Header list of 1htx.pdb file
Complete list - 23 20 Bytes
HEADER PLANT PROTEIN 02-JAN-01 1HTX
TITLE SOLUTION STRUCTURE OF THE MAIN ALPHA-AMYLASE INHIBITOR FROM AMARANTH
TITLE 2 SEEDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE INHIBITOR AAI;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AMARANTHUS HYPOCHONDRIACUS;
SOURCE 3 ORGANISM_COMMON: GRAIN AMARANTH;
SOURCE 4 ORGANISM_TAXID: 28502;
SOURCE 5 ORGAN: SEEDS
KEYWDS CYSTEINE KNOT, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.C.MARTINS,M.ENASSAR,R.WILLEM,J.M.WIERUZESKI,G.LIPPENS,S.J.WODAK
REVDAT 4 23-FEB-22 1HTX 1 REMARK
REVDAT 3 24-FEB-09 1HTX 1 VERSN
REVDAT 2 01-APR-03 1HTX 1 JRNL
REVDAT 1 18-JUL-01 1HTX 0
JRNL AUTH J.C.MARTINS,M.ENASSAR,R.WILLEM,J.M.WIERUZESKI,G.LIPPENS,
JRNL AUTH 2 S.J.WODAK
JRNL TITL SOLUTION STRUCTURE OF THE MAIN ALPHA-AMYLASE INHIBITOR FROM
JRNL TITL 2 AMARANTH SEEDS.
JRNL REF EUR.J.BIOCHEM. V. 268 2379 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11298757
JRNL DOI 10.1046/J.1432-1327.2001.02118.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, NMR_REFINE 98.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), MSI (NMR_REFINE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED MD AT 1000K FOLLWED BY
REMARK 3 STEPWISE COOLING TO 300K AND FINAL RESTRAINED ENERGY OPTIMISATION
REMARK 4
REMARK 4 1HTX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012582.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277; 277
REMARK 210 PH : 2.95; 2.95
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8 MM AAI, 0.05 MM NAN3; 1.8 MM
REMARK 210 AAI, 0.05 MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; AMX; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY,STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED FROM 2D 1H NMR TECHNIQUES
REMARK 210 ONLY USING THE SEQUENCE SPECIFIC RESONANCE ASSIGNMENT PROCEDURE,
REMARK 210 FOLLOWED BY NOE AND J DATA COLLECTION, CALCULATION BIJ X-PLOR
REMARK 210 AND REFINEMENT WITH MSI'S CVFF FORCEFIELD
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 1 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 1 SER A 32 C SER A 32 OXT 0.147
REMARK 500 2 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 2 SER A 32 C SER A 32 OXT 0.140
REMARK 500 3 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 3 SER A 32 C SER A 32 OXT 0.145
REMARK 500 4 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 4 SER A 32 C SER A 32 OXT 0.141
REMARK 500 5 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 5 SER A 32 C SER A 32 OXT 0.145
REMARK 500 6 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 6 SER A 32 C SER A 32 OXT 0.146
REMARK 500 7 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 7 SER A 32 C SER A 32 OXT 0.138
REMARK 500 8 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 8 SER A 32 C SER A 32 OXT 0.145
REMARK 500 9 GLU A 19 CD GLU A 19 OE2 0.121
REMARK 500 9 SER A 32 C SER A 32 OXT 0.147
REMARK 500 10 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 10 SER A 32 C SER A 32 OXT 0.140
REMARK 500 11 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 11 SER A 32 C SER A 32 OXT 0.140
REMARK 500 12 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 12 SER A 32 C SER A 32 OXT 0.138
REMARK 500 13 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 13 SER A 32 C SER A 32 OXT 0.147
REMARK 500 14 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 14 SER A 32 C SER A 32 OXT 0.145
REMARK 500 15 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 15 SER A 32 C SER A 32 OXT 0.140
REMARK 500 16 GLU A 19 CD GLU A 19 OE2 0.120
REMARK 500 16 SER A 32 C SER A 32 OXT 0.143
REMARK 500 17 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 17 SER A 32 C SER A 32 OXT 0.141
REMARK 500 18 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 18 SER A 32 C SER A 32 OXT 0.146
REMARK 500 19 GLU A 19 CD GLU A 19 OE2 0.121
REMARK 500 19 SER A 32 C SER A 32 OXT 0.147
REMARK 500 20 GLU A 19 CD GLU A 19 OE2 0.119
REMARK 500 20 SER A 32 C SER A 32 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 TRP A 5 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 TRP A 5 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ASP A 13 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ASP A 26 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 ASP A 13 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 3 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 TRP A 5 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 4 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ASP A 13 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 5 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 6 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 7 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ASP A 13 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 7 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 7 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 8 TRP A 5 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 ASP A 13 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 