Header list of 1c5a.pdb file
Complete list - b 16 2 Bytes
HEADER COMPLEMENT FACTOR 12-JUN-90 1C5A
TITLE THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR
TITLE 2 MAGNETIC RESONANCE DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT C5A ANAPHYLATOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA DOMESTICA;
SOURCE 3 ORGANISM_COMMON: DOMESTIC PIG;
SOURCE 4 ORGANISM_TAXID: 9825;
SOURCE 5 STRAIN: DOMESTICA
KEYWDS COMPLEMENT FACTOR
EXPDTA SOLUTION NMR
NUMMDL 41
AUTHOR M.P.WILLIAMSON,V.S.MADISON
REVDAT 4 16-FEB-22 1C5A 1 REMARK
REVDAT 3 24-FEB-09 1C5A 1 VERSN
REVDAT 2 15-JAN-95 1C5A 1 SEQRES
REVDAT 1 15-OCT-91 1C5A 0
JRNL AUTH M.P.WILLIAMSON,V.S.MADISON
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADESARG FROM 1H
JRNL TITL 2 NUCLEAR MAGNETIC RESONANCE DATA.
JRNL REF BIOCHEMISTRY V. 29 2895 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2337573
JRNL DOI 10.1021/BI00464A002
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.P.WILLIAMSON
REMARK 1 TITL 1H NUCLEAR MAGNETIC RESONANCE ASSIGNMENTS AND SECONDARY
REMARK 1 TITL 2 STRUCTURE OF PORCINE C5ADESARG
REMARK 1 REF J.MOL.BIOL. V. 206 407 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C5A 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_1000172172.
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 : 41
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-41
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 67
REMARK 465 LYS A 68
REMARK 465 ASN A 69
REMARK 465 ILE A 70
REMARK 465 GLN A 71
REMARK 465 LEU A 72
REMARK 465 GLY A 73
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-41
REMARK 470 RES CSSEQI ATOMS
REMARK 470 SER A 66 CA C O CB OG
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 HZ3 LYS A 52 OH TYR A 56 1.41
REMARK 500 HZ1 LYS A 5 OD2 ASP A 53 1.48
REMARK 500 HZ1 LYS A 4 OE1 GLU A 7 1.48
REMARK 500 O GLU A 8 HZ1 LYS A 12 1.49
REMARK 500 HZ1 LYS A 20 OD1 ASP A 24 1.54
REMARK 500 HZ2 LYS A 20 OH TYR A 27 1.59
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 TYR A 23 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TYR A 23 CB - CG - CD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 1 ARG A 37 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 TYR A 56 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 1 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 2 TYR A 15 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 TYR A 23 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 TYR A 23 CB - CG - CD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 2 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 ARG A 37 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 2 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 2 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 2 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 3 TYR A 23 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 TYR A 23 CB - CG - CD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 3 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 4 TYR A 23 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TYR A 23 CB - CG - CD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 4 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 4 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 4 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 4 ARG A 37 