Header list of 1eze.pdb file
Complete list - 16 20 Bytes
HEADER TRANSFERASE INHIBITOR 10-MAY-00 1EZE
TITLE STRUCTURAL STUDIES OF A BABOON (PAPIO SP.) PLASMA PROTEIN INHIBITOR OF
TITLE 2 CHOLESTERYL ESTER TRANSFERASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLESTERYL ESTER TRANSFERASE INHIBITOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CETIP, APOLIPOPROTEIN C-I, APO-C1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PEPTIDE OCCURS NATURALLY IN BABOONS (PAPIO SP.)
KEYWDS AMPHIPATHIC HELIX, TRANSFERASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 18
MDLTYP MINIMIZED AVERAGE
AUTHOR G.W.BUCHKO,A.ROZEK,P.KANDA,M.A.KENNEDY,R.J.CUSHLEY
REVDAT 4 16-FEB-22 1EZE 1 REMARK
REVDAT 3 24-FEB-09 1EZE 1 VERSN
REVDAT 2 20-SEP-00 1EZE 1 DBREF
REVDAT 1 13-SEP-00 1EZE 0
JRNL AUTH G.W.BUCHKO,A.ROZEK,P.KANDA,M.A.KENNEDY,R.J.CUSHLEY
JRNL TITL STRUCTURAL STUDIES OF A BABOON (PAPIO SP.) PLASMA PROTEIN
JRNL TITL 2 INHIBITOR OF CHOLESTERYL ESTER TRANSFERASE.
JRNL REF PROTEIN SCI. V. 9 1548 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 10975576
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR V.3.1, X-PLOR V.3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INITIAL ROUNDS OF ITERATION WHERE DONE
REMARK 3 WITH DGII. FINAL STAGES WHERE DONE WITH XPLOR
REMARK 4
REMARK 4 1EZE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011055.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.9
REMARK 210 IONIC STRENGTH : 280 MM SDS
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 280 MM SDS-D25, PH 4.9
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
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 : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 18
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: 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 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 18 ALA A 1 N ALA A 1 CA -0.594
REMARK 500 18 ALA A 1 CA ALA A 1 CB -0.705
REMARK 500 18 ALA A 1 CA ALA A 1 C -0.495
REMARK 500 18 ALA A 1 C ALA A 1 O -0.769
REMARK 500 18 ALA A 1 C PRO A 2 N -0.502
REMARK 500 18 PRO A 2 N PRO A 2 CA -0.436
REMARK 500 18 PRO A 2 CA PRO A 2 CB -0.729
REMARK 500 18 PRO A 2 CB PRO A 2 CG -0.664
REMARK 500 18 PRO A 2 CG PRO A 2 CD -0.384
REMARK 500 18 PRO A 2 CD PRO A 2 N -0.914
REMARK 500 18 PRO A 2 CA PRO A 2 C -0.894
REMARK 500 18 PRO A 2 C PRO A 2 O -0.581
REMARK 500 18 PRO A 2 C ASP A 3 N -0.805
REMARK 500 18 ASP A 3 N ASP A 3 CA -0.858
REMARK 500 18 ASP A 3 CA ASP A 3 CB -0.909
REMARK 500 18 ASP A 3 CB ASP A 3 CG -0.946
