Header list of 1akp.pdb file
Complete list - v 29 2 Bytes
HEADER ANTIBIOTIC CHROMOPROTEIN 20-JUN-94 1AKP
TITLE SEQUENTIAL 1H,13C AND 15N NMR ASSIGNMENTS AND SOLUTION CONFORMATION OF
TITLE 2 APOKEDARCIDIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOKEDARCIDIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINOMYCETE ATCC 53650;
SOURCE 3 ORGANISM_TAXID: 38989;
SOURCE 4 STRAIN: L585-6 / ATCC 53650
KEYWDS ANTIBIOTIC CHROMOPROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.L.CONSTANTINE,K.L.COLSON,M.WITTEKIND,M.S.FRIEDRICHS,N.ZEIN,
AUTHOR 2 J.TUTTLE,D.R.LANGLEY,J.E.LEET,D.R.SCHROEDER,K.S.LAM,B.T.FARMER II,
AUTHOR 3 W.J.METZLER,R.E.BRUCCOLERI,L.MUELLER
REVDAT 5 29-NOV-17 1AKP 1 HELIX
REVDAT 4 22-FEB-12 1AKP 1 JRNL VERSN
REVDAT 3 24-FEB-09 1AKP 1 VERSN
REVDAT 2 01-APR-03 1AKP 1 JRNL
REVDAT 1 31-AUG-94 1AKP 0
JRNL AUTH K.L.CONSTANTINE,K.L.COLSON,M.WITTEKIND,M.S.FRIEDRICHS,
JRNL AUTH 2 N.ZEIN,J.TUTTLE,D.R.LANGLEY,J.E.LEET,D.R.SCHROEDER,K.S.LAM,
JRNL AUTH 3 B.T.FARMER III,W.J.METZLER,R.E.BRUCCOLERI,L.MUELLER
JRNL TITL SEQUENTIAL 1H, 13C, AND 15N NMR ASSIGNMENTS AND SOLUTION
JRNL TITL 2 CONFORMATION OF APOKEDARCIDIN.
JRNL REF BIOCHEMISTRY V. 33 11438 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7918358
JRNL DOI 10.1021/BI00204A006
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.E.LEET,D.R.SCHROEDER,D.R.LANGLEY,K.L.COLSON,S.HUANG,
REMARK 1 AUTH 2 S.E.KLOHR,M.S.LEE,J.GOLIK,S.J.HOFSTEAD,T.W.DOYLE,J.A.MATSON
REMARK 1 TITL CHEMISTRY AND STRUCTURE ELUCIDATION OF THE KEDARCIDIN
REMARK 1 TITL 2 CHROMOPHORE
REMARK 1 REF J.AM.CHEM.SOC. V. 115 8432 1993
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 2
REMARK 1 AUTH N.ZEIN,K.L.COLSON,J.E.LEET,D.R.SCHROEDER,W.SOLOMON,
REMARK 1 AUTH 2 T.W.DOYLE,A.M.CASAZZA
REMARK 1 TITL KEDARCIDIN CHROMOPHORE: AN ENEDIYNE THAT CLEAVES DNA IN A
REMARK 1 TITL 2 SEQUENCE-SPECIFIC MANNER
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 2822 1993
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH N.ZEIN,A.M.CASAZZA,T.W.DOYLE,J.E.LEET,D.R.SCHEOEDER,
REMARK 1 AUTH 2 W.SOLOMON,S.G.NADLER
REMARK 1 TITL SELECTIVE PROTEOLYTIC ACTIVITY OF THE ANTITUMOR AGENT
REMARK 1 TITL 2 KEDARCIDIN
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 8009 1993
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 4
REMARK 1 AUTH S.J.HOFSTEAD,J.A.MATSON,A.R.MALACKO,H.MARQUART
REMARK 1 TITL KEDARCIDIN, A NEW CHROMOPROTEIN ANTITUMOR ANTIBIOTIC. II.
REMARK 1 TITL 2 ISOLATION, PURIFICATION AND PHYSICO-CHEMICAL PROPERTIES
REMARK 1 REF J.ANTIBIOT. V. 45 1250 1992
REMARK 1 REFN ISSN 0021-8820
REMARK 1 REFERENCE 5
REMARK 1 AUTH K.S.LAM,G.A.HESLER,D.R.GUSTAVSON,A.R.CROSSWELL,J.M.VEITCH,
REMARK 1 AUTH 2 S.FORENZA,K.TOMITA
REMARK 1 TITL KEDARCIDIN, A NEW CHROMOPROTEIN ANTITUMOR ANTIBIOTIC I.
