Header list of 2aih.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 29-JUL-05 2AIH
TITLE 1H-NMR SOLUTION STRUCTURE OF A TRYPSIN/CHYMOTRYPSIN BOWMAN-BIRK
TITLE 2 INHIBITOR FROM LENS CULINARIS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOWMAN-BIRK TYPE PROTEASE INHIBITOR, LCTI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 43-109;
COMPND 5 SYNONYM: TRYPSIN/CHYMOTRYPSIN INHIBITOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LENS CULINARIS;
SOURCE 3 ORGANISM_COMMON: LENTIL;
SOURCE 4 ORGANISM_TAXID: 3864;
SOURCE 5 STRAIN: MACROSPERMA GROUP;
SOURCE 6 TISSUE: SEEDS
KEYWDS TRYPSIN/CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR, TWO-STRANDS BETA-SHEET,
KEYWDS 2 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.M.RAGG,V.GALBUSERA,A.SCARAFONI,A.NEGRI,G.TEDESCHI,A.CONSONNI,
AUTHOR 2 F.SESSA,M.DURANTI
REVDAT 4 09-MAR-22 2AIH 1 REMARK
REVDAT 3 24-FEB-09 2AIH 1 VERSN
REVDAT 2 12-SEP-06 2AIH 1 JRNL
REVDAT 1 01-AUG-06 2AIH 0
JRNL AUTH E.M.RAGG,V.GALBUSERA,A.SCARAFONI,A.NEGRI,G.TEDESCHI,
JRNL AUTH 2 A.CONSONNI,F.SESSA,M.DURANTI
JRNL TITL INHIBITORY PROPERTIES AND SOLUTION STRUCTURE OF A POTENT
JRNL TITL 2 BOWMAN-BIRK PROTEASE INHIBITOR FROM LENTIL (LENS CULINARIS,
JRNL TITL 3 L) SEEDS.
JRNL REF FEBS J. V. 273 4024 2006
JRNL REFN ISSN 1742-464X
JRNL PMID 16889634
JRNL DOI 10.1111/J.1742-4658.2006.05406.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1851
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2745 RESTRAINTS, OF WHICH
REMARK 3 632 ARE NOE-DERIVED DISTANCE CONSTRAINTS FOR THE INITIAL STAGE OF
REMARK 3 SIMULATED ANNEALING,
REMARK 3 2068 ARE NOESY-DERIVED CROSS-PEAK VOLUMES FOR FINAL REFINEMENT,
REMARK 3 29 VICINAL COUPLING CONSTANTS RESTRAINTS,
REMARK 3 16 DISTANCE RESTRAINTS
REMARK 3 FOR HYDROGEN BOND DEFINITIONS; THE CHLORIDE ATOMS AT THE END OF
REMARK 3 EACH MODEL WERE ADDED DURING THE REFINEMENT STAGE OF RESTRAINED
REMARK 3 ENERGY MINIMIZATION TO REDUCE OVERALL CHARGE. POSITIONS ARE NOT
REMARK 3 EXPERIMENTALLY DETERMINED BUT ARE A RESULT OF CALCULATIONS
REMARK 4
REMARK 4 2AIH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000033933.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288; 293; 298; 303; 298
REMARK 210 PH : 3.0; 3.0; 3.0; 3.0; 4.2
REMARK 210 IONIC STRENGTH : 3 MM; 3 MM; 3 MM; 3 MM; 5 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM LCTI, UNBUFFERED SOLUTION,
REMARK 210 90% H2O, 10% D2O; 1 MM LCTI,
REMARK 210 UNBUFFERED SOLUTION, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY
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 : XWINNMR 2.6, SPARKY 3.106, X
REMARK 210 -PLOR 3.1851
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS MATRIX RELAXATION
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 52
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NOESY EXPERIMENTS WERE PERFORMED AT 298 K AT THREE
REMARK 210 DIFFERENT MIXING TIMES (0.080S, 0.120S, 0.350S) FOR DISTANCE