REMARK 500 18 ASP A 3 CG ASP A 3 OD1 -1.136
REMARK 500 18 ASP A 3 CG ASP A 3 OD2 -0.914
REMARK 500 18 ASP A 3 CA ASP A 3 C -0.456
REMARK 500 18 ASP A 3 C ASP A 3 O -0.486
REMARK 500 18 ASP A 3 C VAL A 4 N -0.556
REMARK 500 18 VAL A 4 N VAL A 4 CA -0.418
REMARK 500 18 VAL A 4 CA VAL A 4 CB -0.462
REMARK 500 18 VAL A 4 CB VAL A 4 CG1 -0.592
REMARK 500 18 VAL A 4 CB VAL A 4 CG2 -0.632
REMARK 500 18 VAL A 4 CA VAL A 4 C -0.196
REMARK 500 18 VAL A 4 C VAL A 4 O -0.606
REMARK 500 18 VAL A 4 C SER A 5 N -0.522
REMARK 500 18 SER A 5 N SER A 5 CA -0.162
REMARK 500 18 SER A 5 CA SER A 5 CB -0.297
REMARK 500 18 SER A 5 CB SER A 5 OG -0.892
REMARK 500 18 SER A 5 CA SER A 5 C -0.393
REMARK 500 18 SER A 5 C SER A 5 O -0.205
REMARK 500 18 SER A 5 C SER A 6 N -0.328
REMARK 500 18 SER A 6 N SER A 6 CA -0.365
REMARK 500 18 SER A 6 CA SER A 6 CB -0.185
REMARK 500 18 SER A 6 CB SER A 6 OG -0.373
REMARK 500 18 SER A 6 CA SER A 6 C -0.189
REMARK 500 18 SER A 6 C SER A 6 O -0.343
REMARK 500 18 SER A 6 C ALA A 7 N -0.216
REMARK 500 18 ALA A 7 N ALA A 7 CA -0.144
REMARK 500 18 ALA A 7 CA ALA A 7 CB -0.207
REMARK 500 18 ALA A 7 C ALA A 7 O -0.169
REMARK 500 18 ALA A 7 C LEU A 8 N -0.295
REMARK 500 18 LEU A 8 CA LEU A 8 CB -0.188
REMARK 500 18 LEU A 8 CB LEU A 8 CG -0.706
REMARK 500 18 LEU A 8 CG LEU A 8 CD1 -0.578
REMARK 500 18 LEU A 8 CG LEU A 8 CD2 -0.536
REMARK 500 18 ASP A 9 CG ASP A 9 OD1 -0.715
REMARK 500 18 ASP A 9 CG ASP A 9 OD2 -0.659
REMARK 500
REMARK 500 THIS ENTRY HAS 147 BOND DEVIATIONS.
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 18 ALA A 1 CB - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 18 ALA A 1 N - CA - CB ANGL. DEV. = -20.3 DEGREES
REMARK 500 18 ALA A 1 N - CA - C ANGL. DEV. = 20.2 DEGREES
REMARK 500 18 ALA A 1 CA - C - N ANGL. DEV. = 27.1 DEGREES
REMARK 500 18 ALA A 1 O - C - N ANGL. DEV. = -14.5 DEGREES
REMARK 500 18 PRO A 2 C - N - CA ANGL. DEV. = 28.9 DEGREES
REMARK 500 18 PRO A 2 C - N - CD ANGL. DEV. = -23.2 DEGREES
REMARK 500 18 PRO A 2 CB - CA - C ANGL. DEV. = -22.2 DEGREES
REMARK 500 18 PRO A 2 N - CA - CB ANGL. DEV. = 33.0 DEGREES
REMARK 500 18 PRO A 2 CA - CB - CG ANGL. DEV. = -35.9 DEGREES
REMARK 500 18 PRO A 2 CB - CG - CD ANGL. DEV. = 25.1 DEGREES
REMARK 500 18 PRO A 2 N - CD - CG ANGL. DEV. = -10.2 DEGREES
REMARK 500 18 PRO A 2 CA - C - N ANGL. DEV. = -22.4 DEGREES
REMARK 500 18 PRO A 2 O - C - N ANGL. DEV. = 9.6 DEGREES
REMARK 500 18 ASP A 3 C - N - CA ANGL. DEV. = -24.1 DEGREES
REMARK 500 18 ASP A 3 N - CA - CB ANGL. DEV. = -35.2 DEGREES
REMARK 500 18 ASP A 3 CA - CB - CG ANGL. DEV. = -30.5 DEGREES