REMARK 1 TITL 2 TAXONOMY OF PRODUCING ORGANISM, FERMENTATION AND BIOLOGICAL
REMARK 1 TITL 3 ACTIVITY
REMARK 1 REF J.ANTIBIOT. V. 44 472 1991
REMARK 1 REFN ISSN 0021-8820
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AKP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170936.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 PHE A 52 CB PHE A 52 CG 0.104
REMARK 500 1 HIS A 53 CG HIS A 53 ND1 -0.091
REMARK 500 1 TYR A 106 CB TYR A 106 CG 0.095
REMARK 500 3 PHE A 52 CB PHE A 52 CG 0.104
REMARK 500 3 TYR A 106 CB TYR A 106 CG 0.093
REMARK 500 4 HIS A 53 CG HIS A 53 ND1 -0.091
REMARK 500 4 PHE A 72 CB PHE A 72 CG 0.105
REMARK 500 5 HIS A 53 CG HIS A 53 ND1 -0.092
REMARK 500 6 HIS A 53 CG HIS A 53 ND1 -0.090
REMARK 500 7 TYR A 75 CB TYR A 75 CG 0.091
REMARK 500 7 TYR A 106 CB TYR A 106 CG 0.092
REMARK 500 8 HIS A 53 CG HIS A 53 ND1 -0.091
REMARK 500 8 PHE A 55 CB PHE A 55 CG 0.111
REMARK 500 9 HIS A 53 CG HIS A 53 ND1 -0.090
REMARK 500 10 HIS A 53 CG HIS A 53 ND1 -0.092
REMARK 500 11 HIS A 53 CG HIS A 53 ND1 -0.093
REMARK 500 12 PHE A 52 CB PHE A 52 CG 0.103
REMARK 500 12 HIS A 53 CG HIS A 53 ND1 -0.091
REMARK 500 13 HIS A 53 CG HIS A 53 ND1 -0.092
REMARK 500 13 TYR A 106 CB TYR A 106 CG 0.096
REMARK 500 14 TYR A 75 CB TYR A 75 CG 0.093
REMARK 500 15 HIS A 53 CG HIS A 53 ND1 -0.092
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 14 CYS A 47 CA - CB - SG ANGL. DEV. = 7.3 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 8 113.01 -160.42
REMARK 500 1 ALA A 10 -8.65 -140.22
REMARK 500 1 ALA A 27 -59.15 -168.95
REMARK 500 1 HIS A 53 -63.93 -133.82
REMARK 500 1 ASP A 54 98.50 53.41
REMARK 500 1 MET A 77 169.49 48.20
REMARK 500 2 ALA A 3 -173.23 59.40
REMARK 500 2 SER A 8 111.85 -160.88
REMARK 500 2 PHE A 26 146.62 58.90
REMARK 500 2 ALA A 27 -37.74 -163.88
REMARK 500 2 THR A 28 -30.09 -136.84
REMARK 500 2 HIS A 53 -60.06 -146.17
REMARK 500 2 ASP A 54 93.70 45.44
REMARK 500 2 ASP A 79 -47.33 -160.12
REMARK 500 2 VAL A 83 -92.57 -79.92
REMARK 500 2 THR A 103 -70.66 -69.90
REMARK 500 2 ALA A 109 98.36 -161.90
REMARK 500 3 ALA A 3 -172.01 62.02
REMARK 500 3 ALA A 27 -38.24 -165.38
REMARK 500 3 HIS A 53 -66.63 -143.79
REMARK 500 3 ASP A 54 127.81 52.22
REMARK 500 3 PHE A 55 145.43 -172.84
REMARK 500 3 ASP A 79 -60.32 -160.05
REMARK 500 3 GLU A 105 -94.19 62.15
REMARK 500 3 ALA A 109 94.71 -161.47
REMARK 500 4 SER A 2 11.38 -144.63
REMARK 500 4 ALA A 10 -8.18 -141.54
REMARK 500 4 ALA A 27 -70.55 -66.85
REMARK 500 4 HIS A 53 -61.52 -146.24
REMARK 500 4 ASP A 54 99.53 56.55
REMARK 500 4 ASP A 79 -43.04 -160.27
REMARK 500 4 THR A 103 -70.88 -70.00
