Header list of 1mzi.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 08-OCT-02 1MZI
TITLE SOLUTION ENSEMBLE STRUCTURES OF HIV-1 GP41 2F5 MAB EPITOPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2F5 EPITOPE OF HIV-1 GP41 FUSION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 13 RESIDUES 2F5 EPITOPE;
COMPND 5 SYNONYM: ENVELOPE POLYPROTEIN GP160;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: GP160 HIV-1 HBX2 ISOLATE AMINO ACIDS 659-671
KEYWDS ENSEMBLE, STATISTICS, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 81
AUTHOR G.BARBATO,E.BIANCHI,P.INGALLINELLA,W.H.HURNI,M.D.MILLER,G.CILIBERTO,
AUTHOR 2 R.CORTESE,R.BAZZO,J.W.SHIVER,A.PESSI
REVDAT 3 23-FEB-22 1MZI 1 REMARK
REVDAT 2 24-FEB-09 1MZI 1 VERSN
REVDAT 1 02-SEP-03 1MZI 0
JRNL AUTH G.BARBATO,E.BIANCHI,P.INGALLINELLA,W.H.HURNI,M.D.MILLER,
JRNL AUTH 2 G.CILIBERTO,R.CORTESE,R.BAZZO,J.W.SHIVER,A.PESSI
JRNL TITL STRUCTURAL ANALYSIS OF THE EPITOPE OF THE ANTI-HIV ANTIBODY
JRNL TITL 2 2F5 SHEDS LIGHT INTO ITS MECHANISM OF NEUTRALIZATION AND HIV
JRNL TITL 3 FUSION.
JRNL REF J.MOL.BIOL. V. 330 1101 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12860131
JRNL DOI 10.1016/S0022-2836(03)00611-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.BRUSCHWEILER,M.BLACKLEDGE,R.R.ERNST
REMARK 1 TITL MULTI-CONFORMATIONAL PEPTIDE DYNAMICS DERIVED FROM NMR DATA:
REMARK 1 TITL 2 A NEW SEARCH ALGORITHM AND ITS APPLICATION TO ANTAMANIDE
REMARK 1 REF J.BIOMOL.NMR V. 1 3 1991
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.O.CICERO,G.BARBATO,R.BAZZO
REMARK 1 TITL NMR ANALYSIS OF MOLECULAR FLEXIBILITY IN SOLUTION: A NEW
REMARK 1 TITL 2 METHOD FOR THE STUDY OF COMPLEX DISTRIBUTIONS OF RAPIDLY
REMARK 1 TITL 3 EXCHANGING CONFORMATIONS. APPLICATION TO A 13-RESIDUE
REMARK 1 TITL 4 PEPTIDE WITH AN 8-RESIDUE LOOP
REMARK 1 REF J.AM.CHEM.SOC. V. 117 1027 1995
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.A.KELLEY,S.P.GARDNER,M.J.SUTCLIFFE
REMARK 1 TITL AN AUTOMATED APPROACH FOR CLUSTERING AN ENSEMBLE OF
REMARK 1 TITL 2 NMR-DERIVED PROTEIN STRUCTURES INTO CONFORMATIONALLY RELATED
REMARK 1 TITL 3 SUBFAMILIES
REMARK 1 REF PROTEIN ENG. V. 9 1063 1996
REMARK 1 REFN ISSN 0269-2139
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2001, DGII MSI, NAMFIS 1.0, MEDUSA IN
REMARK 3 HOME, NMRCLUST 1.2
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), MSI, INC (DGII), CICERO D.