REMARK 210 RESTRAINTS CALCULATIONS AND CROSS-PEAK VOLUME MEASUREMENTS
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 GLU A 29 CD GLU A 29 OE2 0.118
REMARK 500 1 GLU A 65 CD GLU A 65 OE2 0.121
REMARK 500 1 GLU A 67 CD GLU A 67 OE2 0.125
REMARK 500 2 GLU A 29 CD GLU A 29 OE2 0.122
REMARK 500 2 GLU A 65 CD GLU A 65 OE2 0.120
REMARK 500 2 GLU A 67 CD GLU A 67 OE2 0.135
REMARK 500 3 GLU A 29 CD GLU A 29 OE2 0.117
REMARK 500 3 GLU A 65 CD GLU A 65 OE2 0.122
REMARK 500 3 GLU A 67 CD GLU A 67 OE2 0.123
REMARK 500 3 GLU A 67 C GLU A 67 O 0.143
REMARK 500 4 GLU A 29 CD GLU A 29 OE2 0.118
REMARK 500 4 GLU A 65 CD GLU A 65 OE2 0.116
REMARK 500 4 GLU A 67 CD GLU A 67 OE2 0.125
REMARK 500 5 GLU A 29 CD GLU A 29 OE2 0.115
REMARK 500 5 GLU A 65 CD GLU A 65 OE2 0.128
REMARK 500 5 GLU A 67 CD GLU A 67 OE2 0.129
REMARK 500 6 GLU A 29 CD GLU A 29 OE2 0.109
REMARK 500 6 GLU A 65 CD GLU A 65 OE2 0.111
REMARK 500 6 GLU A 67 CD GLU A 67 OE2 0.123
REMARK 500 7 GLU A 29 CD GLU A 29 OE2 0.119
REMARK 500 7 GLU A 65 CD GLU A 65 OE2 0.114
REMARK 500 7 GLU A 67 CD GLU A 67 OE2 0.126
REMARK 500 8 GLU A 29 CD GLU A 29 OE2 0.118
REMARK 500 8 GLU A 65 CD GLU A 65 OE2 0.117
REMARK 500 8 GLU A 67 CD GLU A 67 OE2 0.126
REMARK 500 9 GLU A 29 CD GLU A 29 OE2 0.117
REMARK 500 9 GLU A 65 CD GLU A 65 OE2 0.118
REMARK 500 9 GLU A 67 CD GLU A 67 OE2 0.128
REMARK 500 10 GLU A 29 CD GLU A 29 OE2 0.122
REMARK 500 10 GLU A 65 CD GLU A 65 OE2 0.119
REMARK 500 10 GLU A 67 CD GLU A 67 OE2 0.126
REMARK 500 11 GLU A 29 CD GLU A 29 OE2 0.122
REMARK 500 11 GLU A 65 CD GLU A 65 OE2 0.117
REMARK 500 11 GLU A 67 CD GLU A 67 OE2 0.133
REMARK 500 12 GLU A 29 CD GLU A 29 OE2 0.123
REMARK 500 12 GLU A 65 CD GLU A 65 OE2 0.107
REMARK 500 12 GLU A 67 CD GLU A 67 OE2 0.134
REMARK 500 13 GLU A 29 CD GLU A 29 OE2 0.127
REMARK 500 13 GLU A 65 CD GLU A 65 OE2 0.112
REMARK 500 13 GLU A 67 CD GLU A 67 OE2 0.126
REMARK 500 14 GLU A 29 CD GLU A 29 OE2 0.118
REMARK 500 14 GLU A 65 CD GLU A 65 OE2 0.118
REMARK 500 14 GLU A 67 CD GLU A 67 OE2 0.128
REMARK 500 15 GLU A 29 CD GLU A 29 OE2 0.118
REMARK 500 15 GLU A 65 CD GLU A 65 OE2 0.120
REMARK 500 15 GLU A 67 CD GLU A 67 OE2 0.129
REMARK 500 16 GLU A 29 CD GLU A 29 OE2 0.113
REMARK 500 16 GLU A 65 CD GLU A 65 OE2 0.121
REMARK 500 16 GLU A 67 CD GLU A 67 OE2 0.126
REMARK 500 17 GLU A 29 CD GLU A 29 OE2 0.123
REMARK 500
REMARK 500 THIS ENTRY HAS 62 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 1 ASP A 2 CB - CG - OD1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 ASP A 2 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 ASP A 3 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 1 ASP A 10 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 1 ASP A 26 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 ASP A 36 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 1 ASP A 36 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 1 ASP A 52 