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 4 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 4 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 5 TYR A 13 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 TYR A 23 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 TYR A 23 CB - CG - CD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 5 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 5 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 5 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 5 CYS A 55 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 5 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 5 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 6 TYR A 23 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 6 TYR A 23 CB - CG - CD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 6 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 6 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 6 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 6 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 6 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 6 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 345 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 TYR A 27 60.66 -68.41
REMARK 500 1 ASP A 31 -25.10 62.32
REMARK 500 1 GLU A 32 -148.58 -69.62
REMARK 500 2 LEU A 2 -99.88 52.21
REMARK 500 2 TYR A 13 -8.68 -55.49
REMARK 500 2 ASP A 31 -50.43 63.06
REMARK 500 2 GLU A 32 -118.52 -73.00
REMARK 500 3 ASN A 29 19.41 -146.98
REMARK 500 3 ASP A 31 -53.91 66.31
REMARK 500 4 LYS A 12 54.38 -68.27
REMARK 500 4 ARG A 28 38.59 -92.52
REMARK 500 4 GLN A 65 -67.58 -107.79
REMARK 500 5 ALA A 10 43.27 -103.63
REMARK 500 5 ALA A 11 28.60 -57.80
REMARK 500 5 TYR A 13 -150.70 -123.58
REMARK 500 5 ASN A 29 -106.81 -134.13
REMARK 500 5 ILE A 41 90.23 -67.04
REMARK 500 6 ALA A 11 56.22 -54.94
REMARK 500 6 LYS A 12 -50.05 65.63
REMARK 500 6 TYR A 13 130.29 64.17
REMARK 500 6 ASP A 30 61.23 -69.51
REMARK 500 6 ILE A 41 95.03 -67.53
REMARK 500 6 GLN A 65 -62.41 -128.64
REMARK 500 7 LYS A 12 -58.99 -155.60
REMARK 500 7 TYR A 13 123.10 70.62
REMARK 500 7 ILE A 41 86.38 -67.92
REMARK 500 8 ALA A 10 45.65 -105.96
REMARK 500 8 ALA A 11 28.01 -59.70
REMARK 500 8 TYR A 13 -152.32 -124.78
REMARK 500 8 ARG A 28 -55.47 63.68
REMARK 500 8 ASN A 29 146.46 71.99
REMARK 500 8 ILE A 41 97.38 -51.63
REMARK 500 9 ASP A 31 -18.38 58.51
REMARK 500 9 GLU A 32 -113.84 -70.31
REMARK 500 10 ARG A 28 47.64 -88.36
REMARK 500 10 LYS A 42 68.56 -11.05
REMARK 500 10 GLN A 65 -51.79 -137.61
REMARK 500 11 ALA A 10 4.57 -68.52
REMARK 500 11 TYR A 13 -22.86 62.19
REMARK 500 11 ASN A 29 -112.02 -85.87
REMARK 500 11 ASP A 30 44.68 -78.26
REMARK 500 12 LEU A 2 -84.07 55.80
REMARK 500 12 LYS A 42 69.89 -9.47
REMARK 500 13 TYR A 13 -26.96 62.09
REMARK 500 13 ASP A 30 64.06 -69.25
REMARK 500 13 ASP A 31 -73.43 -123.94
REMARK 500 13 ILE A 41 82.40 -69.81
REMARK 500 13 GLN A 65 -48.15 -140.70
REMARK 500 14 TYR A 13 -14.84 61.46
REMARK 500 14 ASP A 31 -65.11 -136.61
REMARK 500
REMARK 500 THIS ENTRY HAS 162 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 ALA A 38 ALA A 39 1 146.48
REMARK 500 ALA A 38 ALA A 39 4 144.01
REMARK 500 ALA A 38 ALA A 39 5 143.20
REMARK 500 TYR A 13 LYS A 14 7 149.83
REMARK 500 ALA A 38 ALA A 39 7 148.99
REMARK 500 ALA A 38 ALA A 39 8 145.56
REMARK 500 ALA A 10 ALA A 11 10 148.94
