Header list of 1lv4.pdb file
Complete list - 23 20 Bytes
HEADER SIGNALING PROTEIN 24-MAY-02 1LV4
TITLE HUMAN CATESTATIN 21-MER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATESTATIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 370-390;
COMPND 5 SYNONYM: CHROMOGRANIN A;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID-PHASE SYNTHESIS. THE SEQUENCE OF THE PROTEIN IS
SOURCE 4 NATURALLY FOUND IN HOMO SAPIENS.
KEYWDS GLYCOPROTEIN, AMIDATION, PHOSPHORYLATION, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR D.T.O'CONNOR,N.E.PREECE
REVDAT 4 23-FEB-22 1LV4 1 REMARK
REVDAT 3 24-FEB-09 1LV4 1 VERSN
REVDAT 2 15-FEB-05 1LV4 1 JRNL
REVDAT 1 19-JUN-02 1LV4 0
JRNL AUTH N.E.PREECE,M.NGUYEN,M.MAHATA,S.K.MAHATA,N.R.MAHAPATRA,
JRNL AUTH 2 I.TSIGELNY,D.T.O'CONNOR
JRNL TITL CONFORMATIONAL PREFERENCES AND ACTIVITIES OF PEPTIDES FROM
JRNL TITL 2 THE CATECHOLAMINE RELEASE-INHIBITORY (CATESTATIN) REGION OF
JRNL TITL 3 CHROMOGRANIN A.
JRNL REF REGUL.PEPT. V. 118 75 2004
JRNL REFN ISSN 0167-0115
JRNL PMID 14759560
JRNL DOI 10.1016/J.REGPEP.2003.10.035
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.3F, NMRARCHITECHT
REMARK 3 AUTHORS : VARIAN (VNMR), MSI (NMRARCHITECHT)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LV4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000016303.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.9
REMARK 210 IONIC STRENGTH : 6.4 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : LINEAR CATESTATIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, DISCOVER C
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 LEU A 21 C LEU A 21 OXT 0.141
REMARK 500 2 LEU A 21 C LEU A 21 OXT 0.141
REMARK 500 3 LEU A 21 C LEU A 21 OXT 0.142
REMARK 500 4 LEU A 21 C LEU A 21 OXT 0.143
REMARK 500 5 LEU A 21 C LEU A 21 OXT 0.146
REMARK 500 6 LEU A 21 C LEU A 21 OXT 0.140
REMARK 500 7 LEU A 21 C LEU A 21 OXT 0.141
REMARK 500 8 LEU A 21 C LEU A 21 OXT 0.145
REMARK 500 9 LEU A 21 C LEU A 21 OXT 0.144
REMARK 500 10 LEU A 21 C LEU A 21 OXT 0.143
REMARK 500 11 LEU A 21 C LEU A 21 OXT 0.143
REMARK 500 12 LEU A 21 C LEU A 21 OXT 0.146
REMARK 500 13 LEU A 21 C LEU A 21 OXT 0.143
REMARK 500 14 LEU A 21 C LEU A 21 OXT 0.145
REMARK 500 15 LEU A 21 C LEU A 21 OXT 0.143
REMARK 500 16 LEU A 21 C LEU A 21 OXT 0.145
REMARK 500 17 LEU A 21 C LEU A 21 OXT 0.140
REMARK 500 18 LEU A 21 C LEU A 21 OXT 0.142
REMARK 500 19 LEU A 21 C LEU A 21 OXT 0.141
REMARK 500 20 LEU A 21 C LEU A 21 OXT 0.141
REMARK 500 21 LEU A 21 C LEU A 21 OXT 0.140
REMARK 500 22 LEU A 21 C LEU A 21 OXT 0.142