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 1 ASP A 52 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 ASP A 2 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 2 ASP A 2 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ASP A 3 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 2 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 2 ASP A 10 CB - CG - OD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 2 ASP A 10 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 2 ASP A 26 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 2 ASP A 36 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 2 ASP A 52 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 ASP A 52 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 3 ASP A 2 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 3 ASP A 3 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 3 ASP A 10 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 3 ASP A 10 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 3 ASP A 26 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 3 ASP A 26 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 ASP A 36 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 3 ASP A 52 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 3 ASP A 52 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 4 ASP A 2 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 ASP A 2 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 4 ASP A 3 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 4 ASP A 3 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 4 ASP A 10 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 4 ASP A 10 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 4 ASP A 10 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 4 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 4 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 4 ASP A 26 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 4 ASP A 36 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 4 ASP A 52 CB - CG - OD1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 4 ASP A 52 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 5 ASP A 2 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 5 ASP A 2 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 ASP A 3 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 5 ASP A 3 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 ASP A 26 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 5 ASP A 36 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 5 ASP A 52 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 194 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 ASP A 2 -6.77 -158.34
REMARK 500 1 SER A 17 -179.28 -176.87
REMARK 500 1 SER A 43 -169.60 -60.42
REMARK 500 1 ASN A 63 -73.35 -63.58
REMARK 500 1 GLU A 65 67.01 -56.34
REMARK 500 1 ILE A 66 -47.88 -157.85
