.CHAVEZ,C.ANDREU,P.VIDAL,N.ABOITIZ,F.FREIRE,P.GROVES,J.L.ASENSIO, AUTHOR 2 G.ASENSIO,M.MURAKI,F.J.CANADA,J.JIMENEZ-BARBERO REVDAT 4 29-JUL-20 1ZNT 1 COMPND REMARK HETNAM LINK REVDAT 4 2 1 SITE ATOM REVDAT 3 13-JUL-11 1ZNT 1 VERSN REVDAT 2 24-FEB-09 1ZNT 1 VERSN REVDAT 1 06-DEC-05 1ZNT 0 JRNL AUTH M.I.CHAVEZ,C.ANDREU,P.VIDAL,N.ABOITIZ,F.FREIRE,P.GROVES, JRNL AUTH 2 J.L.ASENSIO,G.ASENSIO,M.MURAKI,F.J.CANADA,J.JIMENEZ-BARBERO 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 1ZNT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000032933. 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 : 1MM ACAMP2F18PFF/Y20PFF, 12MM REMARK 210 CHITOTRIOSE, 20MM PHOSPHATE REMARK 210 BUFFER; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE 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 A REMARK 210 TOTAL 314 CROSS PEAKS, 248 NOE- REMARK 210 DERIVED DISTANCE RESTRAINTS, AND REMARK 210 FINALLY 208 DISTANCE CONSTRAINTS REMARK 210 AND 18 COME FROM CYS-CYS REMARK 210 DISULFIDE WERE USED IN THE FINAL REMARK 210 ROUND OF CALCULATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : FEWEST RESTRAINT VIOLATION, REMARK 210 SECONDARY LOWEST 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 WHICH ARE NOESY AT TM=300 AND TOCSY AT TM= REMARK 210 50 AND 70 MS 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, B 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: 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. = 3.0 DEGREES REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 5 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 5 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 5 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 7 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 8 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES REMARK 500 8 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 8 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 9 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 10 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 11 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 11 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 13 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 14 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 15 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 17 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 17 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.8 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 PRO A 10 177.05 -53.25 REMARK 500 1 SER A 11 82.44 -69.69 REMARK 500 1 PRO A 25 -72.39 -33.13 REMARK 500 2 SER A 11 73.46 -2.66 REMARK 500 3 PRO A 25 -72.76 -45.95 REMARK 500 4 GLU A 3 154.15 -44.22 REMARK 500 4 PRO A 10 -175.88 -57.66 REMARK 500 4 SER A 11 94.98 -28.98 REMARK 500 4 PRO A 25 -78.77 -42.74 REMARK 500 5 SER A 11 78.25 -68.15 REMARK 500 5 GLN A 17 0.07 -64.05 REMARK 500 6 GLU A 3 99.63 -45.10 REMARK 500 6 VAL A 5 49.62 -77.88 REMARK 500 6 SER A 11 39.50 35.86 REMARK 500 7 SER A 11 43.19 36.44 REMARK 500 7 SER A 16 -175.85 -67.06 REMARK 500 7 CYS A 28 -79.15 -105.79 REMARK 500 8 VAL A 5 48.83 -75.79 REMARK 500 8 ARG A 6 38.14 34.69 REMARK 500 8 SER A 11 102.99 -28.96 REMARK 500 9 PRO A 10 -175.79 -54.72 REMARK 500 9 SER A 11 94.62 -30.10 REMARK 500 9 GLN A 17 -9.78 -57.08 REMARK 500 9 PFF A 20 156.87 -46.32 REMARK 500 10 CYS A 9 -179.23 166.82 REMARK 500 10 PRO A 10 -179.58 -54.96 REMARK 500 10 SER A 11 99.18 -26.76 REMARK 500 11 CYS A 9 -174.36 -179.34 REMARK 500 11 PRO A 10 -179.57 -52.44 REMARK 500 11 SER A 11 106.28 -37.20 REMARK 500 11 GLN A 17 -1.24 -59.90 REMARK 500 11 TYR A 27 -61.15 -94.32 REMARK 500 12 GLU A 3 164.81 60.73 REMARK 500 12 CYS A 4 175.42 -49.18 REMARK 500 12 PRO A 10 -179.79 -57.22 REMARK 500 12 SER A 11 89.29 -12.73 REMARK 500 13 SER A 11 -172.59 57.38 REMARK 500 13 LYS A 23 60.18 -102.58 REMARK 500 14 GLU A 3 169.64 38.86 REMARK 500 14 CYS A 4 174.13 -41.54 REMARK 500 14 SER A 11 -168.46 53.88 REMARK 500 14 TYR A 27 -62.12 -97.94 REMARK 500 15 PRO A 10 177.63 -53.02 REMARK 500 16 PRO A 10 178.90 -48.86 REMARK 500 17 CYS A 4 173.04 -57.42 REMARK 500 17 VAL A 5 48.21 -81.95 REMARK 500 17 SER A 11 -170.41 52.10 REMARK 500 18 SER A 11 -174.46 57.74 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 GLY A 2 GLU A 3 9 139.38 REMARK 500 GLY A 29 ARG A 30 9 -145.58 REMARK 500 GLY A 2 GLU A 3 15 139.31 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 2 ARG A 6 0.12 SIDE CHAIN REMARK 500 2 ARG A 8 0.12 SIDE CHAIN REMARK 500 2 ARG A 30 0.10 SIDE CHAIN REMARK 500 3 ARG A 6 0.16 SIDE CHAIN REMARK 500 3 ARG A 30 0.13 SIDE CHAIN REMARK 500 4 ARG A 30 0.19 SIDE CHAIN REMARK 500 6 ARG A 8 0.11 SIDE CHAIN REMARK 500 6 ARG A 30 0.12 SIDE CHAIN REMARK 500 8 ARG A 6 0.14 SIDE CHAIN REMARK 500 9 TYR A 27 0.07 SIDE CHAIN REMARK 500 9 ARG A 30 0.09 SIDE CHAIN REMARK 500 10 ARG A 8 0.11 SIDE CHAIN REMARK 500 10 ARG A 30 0.12 SIDE CHAIN REMARK 500 11 ARG A 6 0.14 SIDE CHAIN REMARK 500 11 ARG A 30 0.09 SIDE CHAIN REMARK 500 12 ARG A 30 0.11 SIDE CHAIN REMARK 500 13 TYR A 27 0.08 SIDE CHAIN REMARK 500 16 TYR A 27 0.07 SIDE CHAIN REMARK 500 17 ARG A 30 0.12 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 1ZNT A 1 31 PDB 1ZNT 1ZNT 1 31 SEQRES 1 A 31 VAL GLY GLU CYS VAL ARG GLY ARG CYS PRO SER GLY MET SEQRES 2 A 31 CYS CYS SER GLN PFF GLY PFF CYS GLY LYS GLY PRO LYS SEQRES 3 A 31 TYR CYS GLY ARG NH2 MODRES 1ZNT PFF A 18 PHE 4-FLUORO-L-PHENYLALANINE MODRES 1ZNT PFF A 20 PHE 4-FLUORO-L-PHENYLALANINE HET PFF A 18 20 HET PFF A 20 20 HET NH2 A 31 3 HET NAG B 1 29 HET NAG B 2 27 HET NAG B 3 28 HETNAM PFF 4-FLUORO-L-PHENYLALANINE HETNAM NH2 AMINO GROUP HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE FORMUL 1 PFF 2(C9 H10 F N O2) FORMUL 1 NH2 H2 N FORMUL 2 NAG 3(C8 H15 N O6) HELIX 1 1 GLY A 24 GLY A 29 1 6 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 LINK C GLN A 17 N PFF A 18 1555 1555 1.34 LINK C PFF A 18 N GLY A 19 1555 1555 1.33 LINK C GLY A 19 N PFF A 20 1555 1555 1.33 LINK C PFF A 20 N CYS A 21 1555 1555 1.33 LINK C ARG A 30 N NH2 A 31 1555 1555 1.32 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39 LINK O4 NAG B 2 C1 NAG B 3 1555 1555 1.40 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 - 29 20 Bytes