REMARK 3 (NAMFIS), BRUSHWEILER R. (MEDUSA), KELLEY
REMARK 3 (NMRCLUST)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MZI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017332.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM PEPTIDE, 50MM PHOSPHATE
REMARK 210 BUFFER, PH 6.5; 1.5MM PEPTIDE,
REMARK 210 50MM PHOSPHATE BUFFER, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; PE-COSY;
REMARK 210 HSQC (1H-13C)-DIPSI-2(1H); HMQC
REMARK 210 (1H-15N) JR
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 2001
REMARK 210 METHOD USED : ENSEMBLE GENERATION WITH MEDUSA,
REMARK 210 CLUSTERING ANALYSIS WITH
REMARK 210 NMRCLUST, STATISTICAL ANALYSIS
REMARK 210 OF THE ENSEMBLE WITH NAMFIS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 6400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 81
REMARK 210 CONFORMERS, SELECTION CRITERIA : BASE SET ENSEMBLE REPRESENTATIVE
REMARK 210 OF THE CONFORMATIONAL SPACE
REMARK 210 EXPERIMENTALLY ALLOWED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: DISTANCE RESTRAINTS WERE DETERMINED USING NOESY BUILD-UP
REMARK 210 CURVES. THE COUPLING CONSTANTS WERE DETERMINED USING PHASE
REMARK 210 SENSITIVE COSY AND TOCSY EXPERIMENTS. E THRESHOLD CUTOFF AND
REMARK 210 DELTAE ALLOWANCE FOR MEDUSA WERE 600 AND 100 KCAL/MOL
REMARK 210 RESPECTIVELY CLUSTERING WAS PERFORMED WITH A CUTOFF OF
REMARK 210 1.0ANGSTROM A CONFORMER WAS DEFINED AS DIFFERENT IF EITHER PHI
REMARK 210 OR PSI ANGLE FOR AT LEAST ONE AMINOACID WAS DIFFERING BY >15
REMARK 210 DEGREES
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 HA ASP A 6 H LYS A 7 1.35
REMARK 500 C ASP A 6 H LYS A 7 1.59
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 1 LYS A 7 N LYS A 7 CA 0.135
REMARK 500 1 ALA A 9 CA ALA A 9 CB 0.207
REMARK 500 4 ALA A 9 CA ALA A 9 CB 0.204
REMARK 500 27 ALA A 9 CA ALA A 9 CB 0.261
REMARK 500 37 ALA A 9 CA ALA A 9 CB 0.222
REMARK 500 49 ALA A 9 CA ALA A 9 CB 0.230
REMARK 500 63 ALA A 9 CA ALA A 9 CB 0.199
REMARK 500 64 ALA A 9 CA ALA A 9 CB 0.194
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 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 ASP A 6 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 4 TRP A 8 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 6 ALA A 9 N - CA - CB ANGL. DEV. = -8.9 DEGREES
REMARK 500 7 LEU A 3 CB - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 7 ASP A 6 N - CA - CB ANGL. DEV. = 21.6 DEGREES
REMARK 500 12 ALA A 9 N - CA - CB ANGL. DEV. = -10.5 DEGREES
REMARK 500 12 SER A 10 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 14 GLU A 1 O - C - N ANGL. DEV. = -9.9 DEGREES
REMARK 500 14 LEU A 2 O - C - N ANGL. DEV. = -11.2 DEGREES
REMARK 500 14 ASP A 6 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 14 TRP A 8 CB - CA - C ANGL. DEV. = 15.0 DEGREES