REMARK 500 23 LEU A 21 C LEU A 21 OXT 0.140
REMARK 500 24 LEU A 21 C LEU A 21 OXT 0.141
REMARK 500 25 LEU A 21 C LEU A 21 OXT 0.140
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. = 5.8 DEGREES
REMARK 500 1 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 1 ALA A 9 CB - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 1 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 1 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 1 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 ALA A 9 CB - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 2 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 2 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 SER A 6 O - C - N ANGL. DEV. = -10.9 DEGREES
REMARK 500 3 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 3 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 3 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 3 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 ALA A 11 CA - C - N ANGL. DEV. = 15.0 DEGREES
REMARK 500 3 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 3 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 4 PHE A 7 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 4 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 4 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 4 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 4 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 4 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 4 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 5 PHE A 7 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 5 PHE A 7 CB - CG - CD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 5 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 5 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 5 ARG A 10 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 5 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 5 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 5 TYR A 12 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 5 TYR A 12 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 5 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 5 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 5 GLN A 20 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 6 LYS A 4 CA - C - N ANGL. DEV. = 14.0 DEGREES
REMARK 500 6 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 6 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 6 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 6 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 6 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 6 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 7 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 7 ARG A 8 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 186 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 MET A 3 43.14 35.21
REMARK 500 1 SER A 6 81.71 -155.11
REMARK 500 1 ALA A 9 -157.48 -89.98
REMARK 500 1 ALA A 11 -20.21 -142.43
REMARK 500 2 LEU A 5 -75.88 -145.15
REMARK 500 2 ARG A 8 -9.14 -23.17
REMARK 500 2 ALA A 9 -142.88 -82.02
REMARK 500 2 ARG A 10 -39.67 -168.88
REMARK 500 2 ALA A 11 -15.76 -143.10
REMARK 500 2 TYR A 12 -60.92 -135.51
REMARK 500 2 ARG A 15 -68.16 -151.66
REMARK 500 3 SER A 2 113.41 49.20
REMARK 500 3 MET A 3 119.53 46.56
REMARK 500 3 LYS A 4 89.51 68.63
REMARK 500 3 SER A 6 57.13 -156.57
REMARK 500 3 ARG A 8 -44.29 -16.80
REMARK 500 3 ALA A 9 83.40 18.00
REMARK 500 3 ARG A 10 -70.63 46.35
REMARK 500 3 ALA A 11 -73.65 -112.40
REMARK 500 3 ARG A 15 -26.80 -179.47
REMARK 500 3 GLN A 20 -41.46 72.87
REMARK 500 4 SER A 2 89.21 66.33
REMARK 500 4 LEU A 5 -64.55 -135.60
REMARK 500 4 PHE A 7 -101.22 -102.93
REMARK 500 4 ARG A 8 -59.93 -136.27
REMARK 500 4 TYR A 12 73.75 49.66
REMARK 500 4 PHE A 14 14.49 -143.72
REMARK 500 4 ARG A 15 -59.91 -139.78
REMARK 500 5 LEU A 5 -76.93 -151.17
REMARK 500 5 ARG A 10 -69.06 92.02
REMARK 500 5 ALA A 11 -38.56 -135.87
REMARK 500 5 TYR A 12 88.65 88.74
REMARK 500 5 PHE A 14 -55.78 -166.01
REMARK 500 5 GLN A 20 -50.59 165.29
REMARK 500 6 SER A 2 93.94 57.17
REMARK 500 6 MET A 3 127.16 59.23
REMARK 500 6 LYS A 4 -56.13 -153.99
REMARK 500 6 LEU A 5 -87.34 -105.92
REMARK 500 6 SER A 6 67.49 23.35
REMARK 500 6 PHE A 7 -121.22 -123.61
REMARK 500 6 ARG A 8 0.76 -158.24
REMARK 500 6 ARG A 10 -57.98 -158.55
REMARK 500 6 TYR A 12 -64.94 -153.18
REMARK 500 6 ARG A 15 89.53 -150.55
REMARK 500 7 LYS A 4 87.00 66.48
REMARK 500 7 SER A 6 88.34 63.91
REMARK 500 7 PHE A 7 -88.64 -111.44
REMARK 500 7 ARG A 8 -58.50 -155.80
REMARK 500 7 ARG A 10 -34.40 -155.65
REMARK 500 7 TYR A 12 -47.43 -136.27
REMARK 500
REMARK 500 THIS ENTRY HAS 192 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 LEU A 5 SER A 6 1 147.74
REMARK 500 ALA A 9 ARG A 10 1 -145.37
REMARK 500 PHE A 14 ARG A 15 1 -133.17
REMARK 500 GLN A 20 LEU A 21 1 141.99
REMARK 500 LEU A 5 SER A 6 2 123.28
REMARK 500 PHE A 7 ARG A 8 2 146.74
REMARK 500 ARG A 8 ALA A 9 2 -85.55
REMARK 500 ALA A 9 ARG A 10 2 -127.16
REMARK 500 ARG A 10 ALA A 11 2 -130.54
REMARK 500 GLY A 13 PHE A 14 2 -147.42