REMARK 500 18 ASP A 3 OD1 - CG - OD2 ANGL. DEV. = -80.2 DEGREES
REMARK 500 18 ASP A 3 CB - CG - OD1 ANGL. DEV. = 28.9 DEGREES
REMARK 500 18 ASP A 3 CB - CG - OD2 ANGL. DEV. = 51.4 DEGREES
REMARK 500 18 ASP A 3 O - C - N ANGL. DEV. = -11.4 DEGREES
REMARK 500 18 VAL A 4 CA - CB - CG1 ANGL. DEV. = -15.5 DEGREES
REMARK 500 18 VAL A 4 CA - C - O ANGL. DEV. = 14.4 DEGREES
REMARK 500 18 VAL A 4 CA - C - N ANGL. DEV. = 25.5 DEGREES
REMARK 500 18 VAL A 4 O - C - N ANGL. DEV. = -39.9 DEGREES
REMARK 500 18 SER A 5 C - N - CA ANGL. DEV. = 21.9 DEGREES
REMARK 500 18 SER A 6 CA - CB - OG ANGL. DEV. = 18.3 DEGREES
REMARK 500 18 ALA A 7 O - C - N ANGL. DEV. = -9.7 DEGREES
REMARK 500 18 LEU A 8 CA - CB - CG ANGL. DEV. = 22.6 DEGREES
REMARK 500 18 LEU A 8 CB - CG - CD2 ANGL. DEV. = 15.5 DEGREES
REMARK 500 18 ASP A 9 OD1 - CG - OD2 ANGL. DEV. = 100.0 DEGREES
REMARK 500 18 ASP A 9 CB - CG - OD1 ANGL. DEV. = 49.4 DEGREES
REMARK 500 18 ASP A 9 CB - CG - OD2 ANGL. DEV. = 50.6 DEGREES
REMARK 500 18 LYS A 10 CD - CE - NZ ANGL. DEV. = 18.9 DEGREES
REMARK 500 18 LEU A 11 CD1 - CG - CD2 ANGL. DEV. = -85.2 DEGREES
REMARK 500 18 LEU A 11 CB - CG - CD1 ANGL. DEV. = 57.5 DEGREES
REMARK 500 18 LEU A 11 CB - CG - CD2 ANGL. DEV. = 50.9 DEGREES
REMARK 500 18 LYS A 12 CG - CD - CE ANGL. DEV. = 37.0 DEGREES
REMARK 500 18 LYS A 12 CD - CE - NZ ANGL. DEV. = 54.5 DEGREES
REMARK 500 18 GLU A 13 CB - CG - CD ANGL. DEV. = 20.7 DEGREES
REMARK 500 18 GLU A 13 OE1 - CD - OE2 ANGL. DEV. = -90.5 DEGREES
REMARK 500 18 GLU A 13 CG - CD - OE1 ANGL. DEV. = 42.8 DEGREES
REMARK 500 18 GLU A 13 CG - CD - OE2 ANGL. DEV. = 47.8 DEGREES
REMARK 500 18 PHE A 14 CB - CG - CD2 ANGL. DEV. = 26.9 DEGREES
REMARK 500 18 PHE A 14 CD1 - CG - CD2 ANGL. DEV. = -52.6 DEGREES
REMARK 500 18 PHE A 14 CB - CG - CD1 ANGL. DEV. = 25.8 DEGREES
REMARK 500 18 PHE A 14 CG - CD1 - CE1 ANGL. DEV. = 25.8 DEGREES
REMARK 500 18 PHE A 14 CG - CD2 - CE2 ANGL. DEV. = 26.9 DEGREES
REMARK 500 18 PHE A 14 CD1 - CE1 - CZ ANGL. DEV. = 27.5 DEGREES
REMARK 500 18 PHE A 14 CE1 - CZ - CE2 ANGL. DEV. = -54.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 119 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 SER A 5 47.05 -87.99
REMARK 500 1 SER A 6 33.66 162.98
REMARK 500 1 ALA A 7 24.06 -153.82
REMARK 500 1 THR A 17 -131.62 -60.56
REMARK 500 1 LEU A 18 -44.77 -22.78
REMARK 500 1 GLU A 33 0.17 80.16
REMARK 500 1 PHE A 34 62.83 23.05
REMARK 500 1 ALA A 36 95.39 -44.05
REMARK 500 2 SER A 5 40.73 -88.36
REMARK 500 2 SER A 6 39.30 159.69
REMARK 500 2 ALA A 7 24.24 -151.10