REMARK 500 4 ALA A 109 99.36 -162.30
REMARK 500 5 ALA A 27 -30.52 -158.82
REMARK 500 5 THR A 28 -40.38 -143.59
REMARK 500 5 HIS A 53 -44.65 -148.25
REMARK 500 5 ASP A 54 130.88 63.49
REMARK 500 5 ASP A 79 -47.50 -160.13
REMARK 500 5 ALA A 109 102.19 -164.12
REMARK 500 6 ALA A 27 -18.64 -160.81
REMARK 500 6 HIS A 53 -52.99 -145.42
REMARK 500 6 ASP A 54 97.24 51.37
REMARK 500 6 ASP A 79 -45.23 -160.17
REMARK 500 6 ALA A 109 109.78 -164.13
REMARK 500 6 SER A 112 119.65 -161.19
REMARK 500 7 SER A 2 -40.14 -167.47
REMARK 500 7 ALA A 10 -5.31 -141.15
REMARK 500 7 ALA A 27 -21.99 -161.11
REMARK 500 7 HIS A 53 -61.35 -145.85
REMARK 500 7 ASP A 54 112.30 59.43
REMARK 500
REMARK 500 THIS ENTRY HAS 114 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 ARG A 44 0.32 SIDE CHAIN
REMARK 500 1 ARG A 69 0.32 SIDE CHAIN
REMARK 500 1 ARG A 70 0.31 SIDE CHAIN
REMARK 500 2 ARG A 44 0.30 SIDE CHAIN
REMARK 500 2 ARG A 69 0.32 SIDE CHAIN
REMARK 500 2 ARG A 70 0.31 SIDE CHAIN
REMARK 500 3 ARG A 44 0.32 SIDE CHAIN
REMARK 500 3 ARG A 69 0.32 SIDE CHAIN
REMARK 500 3 ARG A 70 0.32 SIDE CHAIN
REMARK 500 4 ARG A 44 0.31 SIDE CHAIN
REMARK 500 4 ARG A 69 0.28 SIDE CHAIN
REMARK 500 4 ARG A 70 0.32 SIDE CHAIN
REMARK 500 5 ARG A 44 0.32 SIDE CHAIN
REMARK 500 5 ARG A 69 0.31 SIDE CHAIN
REMARK 500 5 ARG A 70 0.32 SIDE CHAIN
REMARK 500 6 ARG A 44 0.30 SIDE CHAIN
REMARK 500 6 ARG A 69 0.31 SIDE CHAIN
REMARK 500 6 ARG A 70 0.32 SIDE CHAIN
REMARK 500 7 ARG A 44 0.32 SIDE CHAIN
REMARK 500 7 ARG A 69 0.31 SIDE CHAIN
REMARK 500 7 ARG A 70 0.31 SIDE CHAIN
REMARK 500 8 ARG A 44 0.32 SIDE CHAIN
REMARK 500 8 ARG A 69 0.32 SIDE CHAIN
REMARK 500 8 ARG A 70 0.32 SIDE CHAIN
REMARK 500 9 ARG A 44 0.32 SIDE CHAIN
REMARK 500 9 ARG A 69 0.30 SIDE CHAIN
REMARK 500 9 ARG A 70 0.32 SIDE CHAIN
REMARK 500 10 ARG A 44 0.32 SIDE CHAIN
REMARK 500 10 ARG A 69 0.32 SIDE CHAIN
REMARK 500 10 ARG A 70 0.32 SIDE CHAIN
REMARK 500 11 ARG A 44 0.30 SIDE CHAIN
REMARK 500 11 ARG A 69 0.31 SIDE CHAIN
REMARK 500 11 ARG A 70 0.32 SIDE CHAIN
REMARK 500 12 ARG A 44 0.32 SIDE CHAIN
REMARK 500 12 ARG A 69 0.31 SIDE CHAIN
REMARK 500 12 ARG A 70 0.32 SIDE CHAIN
REMARK 500 13 ARG A 44 0.32 SIDE CHAIN
REMARK 500 13 ARG A 69 0.30 SIDE CHAIN
REMARK 500 13 ARG A 70 0.32 SIDE CHAIN
REMARK 500 14 ARG A 44 0.31 SIDE CHAIN
REMARK 500 14 ARG A 69 0.32 SIDE CHAIN
REMARK 500 14 ARG A 70 0.31 SIDE CHAIN
REMARK 500 15 ARG A 44 0.32 SIDE CHAIN
REMARK 500 15 ARG A 69 0.31 SIDE CHAIN
REMARK 500 15 ARG A 70 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: S1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1AKP A 1 114 UNP P41249 KEDA_ACTSL 1 114