REMARK 500 LEU A 5 SER A 6 3 149.10
REMARK 500 ALA A 9 ARG A 10 3 114.86
REMARK 500 ARG A 10 ALA A 11 3 -144.91
REMARK 500 GLY A 13 PHE A 14 3 -81.98
REMARK 500 ALA A 9 ARG A 10 4 -148.04
REMARK 500 PHE A 14 ARG A 15 4 -127.45
REMARK 500 ARG A 8 ALA A 9 5 145.84
REMARK 500 ARG A 8 ALA A 9 6 -121.98
REMARK 500 ALA A 9 ARG A 10 6 -125.02
REMARK 500 GLY A 13 PHE A 14 6 -129.43
REMARK 500 ALA A 9 ARG A 10 7 -139.41
REMARK 500 PHE A 14 ARG A 15 7 -138.24
REMARK 500 PHE A 7 ARG A 8 8 -132.38
REMARK 500 ALA A 9 ARG A 10 8 -148.03
REMARK 500 GLY A 13 PHE A 14 8 -139.63
REMARK 500 PHE A 14 ARG A 15 8 -141.61
REMARK 500 ARG A 8 ALA A 9 9 -91.29
REMARK 500 ALA A 11 TYR A 12 9 -38.80
REMARK 500 PHE A 14 ARG A 15 10 -140.01
REMARK 500 ALA A 9 ARG A 10 11 -142.54
REMARK 500 ARG A 8 ALA A 9 12 -83.03
REMARK 500 ALA A 9 ARG A 10 12 -105.34
REMARK 500 PHE A 14 ARG A 15 12 -146.08
REMARK 500 ARG A 8 ALA A 9 13 98.87
REMARK 500 ALA A 11 TYR A 12 13 -33.59
REMARK 500 PHE A 14 ARG A 15 13 -125.55
REMARK 500 LYS A 4 LEU A 5 14 -146.15
REMARK 500 ALA A 9 ARG A 10 14 -140.87
REMARK 500 PHE A 14 ARG A 15 14 -134.50
REMARK 500 LEU A 5 SER A 6 15 147.04
REMARK 500 PHE A 7 ARG A 8 15 98.39
REMARK 500 ARG A 8 ALA A 9 15 -149.90
REMARK 500 ALA A 11 TYR A 12 15 145.87
REMARK 500 ALA A 9 ARG A 10 16 -114.80
REMARK 500 ARG A 10 ALA A 11 16 109.59
REMARK 500 GLY A 13 PHE A 14 16 -145.59
REMARK 500 PHE A 14 ARG A 15 16 -144.37
REMARK 500 LEU A 5 SER A 6 17 148.58
REMARK 500 PHE A 7 ARG A 8 17 -142.24
REMARK 500 ALA A 9 ARG A 10 17 83.89
REMARK 500
REMARK 500 THIS ENTRY HAS 78 NON CIS, NON-TRANS OMEGA 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 PHE A 14 0.21 SIDE CHAIN
REMARK 500 2 PHE A 14 0.18 SIDE CHAIN
REMARK 500 3 PHE A 14 0.10 SIDE CHAIN
REMARK 500 4 PHE A 14 0.13 SIDE CHAIN
REMARK 500 5 PHE A 14 0.14 SIDE CHAIN
REMARK 500 6 PHE A 14 0.15 SIDE CHAIN
REMARK 500 7 PHE A 14 0.22 SIDE CHAIN
REMARK 500 8 PHE A 14 0.21 SIDE CHAIN
REMARK 500 9 PHE A 14 0.14 SIDE CHAIN
REMARK 500 10 ARG A 10 0.07 SIDE CHAIN
REMARK 500 10 PHE A 14 0.18 SIDE CHAIN
REMARK 500 11 PHE A 14 0.17 SIDE CHAIN
REMARK 500 12 PHE A 14 0.11 SIDE CHAIN
REMARK 500 13 PHE A 14 0.18 SIDE CHAIN
REMARK 500 14 PHE A 14 0.12 SIDE CHAIN
REMARK 500 15 PHE A 14 0.22 SIDE CHAIN
REMARK 500 16 TYR A 12 0.08 SIDE CHAIN
REMARK 500 16 PHE A 14 0.13 SIDE CHAIN
REMARK 500 17 PHE A 14 0.10 SIDE CHAIN
REMARK 500 18 PHE A 14 0.13 SIDE CHAIN
REMARK 500 19 PHE A 14 0.12 SIDE CHAIN
REMARK 500 20 PHE A 14 0.17 SIDE CHAIN
REMARK 500 21 PHE A 14 0.15 SIDE CHAIN