REMARK 500 2 THR A 17 -119.24 -57.00
REMARK 500 2 LEU A 18 -32.74 -31.45
REMARK 500 2 PHE A 34 57.17 -141.90
REMARK 500 2 PRO A 35 40.07 -78.68
REMARK 500 2 LYS A 37 -79.75 -54.89
REMARK 500 3 SER A 5 40.88 -88.33
REMARK 500 3 SER A 6 40.22 159.12
REMARK 500 3 ALA A 7 23.35 -150.91
REMARK 500 3 THR A 17 -130.17 -60.16
REMARK 500 3 LEU A 18 -43.03 -24.68
REMARK 500 3 GLU A 33 0.29 80.27
REMARK 500 3 PHE A 34 63.24 23.88
REMARK 500 3 PRO A 35 43.32 -80.98
REMARK 500 3 ALA A 36 45.34 -85.02
REMARK 500 4 VAL A 4 -166.78 40.56
REMARK 500 4 SER A 6 38.55 159.36
REMARK 500 4 ALA A 7 26.47 -166.93
REMARK 500 4 THR A 17 -123.87 -66.46
REMARK 500 4 LEU A 18 -53.26 -15.54
REMARK 500 4 GLU A 33 -16.24 84.00
REMARK 500 4 PHE A 34 62.78 21.82
REMARK 500 4 ALA A 36 75.41 75.94
REMARK 500 4 LYS A 37 -81.03 -53.64
REMARK 500 5 VAL A 4 175.12 -47.95
REMARK 500 5 SER A 6 38.86 156.01
REMARK 500 5 ALA A 7 25.57 -162.64
REMARK 500 5 LEU A 8 20.22 -154.51
REMARK 500 5 THR A 17 -131.47 -60.46
REMARK 500 5 LEU A 18 -44.75 -22.89
REMARK 500 5 GLU A 33 -0.46 80.56
REMARK 500 5 PHE A 34 63.06 23.03
REMARK 500 6 VAL A 4 175.12 -47.95
REMARK 500 6 SER A 6 38.86 156.01
REMARK 500 6 ALA A 7 25.57 -162.64
REMARK 500 6 LEU A 8 20.22 -154.51
REMARK 500 6 THR A 17 -131.47 -60.46
REMARK 500 6 LEU A 18 -44.75 -22.89
REMARK 500 6 GLU A 33 -0.46 80.56
REMARK 500 6 PHE A 34 63.06 23.03
REMARK 500
REMARK 500 THIS ENTRY HAS 142 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 28 0.20 SIDE CHAIN
REMARK 500 2 ARG A 28 0.21 SIDE CHAIN
REMARK 500 3 ARG A 28 0.25 SIDE CHAIN
REMARK 500 4 ARG A 28 0.20 SIDE CHAIN
REMARK 500 5 ARG A 28 0.16 SIDE CHAIN
REMARK 500 6 ARG A 28 0.16 SIDE CHAIN
REMARK 500 7 ARG A 28 0.27 SIDE CHAIN
REMARK 500 8 ARG A 28 0.12 SIDE CHAIN
REMARK 500 9 ARG A 28 0.23 SIDE CHAIN
REMARK 500 10 ARG A 28 0.20 SIDE CHAIN
REMARK 500 11 ARG A 28 0.30 SIDE CHAIN
REMARK 500 12 ARG A 28 0.22 SIDE CHAIN
REMARK 500 13 ARG A 28 0.30 SIDE CHAIN
REMARK 500 14 ARG A 28 0.31 SIDE CHAIN
REMARK 500 15 ARG A 28 0.11 SIDE CHAIN
REMARK 500 16 ARG A 28 0.23 SIDE CHAIN
REMARK 500 17 ARG A 28 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EZE A 1 38 UNP P34929 APOC1_PAPHA 27 64
SEQRES 1 A 38 ALA PRO ASP VAL SER SER ALA LEU ASP LYS LEU LYS GLU
SEQRES 2 A 38 PHE GLY ASN THR LEU GLU ASP LYS ALA TRP GLU VAL ILE
SEQRES 3 A 38 ASN ARG ILE LYS GLN SER GLU PHE PRO ALA LYS THR
HELIX 1 1 PRO A 2 ALA A 7 5 6
HELIX 2 2 LEU A 8 GLY A 15 1 8
HELIX 3 3 ASN A 16 GLN A 31 1 16
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 - 16 20 Bytes