REMARK 500 14 TRP A 8 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 14 ALA A 9 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 15 TRP A 12 CB - CG - CD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 17 LEU A 11 CA - C - N ANGL. DEV. = 19.5 DEGREES
REMARK 500 17 LEU A 11 O - C - N ANGL. DEV. = -15.7 DEGREES
REMARK 500 18 ALA A 9 N - CA - CB ANGL. DEV. = -9.3 DEGREES
REMARK 500 18 TRP A 12 CB - CA - C ANGL. DEV. = 24.2 DEGREES
REMARK 500 22 GLU A 1 O - C - N ANGL. DEV. = -9.7 DEGREES
REMARK 500 22 TRP A 8 CB - CA - C ANGL. DEV. = 20.2 DEGREES
REMARK 500 22 TRP A 8 CA - CB - CG ANGL. DEV. = 12.7 DEGREES
REMARK 500 22 ALA A 9 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 22 LEU A 11 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 23 ALA A 9 N - CA - CB ANGL. DEV. = -10.5 DEGREES
REMARK 500 24 SER A 10 CB - CA - C ANGL. DEV. = 21.5 DEGREES
REMARK 500 27 TRP A 8 CA - CB - CG ANGL. DEV. = 13.2 DEGREES
REMARK 500 27 TRP A 8 CB - CG - CD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 27 ALA A 9 CB - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 27 LEU A 11 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 27 TRP A 12 CB - CG - CD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 27 TRP A 12 CB - CG - CD1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 27 TRP A 12 CD1 - NE1 - CE2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 28 ALA A 9 N - CA - CB ANGL. DEV. = -9.8 DEGREES
REMARK 500 28 LEU A 11 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 28 LEU A 11 N - CA - C ANGL. DEV. = 18.2 DEGREES
REMARK 500 28 TRP A 12 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 28 TRP A 12 CA - CB - CG ANGL. DEV. = 12.9 DEGREES
REMARK 500 29 TRP A 8 CB - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 29 TRP A 8 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 29 ALA A 9 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 30 LEU A 5 O - C - N ANGL. DEV. = -10.2 DEGREES
REMARK 500 30 ASP A 6 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 30 TRP A 12 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 31 LEU A 3 CB - CA - C ANGL. DEV. = 19.1 DEGREES
REMARK 500 31 LEU A 5 CB - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 31 TRP A 12 CB - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 33 ALA A 9 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 35 LYS A 7 N - CA - C ANGL. DEV. = 19.2 DEGREES
REMARK 500 35 TRP A 8 CB - CA - C ANGL. DEV. = 20.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 91 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 LEU A 2 90.99 53.24
REMARK 500 1 LEU A 3 56.74 25.92
REMARK 500 1 GLU A 4 -61.70 104.70
REMARK 500 1 LEU A 5 86.04 41.03
REMARK 500 1 ASP A 6 93.46 -24.42
REMARK 500 1 LYS A 7 65.28 85.16