REMARK 500 2 ASP A 2 55.19 -158.75
REMARK 500 2 SER A 17 -166.43 -176.77
REMARK 500 2 VAL A 25 -11.79 -176.83
REMARK 500 2 GLU A 29 -71.47 -51.79
REMARK 500 2 SER A 43 -168.44 -60.35
REMARK 500 2 TYR A 51 48.14 -51.28
REMARK 500 2 HIS A 54 -66.88 -146.48
REMARK 500 2 LYS A 59 154.42 -49.84
REMARK 500 2 CYS A 61 51.72 -116.80
REMARK 500 2 ASN A 63 -91.38 -63.59
REMARK 500 3 ASP A 2 71.42 -158.44
REMARK 500 3 LYS A 5 37.58 -87.14
REMARK 500 3 ALA A 7 107.79 -164.17
REMARK 500 3 SER A 17 -165.33 -177.19
REMARK 500 3 GLU A 29 -85.36 -52.56
REMARK 500 3 SER A 33 -21.69 -158.69
REMARK 500 3 TYR A 42 31.50 -84.06
REMARK 500 3 SER A 43 -167.44 -60.49
REMARK 500 3 HIS A 54 -61.16 -147.19
REMARK 500 3 LYS A 55 -132.18 -94.40
REMARK 500 3 LYS A 59 151.43 -49.74
REMARK 500 3 ASN A 63 -41.37 -176.46
REMARK 500 4 ASP A 2 64.06 -158.71
REMARK 500 4 ASP A 3 49.17 -153.46
REMARK 500 4 ASP A 10 -44.62 168.78
REMARK 500 4 SER A 17 -152.86 -176.85
REMARK 500 4 VAL A 25 28.87 -176.75
REMARK 500 4 CYS A 31 -154.07 -87.51
REMARK 500 4 HIS A 32 112.90 -178.98
REMARK 500 4 ASP A 36 -133.56 -91.43
REMARK 500 4 LYS A 37 84.17 -30.88
REMARK 500 4 TYR A 42 42.35 -83.62
REMARK 500 4 SER A 43 -151.31 -60.42
REMARK 500 4 GLN A 47 76.19 -102.43
REMARK 500 4 HIS A 54 -57.13 -146.46
REMARK 500 4 LYS A 59 164.40 -49.90
REMARK 500 4 HIS A 62 53.25 -96.24
REMARK 500 5 ASP A 2 53.46 -158.64
REMARK 500 5 ASP A 3 -67.20 -156.91
REMARK 500 5 SER A 17 -177.16 -176.89
REMARK 500 5 HIS A 32 -162.69 -100.18
REMARK 500 5 LYS A 37 75.12 -100.32
REMARK 500 5 SER A 43 -172.59 -60.03
REMARK 500 5 GLN A 47 64.64 -110.90
REMARK 500
REMARK 500 THIS ENTRY HAS 216 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 VAL A 25 ASP A 26 2 139.51
REMARK 500 ARG A 28 GLU A 29 3 138.62
REMARK 500 SER A 33 ALA A 34 3 -137.29
REMARK 500 CYS A 24 VAL A 25 4 -143.82
REMARK 500 VAL A 25 ASP A 26 4 138.14
REMARK 500 ARG A 28 GLU A 29 4 149.50
REMARK 500 ASN A 44 PRO A 45 7 -31.06
REMARK 500 HIS A 54 LYS A 55 7 -146.03
REMARK 500 THR A 11 CYS A 12 9 -149.34
REMARK 500 THR A 15 ARG A 16 9 146.37
REMARK 500 ARG A 28 GLU A 29 11 149.17
REMARK 500 GLN A 47 CYS A 48 18 -148.96
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 3 TYR A 51 0.07 SIDE CHAIN
REMARK 500 4 ARG A 23 0.08 SIDE CHAIN
REMARK 500 4 TYR A 42 0.07 SIDE CHAIN
REMARK 500 7 TYR A 51 0.07 SIDE CHAIN
REMARK 500 8 TYR A 51 0.08 SIDE CHAIN
REMARK 500 13 TYR A 51 0.07 SIDE CHAIN
REMARK 500 14 ARG A 16 0.09 SIDE CHAIN
REMARK 500 17 ARG A 23 0.10 SIDE CHAIN
REMARK 500 19 ARG A 23 0.09 SIDE CHAIN
REMARK 500 19 ARG A 28 0.14 SIDE CHAIN
REMARK 500 19 TYR A 51 0.12 SIDE CHAIN
REMARK 500 20 ARG A 23 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 69
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 71
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 73
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 75
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 76