REMARK 500 ALA A 38 ALA A 39 11 144.52
REMARK 500 ALA A 38 ALA A 39 14 147.05
REMARK 500 ALA A 10 ALA A 11 15 147.99
REMARK 500 ALA A 38 ALA A 39 15 148.05
REMARK 500 ALA A 38 ALA A 39 17 143.31
REMARK 500 ALA A 38 ALA A 39 18 148.85
REMARK 500 ALA A 38 ALA A 39 20 143.31
REMARK 500 ALA A 38 ALA A 39 21 145.51
REMARK 500 ALA A 38 ALA A 39 22 149.30
REMARK 500 ALA A 38 ALA A 39 23 136.35
REMARK 500 ALA A 38 ALA A 39 24 147.60
REMARK 500 GLU A 9 ALA A 10 25 147.59
REMARK 500 ALA A 10 ALA A 11 25 -149.87
REMARK 500 GLU A 9 ALA A 10 26 124.63
REMARK 500 ALA A 38 ALA A 39 27 142.87
REMARK 500 ALA A 10 ALA A 11 28 148.54
REMARK 500 ALA A 38 ALA A 39 29 146.40
REMARK 500 ALA A 10 ALA A 11 30 149.46
REMARK 500 ALA A 38 ALA A 39 30 140.07
REMARK 500 ALA A 38 ALA A 39 31 140.70
REMARK 500 ALA A 38 ALA A 39 32 145.38
REMARK 500 ALA A 38 ALA A 39 34 141.27
REMARK 500 GLU A 9 ALA A 10 35 114.52
REMARK 500 TYR A 15 ALA A 16 35 -144.43
REMARK 500 LEU A 18 LYS A 19 35 148.50
REMARK 500 ALA A 38 ALA A 39 35 140.64
REMARK 500 GLU A 9 ALA A 10 36 85.56
REMARK 500 TYR A 15 ALA A 16 36 -143.25
REMARK 500 GLU A 9 ALA A 10 37 81.17
REMARK 500 ALA A 38 ALA A 39 37 142.26
REMARK 500 ALA A 38 ALA A 39 38 149.07
REMARK 500 ALA A 38 ALA A 39 39 147.46
REMARK 500 ALA A 38 ALA A 39 40 140.31
REMARK 500 ALA A 38 ALA A 39 41 145.78
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 TYR A 23 0.07 SIDE CHAIN
REMARK 500 3 TYR A 15 0.08 SIDE CHAIN
REMARK 500 4 ARG A 37 0.09 SIDE CHAIN
REMARK 500 6 TYR A 23 0.07 SIDE CHAIN
REMARK 500 6 PHE A 51 0.08 SIDE CHAIN
REMARK 500 7 TYR A 15 0.08 SIDE CHAIN
REMARK 500 8 PHE A 51 0.07 SIDE CHAIN
REMARK 500 10 TYR A 15 0.07 SIDE CHAIN
REMARK 500 10 ARG A 37 0.08 SIDE CHAIN
REMARK 500 11 TYR A 23 0.07 SIDE CHAIN
REMARK 500 12 TYR A 23 0.09 SIDE CHAIN
REMARK 500 13 ARG A 37 0.08 SIDE CHAIN
REMARK 500 16 ARG A 28 0.09 SIDE CHAIN
REMARK 500 17 TYR A 23 0.07 SIDE CHAIN
REMARK 500 19 TYR A 23 0.06 SIDE CHAIN
REMARK 500 20 TYR A 23 0.07 SIDE CHAIN
REMARK 500 22 TYR A 13 0.08 SIDE CHAIN
REMARK 500 24 TYR A 23 0.07 SIDE CHAIN
REMARK 500 25 TYR A 23 0.07 SIDE CHAIN
REMARK 500 26 TYR A 23 0.09 SIDE CHAIN
REMARK 500 26 PHE A 51 0.09 SIDE CHAIN
REMARK 500 27 TYR A 23 0.07 SIDE CHAIN
REMARK 500 29 ARG A 28 0.09 SIDE CHAIN
REMARK 500 29 ARG A 62 0.08 SIDE CHAIN
REMARK 500 31 TYR A 23 0.07 SIDE CHAIN
REMARK 500 32 TYR A 23 0.07 SIDE CHAIN
REMARK 500 33 ARG A 37 0.07 SIDE CHAIN
REMARK 500 34 ARG A 62 0.07 SIDE CHAIN
REMARK 500 36 TYR A 56 0.09 SIDE CHAIN
REMARK 500 40 ARG A 37 0.10 SIDE CHAIN
REMARK 500 41 ARG A 37 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1C5A A 1 73 UNP P01032 CO5_PIG 1 73
SEQRES 1 A 73 MET LEU GLN LYS LYS ILE GLU GLU GLU ALA ALA LYS TYR
SEQRES 2 A 73 LYS TYR ALA MET LEU LYS LYS CYS CYS TYR ASP GLY ALA
SEQRES 3 A 73 TYR ARG ASN ASP ASP GLU THR CYS GLU GLU ARG ALA ALA
SEQRES 4 A 73 ARG ILE LYS ILE GLY PRO LYS CYS VAL LYS ALA PHE LYS
SEQRES 5 A 73 ASP CYS CYS TYR ILE ALA ASN GLN VAL ARG ALA GLU GLN
SEQRES 6 A 73 SER HIS LYS ASN ILE GLN LEU GLY
HELIX 1 A LEU A 2 ALA A 11 1 10
HELIX 2 B ALA A 16 TYR A 27 1 12
HELIX 3 C CYS A 34 ILE A 41 1 8
HELIX 4 D PRO A 45 ALA A 63 1 19
SSBOND 1 CYS A 21 CYS A 47 1555 1555 2.02
SSBOND 2 CYS A 22 CYS A 54 1555 1555 2.03
SSBOND 3 CYS A 34 CYS A 55 1555 1555 2.02
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 - b 16 2 Bytes