8 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 9 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 9 ASP A 13 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 9 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 9 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 10 TRP A 5 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 10 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 10 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 11 TRP A 5 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 11 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 11 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 12 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 12 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 12 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 13 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 13 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 13 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 14 ARG A 7 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 14 ASP A 13 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 14 ASP A 13 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 14 ASP A 26 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 74 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 PRO A 3 -175.29 -66.37
REMARK 500 1 MET A 12 -63.33 -103.29
REMARK 500 1 THR A 24 50.59 -91.27
REMARK 500 1 ASP A 26 -57.91 -136.72
REMARK 500 2 PRO A 3 -177.57 -66.44
REMARK 500 2 PRO A 16 174.26 -59.44
REMARK 500 2 THR A 24 49.85 -92.74
REMARK 500 2 ASP A 26 -67.45 -137.46
REMARK 500 3 MET A 12 -67.96 -97.76
REMARK 500 3 THR A 24 55.39 -93.62
REMARK 500 3 ASP A 26 -59.30 -133.21
REMARK 500 4 PRO A 3 -178.62 -65.82
REMARK 500 4 MET A 12 -65.27 -93.68
REMARK 500 4 THR A 24 40.50 -90.15
REMARK 500 4 ASP A 26 -63.56 -141.22
REMARK 500 4 ASN A 30 147.33 -174.20
REMARK 500 5 ASP A 13 17.33 -142.50
REMARK 500 5 THR A 24 41.86 -90.58
REMARK 500 5 ASP A 26 -69.78 -134.02
REMARK 500 5 ASN A 30 149.07 -173.10
REMARK 500 6 MET A 12 -68.83 -98.44
REMARK 500 6 THR A 24 56.46 -95.22
REMARK 500 6 ASP A 26 -62.84 -144.73
REMARK 500 7 MET A 12 -68.52 -97.05
REMARK 500 7 THR A 24 54.76 -92.74
REMARK 500 7 ASP A 26 -56.09 -135.05
REMARK 500 8 PRO A 16 173.28 -59.44
REMARK 500 8 THR A 24 48.65 -92.11
REMARK 500 8 ASP A 26 -69.75 -134.66
REMARK 500 9 MET A 12 -69.36 -101.91
REMARK 500 9 PRO A 16 175.05 -54.08
REMARK 500 9 ASP A 26 -60.99 -130.32
REMARK 500 9 ASN A 30 149.15 -175.19
REMARK 500 10 PRO A 3 -178.75 -65.66
REMARK 500 10 MET A 12 -66.75 -95.19
REMARK 500 10 THR A 24 49.34 -93.03
REMARK 500 10 ASP A 26 -66.73 -137.85
REMARK 500 11 PRO A 3 -175.25 -65.89
REMARK 500 11 MET A 12 -63.03 -101.84
REMARK 500 11 ASP A 26 -60.18 -130.65
REMARK 500 11 ASN A 30 146.23 -175.88
REMARK 500 12 PRO A 16 174.54 -57.99
REMARK 500 12 CYS A 23 106.92 -59.35
REMARK 500 12 THR A 24 56.58 -95.03
REMARK 500 12 ASP A 26 -67.84 -140.33
REMARK 500 13 TRP A 5 65.68 64.18
REMARK 500 13 MET A 12 -64.97 -93.09
REMARK 500 13 THR A 24 33.33 -83.91
REMARK 500 13 ASP A 26 -73.59 -136.29
REMARK 500 14 MET A 12 -69.09 -101.46
REMARK 500
REMARK 500 THIS ENTRY HAS 77 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 3 TYR A 21 0.07 SIDE CHAIN
REMARK 500 7 TYR A 21 0.07 SIDE CHAIN
REMARK 500 9 TYR A 21 0.07 SIDE CHAIN
REMARK 500 12 TYR A 21 0.07 SIDE CHAIN
REMARK 500 13 TYR A 21 0.07 SIDE CHAIN
REMARK 500 15 TYR A 21 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QFD RELATED DB: PDB
REMARK 900 ALPHA-AMYLASE INHIBITOR INDEPENDANTLY DETERMINED NMR SOLUTION
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1CLV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE AMARANTH ALPHA-AMYLASE INHIBITOR IN
REMARK 900 COMPLEX WITH THE ALPHA-AMYLASE FROM THE YELLOW MEALWORM AT 2.00 A
REMARK 900 RESOLUTION
DBREF 1HTX A 1 32 UNP P80403 IAAI_AMAHP 1 32
SEQRES 1 A 32 CYS ILE PRO LYS TRP ASN ARG CYS GLY PRO LYS MET ASP
SEQRES 2 A 32 GLY VAL PRO CYS CYS GLU PRO TYR THR CYS THR SER ASP
SEQRES 3 A 32 TYR TYR GLY ASN CYS SER
SHEET 1 A 2 ARG A 7 CYS A 8 0
SHEET 2 A 2 GLY A 29 ASN A 30 -1 N GLY A 29 O CYS A 8
SSBOND 1 CYS A 1 CYS A 18 1555 1555 1.99
SSBOND 2 CYS A 8 CYS A 23 1555 1555 1.99
SSBOND 3 CYS A 17 CYS A 31 1555 1555 1.96
CISPEP 1 GLU A 19 PRO A 20 1 6.78
CISPEP 2 GLU A 19 PRO A 20 2 6.68
CISPEP 3 GLU A 19 PRO A 20 3 6.48
CISPEP 4 GLU A 19 PRO A 20 4 6.67
CISPEP 5 GLU A 19 PRO A 20 5 6.45
CISPEP 6 GLU A 19 PRO A 20 6 6.34
CISPEP 7 GLU A 19 PRO A 20 7 6.57
CISPEP 8 GLU A 19 PRO A 20 8 6.61
CISPEP 9 GLU A 19 PRO A 20 9 6.47
CISPEP 10 GLU A 19 PRO A 20 10 6.74
CISPEP 11 GLU A 19 PRO A 20 11 6.83
CISPEP 12 GLU A 19 PRO A 20 12 6.55
CISPEP 13 GLU A 19 PRO A 20 13 6.45
CISPEP 14 GLU A 19 PRO A 20 14 5.68
CISPEP 15 GLU A 19 PRO A 20 15 6.50
CISPEP 16 GLU A 19 PRO A 20 16 6.49
CISPEP 17 GLU A 19 PRO A 20 17 6.74
CISPEP 18 GLU A 19 PRO A 20 18 6.82
CISPEP 19 GLU A 19 PRO A 20 19 6.70
CISPEP 20 GLU A 19 PRO A 20 20 6.70
CRYST1 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