Header list of 1bv8.pdb file
Complete list - 16 20 Bytes
HEADER PROTEIN BINDING 22-SEP-98 1BV8
TITLE RECEPTOR DOMAIN FROM ALPHA-2-MACROGLOBULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-2-MACROGLOBULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RECEPTOR BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PROTEINASE, PROTEIN BINDING
EXPDTA SOLUTION NMR
AUTHOR W.HUANG,K.DOLMER,X.LIAO,P.G.W.GETTINS
REVDAT 5 16-FEB-22 1BV8 1 REMARK
REVDAT 4 24-FEB-09 1BV8 1 VERSN
REVDAT 3 01-APR-03 1BV8 1 JRNL
REVDAT 2 05-APR-00 1BV8 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 05-APR-00 1BV8 0
JRNL AUTH W.HUANG,K.DOLMER,P.G.GETTINS
JRNL TITL NMR SOLUTION STRUCTURE OF COMPLEMENT-LIKE REPEAT CR8 FROM
JRNL TITL 2 THE LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN.
JRNL REF J.BIOL.CHEM. V. 274 14130 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10318830
JRNL DOI 10.1074/JBC.274.20.14130
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, DYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BV8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000008433.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : 0.4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 MEAN STRUCTURE. THE STRUCTURE WAS DETERMINED USING TRIPLE-
REMARK 210 RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED UTEROGLOBIN.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLU A 1 N
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 C ASP A 100 H VAL A 101 0.22
REMARK 500 O ASP A 100 N VAL A 101 0.25
REMARK 500 O ASP A 115 N TYR A 116 0.48
REMARK 500 C ASP A 115 H TYR A 116 0.49
REMARK 500 HB3 ASN A 137 N ALA A 138 0.51
REMARK 500 CG ASN A 137 N ALA A 138 0.55
REMARK 500 C LEU A 135 H GLY A 136 0.59
REMARK 500 HB3 ASN A 137 H ALA A 138 0.59
REMARK 500 O LYS A 85 N VAL A 86 0.60
REMARK 500 C LYS A 85 H VAL A 86 0.61
REMARK 500 O ASP A 100 H VAL A 101 0.63
REMARK 500 CG ASN A 137 H ALA A 138 0.63
REMARK 500 HD1 TYR A 117 H GLU A 118 0.64
REMARK 500 O ASP A 115 H TYR A 116 0.65
REMARK 500 O LYS A 85 H VAL A 86 0.65
REMARK 500 O LEU A 135 N GLY A 136 0.66
REMARK 500 OD1 ASN A 137 N ALA A 138 0.68
REMARK 500 O ASN A 41 N MET A 42 0.70
REMARK 500 C ASN A 41 H MET A 42 0.70
REMARK 500 ND2 ASN A 137 N ALA A 138 0.70
REMARK 500 HD21 ASN A 137 CA ALA A 138 0.70
REMARK 500 HD21 ASN A 137 HA ALA A 138 0.71
REMARK 500 ND2 ASN A 137 HA ALA A 138 0.71
REMARK 500 C ASP A 134 H LEU A 135 0.72
REMARK 500 ND2 ASN A 137 H ALA A 138 0.72
REMARK 500 O ASP A 134 N LEU A 135 0.74
REMARK 500 HD21 ASN A 137 N ALA A 138 0.75
REMARK 500 HD21 ASN A 137 H ALA A 138 0.75
REMARK 500 HD22 ASN A 137 CA ALA A 138 0.75
REMARK 500 ND2 ASN A 137 CA ALA A 138 0.75
REMARK 500 C ASN A 137 H ALA A 138 0.75
REMARK 500 OD1 ASN A 137 H ALA A 138 0.77
REMARK 500 O ASN A 41 H MET A 42 0.77
REMARK 500 O ASN A 137 N ALA A 138 0.78
REMARK 500 C GLU A 118 H THR A 119 0.80
REMARK 500 C THR A 119 H ASP A 120 0.81
REMARK 500 C VAL A 86 H SER A 87 0.81
REMARK 500 HD22 ASN A 137 HA ALA A 138 0.82
REMARK 500 O VAL A 86 N SER A 87 0.83
REMARK 500 O GLU A 118 N THR A 119 0.84