SEQRES 1 A 114 ALA SER ALA ALA VAL SER VAL SER PRO ALA THR GLY LEU
SEQRES 2 A 114 ALA ASP GLY ALA THR VAL THR VAL SER ALA SER GLY PHE
SEQRES 3 A 114 ALA THR SER THR SER ALA THR ALA LEU GLN CYS ALA ILE
SEQRES 4 A 114 LEU ALA ASP GLY ARG GLY ALA CYS ASN VAL ALA GLU PHE
SEQRES 5 A 114 HIS ASP PHE SER LEU SER GLY GLY GLU GLY THR THR SER
SEQRES 6 A 114 VAL VAL VAL ARG ARG SER PHE THR GLY TYR VAL MET PRO
SEQRES 7 A 114 ASP GLY PRO GLU VAL GLY ALA VAL ASP CYS ASP THR ALA
SEQRES 8 A 114 PRO GLY GLY CYS GLU ILE VAL VAL GLY GLY ASN THR GLY
SEQRES 9 A 114 GLU TYR GLY ASN ALA ALA ILE SER PHE GLY
HELIX 1 I VAL A 49 PHE A 52 1TYPE III (HELIX-LIKE) TURN 4
HELIX 2 II CYS A 88 ALA A 91 1TYPE III (HELIX-LIKE) TURN 4
SHEET 1 S1 3 ALA A 4 SER A 8 0
SHEET 2 S1 3 ALA A 17 GLY A 25 -1 N SER A 24 O ALA A 4
SHEET 3 S1 3 GLU A 61 VAL A 68 -1 N GLY A 62 O ALA A 23
SHEET 1 S2 4 HIS A 53 LEU A 57 0
SHEET 2 S2 4 THR A 30 LEU A 40 -1 O THR A 30 N LEU A 57
SHEET 3 S2 4 GLY A 94 GLY A 101 -1 O GLY A 100 N THR A 33
SHEET 4 S2 4 TYR A 106 GLY A 114 -1 N ILE A 111 O CYS A 95
SHEET 1 S3 2 THR A 30 LEU A 40 0
SHEET 2 S3 2 ARG A 44 ASN A 48 -1 O ALA A 46 N ALA A 38
SHEET 1 S4 2 SER A 71 VAL A 76 0
SHEET 2 S4 2 VAL A 83 ASP A 87 -1 N VAL A 86 O PHE A 72
SSBOND 1 CYS A 37 CYS A 47 1555 1555 2.02
SSBOND 2 CYS A 88 CYS A 95 1555 1555 2.02
CISPEP 1 SER A 8 PRO A 9 1 -3.28
CISPEP 2 GLY A 80 PRO A 81 1 -1.52
CISPEP 3 SER A 8 PRO A 9 2 -3.96
CISPEP 4 GLY A 80 PRO A 81 2 0.09
CISPEP 5 SER A 8 PRO A 9 3 -3.70
CISPEP 6 GLY A 80 PRO A 81 3 -1.07
CISPEP 7 SER A 8 PRO A 9 4 -3.02
CISPEP 8 GLY A 80 PRO A 81 4 0.13
CISPEP 9 SER A 8 PRO A 9 5 -2.65
CISPEP 10 GLY A 80 PRO A 81 5 0.05
CISPEP 11 SER A 8 PRO A 9 6 -4.38
CISPEP 12 GLY A 80 PRO A 81 6 -0.10
CISPEP 13 SER A 8 PRO A 9 7 -3.96
CISPEP 14 GLY A 80 PRO A 81 7 0.79
CISPEP 15 SER A 8 PRO A 9 8 -4.59
CISPEP 16 GLY A 80 PRO A 81 8 -0.13
CISPEP 17 SER A 8 PRO A 9 9 -4.12
CISPEP 18 GLY A 80 PRO A 81 9 -0.67
CISPEP 19 SER A 8 PRO A 9 10 -3.34
CISPEP 20 GLY A 80 PRO A 81 10 -1.25
CISPEP 21 SER A 8 PRO A 9 11 -4.05
CISPEP 22 GLY A 80 PRO A 81 11 -0.54
CISPEP 23 SER A 8 PRO A 9 12 -3.81
CISPEP 24 GLY A 80 PRO A 81 12 -6.86
CISPEP 25 SER A 8 PRO A 9 13 -2.99
CISPEP 26 GLY A 80 PRO A 81 13 -0.87
CISPEP 27 SER A 8 PRO A 9 14 -2.80
CISPEP 28 GLY A 80 PRO A 81 14 -6.13
CISPEP 29 SER A 8 PRO A 9 15 -4.36
CISPEP 30 GLY A 80 PRO A 81 15 -1.03
SITE 1 S1 15 THR A 33 LEU A 35 CYS A 37 ILE A 39
SITE 2 S1 15 ARG A 44 CYS A 47 VAL A 49 PHE A 52
SITE 3 S1 15 ASP A 54 TYR A 75 MET A 77 GLU A 96
SITE 4 S1 15 VAL A 98 TYR A 106 ASN A 108
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 - v 29 2 Bytes