REMARK 500 1 TRP A 8 76.81 56.35
REMARK 500 1 ALA A 9 79.03 31.79
REMARK 500 1 SER A 10 -112.12 51.49
REMARK 500 2 SER A 10 -93.47 -78.61
REMARK 500 2 LEU A 11 -146.78 47.05
REMARK 500 3 ASP A 6 -76.60 -174.65
REMARK 500 4 LEU A 3 168.98 54.89
REMARK 500 4 LEU A 5 173.38 66.13
REMARK 500 4 LYS A 7 -133.44 -72.86
REMARK 500 4 ALA A 9 150.66 156.55
REMARK 500 5 LEU A 2 87.44 74.54
REMARK 500 5 GLU A 4 -62.27 -159.60
REMARK 500 5 ASP A 6 -76.78 44.08
REMARK 500 5 ALA A 9 -166.73 66.61
REMARK 500 5 SER A 10 -72.04 75.67
REMARK 500 5 LEU A 11 -30.40 -135.31
REMARK 500 6 LEU A 2 -116.29 -98.44
REMARK 500 6 ASP A 6 86.94 51.08
REMARK 500 6 SER A 10 -51.07 -123.30
REMARK 500 7 LEU A 2 -128.21 -97.45
REMARK 500 7 LEU A 3 -103.01 70.05
REMARK 500 7 GLU A 4 107.73 -30.33
REMARK 500 7 LEU A 5 111.35 22.10
REMARK 500 7 LYS A 7 172.56 -50.89
REMARK 500 7 TRP A 8 -75.67 68.76
REMARK 500 7 ALA A 9 -146.54 -95.15
REMARK 500 7 SER A 10 34.91 -174.04
REMARK 500 8 LYS A 7 -67.88 15.29
REMARK 500 8 TRP A 12 49.48 23.39
REMARK 500 9 ASP A 6 -64.68 -171.68
REMARK 500 9 LYS A 7 -104.07 -151.86
REMARK 500 10 GLU A 4 133.45 62.64
REMARK 500 10 ASP A 6 -76.86 -168.83
REMARK 500 11 ASP A 6 77.79 -169.00
REMARK 500 11 SER A 10 38.71 -95.87
REMARK 500 12 LEU A 3 142.59 74.20
REMARK 500 12 GLU A 4 -67.68 72.77
REMARK 500 12 ASP A 6 -98.57 -109.05
REMARK 500 12 LYS A 7 -156.75 63.78
REMARK 500 12 ALA A 9 -118.07 -93.47
REMARK 500 12 SER A 10 -36.58 37.73
REMARK 500 12 LEU A 11 -100.60 -77.67
REMARK 500 13 LYS A 7 89.74 22.17
REMARK 500 13 TRP A 8 -31.92 60.24
REMARK 500
REMARK 500 THIS ENTRY HAS 417 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 GLU A 4 LEU A 5 1 -102.69
REMARK 500 ASP A 6 LYS A 7 1 146.36
REMARK 500 LEU A 11 TRP A 12 2 130.85
REMARK 500 GLU A 4 LEU A 5 4 -90.34
REMARK 500 ASP A 6 LYS A 7 4 128.75
REMARK 500 LYS A 7 TRP A 8 4 143.40
REMARK 500 LEU A 5 ASP A 6 5 100.37
REMARK 500 LEU A 3 GLU A 4 7 -136.42
REMARK 500 GLU A 4 LEU A 5 7 -131.36
REMARK 500 ASP A 6 LYS A 7 7 141.71
REMARK 500 ALA A 9 SER A 10 7 -149.34
REMARK 500 TRP A 8 ALA A 9 12 142.94
REMARK 500 ALA A 9 SER A 10 12 -146.94
REMARK 500 GLU A 4 LEU A 5 14 123.21
REMARK 500 TRP A 8 ALA A 9 14 137.66
REMARK 500 SER A 10 LEU A 11 14 -125.47
REMARK 500 LEU A 11 TRP A 12 16 -89.75
REMARK 500 SER A 10 LEU A 11 17 -143.97
REMARK 500 LYS A 7 TRP A 8 18 -127.56
REMARK 500 TRP A 12 ASN A 13 20 -149.13
REMARK 500 GLU A 4 LEU A 5 22 142.23
REMARK 500 ASP A 6 LYS A 7 22 -148.60
REMARK 500 SER A 10 LEU A 11 26 -135.54
REMARK 500 GLU A 4 LEU A 5 27 33.33
REMARK 500 ASP A 6 LYS A 7 27 -141.75
REMARK 500 TRP A 8 ALA A 9 27 -147.97
REMARK 500 ALA A 9 SER A 10 27 -149.93
REMARK 500 SER A 10 LEU A 11 27 -137.14
REMARK 500 SER A 10 LEU A 11 28 -142.41
REMARK 500 SER A 10 LEU A 11 29 -142.43