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACCORDING TO AUTHORS, THE GLU AT POSITION 110 IN THE
REMARK 999 SEQUENCE DATABASE IS MISSING.
DBREF 2AIH A 1 67 UNP Q8W4Y8 IBB_LENCU 43 109
SEQRES 1 A 67 GLY ASP ASP VAL LYS SER ALA CYS CYS ASP THR CYS LEU
SEQRES 2 A 67 CYS THR ARG SER GLN PRO PRO THR CYS ARG CYS VAL ASP
SEQRES 3 A 67 VAL ARG GLU SER CYS HIS SER ALA CYS ASP LYS CYS VAL
SEQRES 4 A 67 CYS ALA TYR SER ASN PRO PRO GLN CYS GLN CYS TYR ASP
SEQRES 5 A 67 THR HIS LYS PHE CYS TYR LYS ALA CYS HIS ASN SER GLU
SEQRES 6 A 67 ILE GLU
HET CL A 68 1
HET CL A 69 1
HET CL A 70 1
HET CL A 71 1
HET CL A 72 1
HET CL A 73 1
HET CL A 74 1
HET CL A 75 1
HET CL A 76 1
HET CL A 77 1
HET CL A 78 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL 11(CL 1-)
SHEET 1 A 2 CYS A 12 CYS A 14 0
SHEET 2 A 2 CYS A 22 CYS A 24 -1 O ARG A 23 N LEU A 13
SHEET 1 B 2 CYS A 38 ALA A 41 0
SHEET 2 B 2 GLN A 47 CYS A 50 -1 O GLN A 49 N VAL A 39
SSBOND 1 CYS A 8 CYS A 61 1555 1555 2.03
SSBOND 2 CYS A 9 CYS A 24 1555 1555 2.02
SSBOND 3 CYS A 12 CYS A 57 1555 1555 2.03
SSBOND 4 CYS A 14 CYS A 22 1555 1555 2.04
SSBOND 5 CYS A 31 CYS A 38 1555 1555 2.02
SSBOND 6 CYS A 35 CYS A 50 1555 1555 2.03
SSBOND 7 CYS A 40 CYS A 48 1555 1555 2.03
CISPEP 1 GLN A 18 PRO A 19 1 -13.61
CISPEP 2 ASN A 44 PRO A 45 1 -5.18
CISPEP 3 GLN A 18 PRO A 19 2 -10.88
CISPEP 4 ASN A 44 PRO A 45 2 -11.05
CISPEP 5 GLN A 18 PRO A 19 3 -2.12
CISPEP 6 ASN A 44 PRO A 45 3 -4.40
CISPEP 7 GLN A 18 PRO A 19 4 -10.79
CISPEP 8 ASN A 44 PRO A 45 4 -14.36
CISPEP 9 GLN A 18 PRO A 19 5 -4.41
CISPEP 10 ASN A 44 PRO A 45 5 -7.72
CISPEP 11 GLN A 18 PRO A 19 6 -20.98
CISPEP 12 ASN A 44 PRO A 45 6 -14.17
CISPEP 13 GLN A 18 PRO A 19 7 -5.82
CISPEP 14 GLN A 18 PRO A 19 8 -6.05
CISPEP 15 ASN A 44 PRO A 45 8 -10.89
CISPEP 16 GLN A 18 PRO A 19 9 0.34
CISPEP 17 ASN A 44 PRO A 45 9 -17.06
CISPEP 18 GLN A 18 PRO A 19 10 -8.43
CISPEP 19 ASN A 44 PRO A 45 10 0.31
CISPEP 20 GLN A 18 PRO A 19 11 -1.60
CISPEP 21 ASN A 44 PRO A 45 11 -7.42
CISPEP 22 GLN A 18 PRO A 19 12 -8.71
CISPEP 23 ASN A 44 PRO A 45 12 -11.74
CISPEP 24 GLN A 18 PRO A 19 13 -9.31
CISPEP 25 ASN A 44 PRO A 45 13 -3.76
CISPEP 26 GLN A 18 PRO A 19 14 -12.75
CISPEP 27 ASN A 44 PRO A 45 14 -7.99
CISPEP 28 GLN A 18 PRO A 19 15 -5.83
CISPEP 29 ASN A 44 PRO A 45 15 -0.24
CISPEP 30 GLN A 18 PRO A 19 16 9.15
CISPEP 31 ASN A 44 PRO A 45 16 -2.23
CISPEP 32 GLN A 18 PRO A 19 17 -12.29
CISPEP 33 ASN A 44 PRO A 45 17 -20.83
CISPEP 34 GLN A 18 PRO A 19 18 -14.94
CISPEP 35 ASN A 44 PRO A 45 18 -20.25
CISPEP 36 GLN A 18 PRO A 19 19 -13.30
CISPEP 37 ASN A 44 PRO A 45 19 -24.05
CISPEP 38 GLN A 18 PRO A 19 20 -1.82
CISPEP 39 ASN A 44 PRO A 45 20 -5.25
SITE 1 AC1 1 HIS A 32
SITE 1 AC2 1 HIS A 54
SITE 1 AC3 1 HIS A 54
SITE 1 AC4 1 GLY A 1
SITE 1 AC5 1 TYR A 42
SITE 1 AC6 1 ARG A 16
SITE 1 AC7 1 HIS A 62
SITE 1 AC8 1 SER A 30
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 - r 9 2 Bytes