REMARK 500 22 PHE A 14 0.17 SIDE CHAIN
REMARK 500 23 PHE A 14 0.12 SIDE CHAIN
REMARK 500 24 PHE A 14 0.21 SIDE CHAIN
REMARK 500 25 TYR A 12 0.08 SIDE CHAIN
REMARK 500 25 PHE A 14 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CFK RELATED DB: PDB
REMARK 900 HOMOLOGY MODEL
REMARK 900 RELATED ID: 1KRK RELATED DB: PDB
REMARK 900 CYCLIC VERSION
DBREF 1LV4 A 1 21 UNP P10645 CMGA_HUMAN 370 390
SEQRES 1 A 21 SER SER MET LYS LEU SER PHE ARG ALA ARG ALA TYR GLY
SEQRES 2 A 21 PHE ARG GLY PRO GLY PRO GLN LEU
CISPEP 1 ARG A 8 ALA A 9 1 -15.23
CISPEP 2 GLY A 16 PRO A 17 1 5.09
CISPEP 3 PRO A 19 GLN A 20 1 -0.39
CISPEP 4 SER A 2 MET A 3 2 -5.40
CISPEP 5 SER A 6 PHE A 7 2 -6.73
CISPEP 6 GLY A 16 PRO A 17 2 13.74
CISPEP 7 GLY A 18 PRO A 19 2 13.52
CISPEP 8 PRO A 19 GLN A 20 2 -7.19
CISPEP 9 LYS A 4 LEU A 5 3 -4.03
CISPEP 10 SER A 6 PHE A 7 3 4.63
CISPEP 11 ALA A 11 TYR A 12 3 -6.58
CISPEP 12 GLY A 16 PRO A 17 3 12.78
CISPEP 13 GLY A 18 PRO A 19 3 -9.96
CISPEP 14 MET A 3 LYS A 4 4 -9.42
CISPEP 15 ARG A 8 ALA A 9 4 -6.25
CISPEP 16 TYR A 12 GLY A 13 4 10.86
CISPEP 17 GLY A 16 PRO A 17 4 -3.07
CISPEP 18 GLY A 18 PRO A 19 4 -3.59
CISPEP 19 PRO A 19 GLN A 20 4 -6.90
CISPEP 20 PHE A 7 ARG A 8 5 12.28
CISPEP 21 ALA A 9 ARG A 10 5 1.39
CISPEP 22 GLY A 16 PRO A 17 5 6.20
CISPEP 23 GLY A 18 PRO A 19 5 1.87
CISPEP 24 LYS A 4 LEU A 5 6 7.59
CISPEP 25 PHE A 14 ARG A 15 6 18.77
CISPEP 26 GLY A 16 PRO A 17 6 3.20
CISPEP 27 GLY A 18 PRO A 19 6 1.54
CISPEP 28 PRO A 19 GLN A 20 6 14.80
CISPEP 29 SER A 2 MET A 3 7 -9.09
CISPEP 30 ARG A 8 ALA A 9 7 3.30
CISPEP 31 GLY A 16 PRO A 17 7 2.63
CISPEP 32 GLY A 18 PRO A 19 7 8.31
CISPEP 33 PRO A 19 GLN A 20 7 -6.53
CISPEP 34 MET A 3 LYS A 4 8 12.97
CISPEP 35 LYS A 4 LEU A 5 8 5.83
CISPEP 36 GLY A 16 PRO A 17 8 5.18
CISPEP 37 GLY A 18 PRO A 19 8 3.96
CISPEP 38 PRO A 19 GLN A 20 8 5.60
CISPEP 39 MET A 3 LYS A 4 9 -11.96
CISPEP 40 PHE A 7 ARG A 8 9 -8.41
CISPEP 41 ALA A 9 ARG A 10 9 -12.48
CISPEP 42 GLY A 13 PHE A 14 9 11.53
CISPEP 43 GLY A 16 PRO A 17 9 13.43
CISPEP 44 GLY A 18 PRO A 19 9 6.11
CISPEP 45 MET A 3 LYS A 4 10 -4.99
CISPEP 46 SER A 6 PHE A 7 10 -2.06
CISPEP 47 ARG A 8 ALA A 9 10 -6.43
CISPEP 48 PRO A 17 GLY A 18 10 4.13
CISPEP 49 GLY A 18 PRO A 19 10 -5.16
CISPEP 50 PRO A 19 GLN A 20 10 -10.30
CISPEP 51 SER A 6 PHE A 7 11 -9.39
CISPEP 52 ARG A 8 ALA A 9 11 2.94
CISPEP 53 TYR A 12 GLY A 13 11 -3.31
CISPEP 54 GLY A 16 PRO A 17 11 2.73
CISPEP 55 PRO A 19 GLN A 20 11 19.13
CISPEP 56 MET A 3 LYS A 4 12 -18.23
CISPEP 57 SER A 6 PHE A 7 12 -0.58
CISPEP 58 TYR A 12 GLY A 13 12 -12.99