REMARK 500 GLU A 4 LEU A 5 30 -42.65
REMARK 500 ASP A 6 LYS A 7 30 92.56
REMARK 500 SER A 10 LEU A 11 30 -135.49
REMARK 500 TRP A 12 ASN A 13 30 -145.75
REMARK 500 GLU A 4 LEU A 5 31 -139.31
REMARK 500 TRP A 12 ASN A 13 31 -81.99
REMARK 500 LEU A 2 LEU A 3 34 103.20
REMARK 500 LYS A 7 TRP A 8 34 136.88
REMARK 500 LYS A 7 TRP A 8 35 143.42
REMARK 500 TRP A 8 ALA A 9 35 130.43
REMARK 500 GLU A 4 LEU A 5 37 -129.10
REMARK 500 ASP A 6 LYS A 7 37 141.91
REMARK 500 ALA A 9 SER A 10 38 113.78
REMARK 500 SER A 10 LEU A 11 38 -146.98
REMARK 500 LEU A 3 GLU A 4 39 -122.32
REMARK 500 GLU A 4 LEU A 5 39 -60.87
REMARK 500 ASP A 6 LYS A 7 39 -123.23
REMARK 500 LYS A 7 TRP A 8 39 95.15
REMARK 500 LEU A 11 TRP A 12 40 123.50
REMARK 500 TRP A 8 ALA A 9 41 122.39
REMARK 500
REMARK 500 THIS ENTRY HAS 105 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 17 ASN A 13 0.07 SIDE CHAIN
REMARK 500 22 ASN A 13 0.08 SIDE CHAIN
REMARK 500 29 ASN A 13 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MZI A 1 13 UNP P04578 ENV_HV1H2 659 671
SEQRES 1 A 13 GLU LEU LEU GLU LEU ASP LYS TRP ALA SER LEU TRP ASN
CISPEP 1 GLU A 1 LEU A 2 5 -2.33
CISPEP 2 LEU A 2 LEU A 3 5 -29.47
CISPEP 3 TRP A 8 ALA A 9 5 -26.51
CISPEP 4 TRP A 12 ASN A 13 5 2.98
CISPEP 5 TRP A 12 ASN A 13 6 -10.71
CISPEP 6 GLU A 1 LEU A 2 7 -11.32
CISPEP 7 GLU A 1 LEU A 2 14 4.72
CISPEP 8 LEU A 2 LEU A 3 14 -2.80
CISPEP 9 LEU A 11 TRP A 12 17 9.49
CISPEP 10 GLU A 1 LEU A 2 22 0.17
CISPEP 11 LEU A 2 LEU A 3 22 22.40
CISPEP 12 TRP A 12 ASN A 13 22 -12.31
CISPEP 13 LEU A 5 ASP A 6 30 4.22
CISPEP 14 GLU A 4 LEU A 5 32 27.92
CISPEP 15 GLU A 4 LEU A 5 34 -12.66
CISPEP 16 GLU A 1 LEU A 2 35 0.75
CISPEP 17 LEU A 2 LEU A 3 35 9.69
CISPEP 18 GLU A 1 LEU A 2 39 -12.44
CISPEP 19 LEU A 2 LEU A 3 39 0.00
CISPEP 20 GLU A 1 LEU A 2 42 4.87
CISPEP 21 GLU A 1 LEU A 2 43 1.11
CISPEP 22 LEU A 2 LEU A 3 43 21.58
CISPEP 23 GLU A 4 LEU A 5 44 -28.20
CISPEP 24 LEU A 2 LEU A 3 48 -2.16
CISPEP 25 GLU A 1 LEU A 2 51 -4.71
CISPEP 26 LEU A 2 LEU A 3 51 21.97
CISPEP 27 GLU A 4 LEU A 5 52 17.95
CISPEP 28 GLU A 4 LEU A 5 53 -13.55
CISPEP 29 GLU A 1 LEU A 2 54 0.92
CISPEP 30 LEU A 2 LEU A 3 54 1.15
CISPEP 31 ASP A 6 LYS A 7 54 4.13
CISPEP 32 TRP A 12 ASN A 13 55 -29.53
CISPEP 33 LEU A 11 TRP A 12 57 17.09
CISPEP 34 GLU A 4 LEU A 5 59 -6.98
CISPEP 35 LEU A 2 LEU A 3 60 -10.52
CISPEP 36 LEU A 2 LEU A 3 66 -3.25
CISPEP 37 TRP A 12 ASN A 13 66 -1.62
CISPEP 38 GLU A 1 LEU A 2 67 0.31
CISPEP 39 LEU A 2 LEU A 3 67 8.80
CISPEP 40 LEU A 2 LEU A 3 72 8.23
CISPEP 41 GLU A 1 LEU A 2 73 -1.97
CISPEP 42 GLU A 1 LEU A 2 75 -1.36
CISPEP 43 LEU A 2 LEU A 3 75 13.53
CISPEP 44 GLU A 1 LEU A 2 76 -0.97
CISPEP 45 LEU A 2 LEU A 3 76 14.07
CISPEP 46 LEU A 11 TRP A 12 77 2.34
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 23 2 Bytes