CISPEP 59 GLY A 16 PRO A 17 12 -7.53
CISPEP 60 PRO A 17 GLY A 18 12 1.23
CISPEP 61 GLY A 18 PRO A 19 12 -1.50
CISPEP 62 PRO A 19 GLN A 20 12 2.71
CISPEP 63 MET A 3 LYS A 4 13 16.07
CISPEP 64 LYS A 4 LEU A 5 13 -11.05
CISPEP 65 SER A 6 PHE A 7 13 7.60
CISPEP 66 ALA A 9 ARG A 10 13 -8.81
CISPEP 67 GLY A 16 PRO A 17 13 8.06
CISPEP 68 GLY A 18 PRO A 19 13 6.43
CISPEP 69 SER A 2 MET A 3 14 12.65
CISPEP 70 ARG A 8 ALA A 9 14 0.73
CISPEP 71 GLY A 16 PRO A 17 14 7.08
CISPEP 72 GLY A 18 PRO A 19 14 8.60
CISPEP 73 PRO A 19 GLN A 20 14 -4.14
CISPEP 74 SER A 6 PHE A 7 15 -17.96
CISPEP 75 ALA A 9 ARG A 10 15 4.53
CISPEP 76 GLY A 16 PRO A 17 15 12.13
CISPEP 77 GLY A 18 PRO A 19 15 10.44
CISPEP 78 PRO A 19 GLN A 20 15 0.35
CISPEP 79 PHE A 7 ARG A 8 16 13.64
CISPEP 80 ARG A 8 ALA A 9 16 -19.48
CISPEP 81 ALA A 11 TYR A 12 16 -7.77
CISPEP 82 GLY A 16 PRO A 17 16 16.16
CISPEP 83 GLY A 18 PRO A 19 16 4.28
CISPEP 84 SER A 6 PHE A 7 17 11.01
CISPEP 85 ALA A 11 TYR A 12 17 -5.66
CISPEP 86 GLY A 16 PRO A 17 17 -2.37
CISPEP 87 PHE A 7 ARG A 8 18 11.83
CISPEP 88 ALA A 11 TYR A 12 18 11.00
CISPEP 89 GLY A 16 PRO A 17 18 -0.47
CISPEP 90 SER A 6 PHE A 7 19 6.01
CISPEP 91 PHE A 7 ARG A 8 19 10.51
CISPEP 92 GLY A 16 PRO A 17 19 0.78
CISPEP 93 GLY A 18 PRO A 19 19 5.89
CISPEP 94 LYS A 4 LEU A 5 20 -9.38
CISPEP 95 LEU A 5 SER A 6 20 -8.52
CISPEP 96 TYR A 12 GLY A 13 20 -5.69
CISPEP 97 PHE A 14 ARG A 15 20 -8.68
CISPEP 98 GLY A 16 PRO A 17 20 4.17
CISPEP 99 GLY A 18 PRO A 19 20 27.13
CISPEP 100 GLY A 16 PRO A 17 21 4.38
CISPEP 101 GLY A 18 PRO A 19 21 10.19
CISPEP 102 LYS A 4 LEU A 5 22 -3.01
CISPEP 103 ALA A 9 ARG A 10 22 -22.99
CISPEP 104 GLY A 16 PRO A 17 22 14.01
CISPEP 105 GLY A 18 PRO A 19 22 -8.84
CISPEP 106 PRO A 19 GLN A 20 22 -2.62
CISPEP 107 LYS A 4 LEU A 5 23 14.55
CISPEP 108 LEU A 5 SER A 6 23 -17.56
CISPEP 109 SER A 6 PHE A 7 23 5.72
CISPEP 110 ALA A 9 ARG A 10 23 -23.87
CISPEP 111 GLY A 16 PRO A 17 23 6.58
CISPEP 112 GLY A 18 PRO A 19 23 3.29
CISPEP 113 PRO A 19 GLN A 20 23 17.50
CISPEP 114 SER A 6 PHE A 7 24 -10.35
CISPEP 115 PHE A 7 ARG A 8 24 2.77
CISPEP 116 TYR A 12 GLY A 13 24 -5.92
CISPEP 117 GLY A 16 PRO A 17 24 -1.19
CISPEP 118 PRO A 17 GLY A 18 24 9.25
CISPEP 119 GLY A 18 PRO A 19 24 -6.18
CISPEP 120 PRO A 19 GLN A 20 24 -0.22
CISPEP 121 LYS A 4 LEU A 5 25 -10.10
CISPEP 122 SER A 6 PHE A 7 25 14.22
CISPEP 123 PHE A 7 ARG A 8 25 3.61
CISPEP 124 ARG A 8 ALA A 9 25 -10.15
CISPEP 125 GLY A 16 PRO A 17 25 8.68
CISPEP 126 GLY A 18 PRO A 19 25 0.42
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 - 23 20 Bytes