REMARK 500 O THR A 119 N ASP A 120 0.84
REMARK 500 CB ASN A 137 N ALA A 138 0.85
REMARK 500 HD21 ASN A 137 HB2 ALA A 138 0.85
REMARK 500 O ASN A 137 H ALA A 138 0.86
REMARK 500 O ASP A 134 H LEU A 135 0.88
REMARK 500 C ALA A 39 H SER A 40 0.89
REMARK 500 HD21 ASN A 137 CB ALA A 138 0.89
REMARK 500 C CYS A 131 H SER A 132 0.89
REMARK 500 O CYS A 131 N SER A 132 0.90
REMARK 500 C SER A 66 H ASN A 67 0.90
REMARK 500
REMARK 500 THIS ENTRY HAS 295 CLOSE CONTACTS
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 GLU A 1 CA GLU A 1 CB -0.576
REMARK 500 GLU A 1 CB GLU A 1 CG -0.613
REMARK 500 GLU A 1 CG GLU A 1 CD -0.587
REMARK 500 GLU A 1 CD GLU A 1 OE1 -0.891
REMARK 500 GLU A 1 CD GLU A 1 OE2 -0.762
REMARK 500 GLU A 1 CA GLU A 1 C -0.561
REMARK 500 GLU A 1 C GLU A 1 O -0.875
REMARK 500 GLU A 1 C GLU A 2 N -0.438
REMARK 500 GLU A 2 N GLU A 2 CA -0.489
REMARK 500 GLU A 2 CA GLU A 2 CB -0.939
REMARK 500 GLU A 2 CB GLU A 2 CG -1.084
REMARK 500 GLU A 2 CG GLU A 2 CD -0.959
REMARK 500 GLU A 2 CD GLU A 2 OE1 -0.763
REMARK 500 GLU A 2 CD GLU A 2 OE2 -0.927
REMARK 500 GLU A 2 CA GLU A 2 C -0.425
REMARK 500 GLU A 2 C GLU A 2 O -1.035
REMARK 500 GLU A 2 C PHE A 3 N -0.268
REMARK 500 PHE A 3 N PHE A 3 CA -0.337
REMARK 500 PHE A 3 CA PHE A 3 CB -0.717
REMARK 500 PHE A 3 CB PHE A 3 CG -0.778
REMARK 500 PHE A 3 CG PHE A 3 CD2 -1.252
REMARK 500 PHE A 3 CG PHE A 3 CD1 -0.747
REMARK 500 PHE A 3 CD1 PHE A 3 CE1 -0.710
REMARK 500 PHE A 3 CE1 PHE A 3 CZ -1.237
REMARK 500 PHE A 3 CZ PHE A 3 CE2 -0.734
REMARK 500 PHE A 3 CE2 PHE A 3 CD2 -0.710
REMARK 500 PHE A 3 CA PHE A 3 C -0.513
REMARK 500 PHE A 3 C PHE A 3 O -0.395
REMARK 500 PHE A 3 C PRO A 4 N -0.533
REMARK 500 PRO A 4 N PRO A 4 CA -0.522
REMARK 500 PRO A 4 CA PRO A 4 CB -0.505
REMARK 500 PRO A 4 CB PRO A 4 CG -0.517
REMARK 500 PRO A 4 CG PRO A 4 CD -0.619
REMARK 500 PRO A 4 CD PRO A 4 N -0.488
REMARK 500 PHE A 5 CB PHE A 5 CG -0.234
REMARK 500 PHE A 5 CG PHE A 5 CD2 -0.867
REMARK 500 PHE A 5 CG PHE A 5 CD1 -0.750
REMARK 500 PHE A 5 CD1 PHE A 5 CE1 -0.204
REMARK 500 PHE A 5 CE1 PHE A 5 CZ -0.854
REMARK 500 PHE A 5 CZ PHE A 5 CE2 -0.737
REMARK 500 PHE A 5 CE2 PHE A 5 CD2 -0.205
REMARK 500 LEU A 7 CB LEU A 7 CG -0.202
REMARK 500 LEU A 7 CG LEU A 7 CD1 -0.368
REMARK 500 LEU A 7 CG LEU A 7 CD2 -0.409
REMARK 500 VAL A 9 CB VAL A 9 CG1 -0.616
REMARK 500 VAL A 9 CB VAL A 9 CG2 -0.605
REMARK 500 GLN A 10 CG GLN A 10 CD -0.363
REMARK 500 GLN A 10 CD GLN A 10 OE1 -0.747
REMARK 500 GLN A 10 CD GLN A 10 NE2 -0.654
REMARK 500 LEU A 12 CG LEU A 12 CD1 -0.839
REMARK 500
REMARK 500 THIS ENTRY HAS 578 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 GLU A 1 CB - CA - C ANGL. DEV. = 23.7 DEGREES
REMARK 500 GLU A 1 CA - CB - CG ANGL. DEV. = 32.8 DEGREES
REMARK 500 GLU A 1 CB - CG - CD ANGL. DEV. = 33.5 DEGREES
REMARK 500 GLU A 1 OE1 - CD - OE2 ANGL. DEV. = -56.8 DEGREES
REMARK 500 GLU A 1 CG - CD - OE1 ANGL. DEV. = 24.2 DEGREES
REMARK 500 GLU A 1 CG - CD - OE2 ANGL. DEV. = 32.7 DEGREES
REMARK 500 GLU A 1 CA - C - O ANGL. DEV. = -30.8 DEGREES
REMARK 500 GLU A 1 CA - C - N ANGL. DEV. = 36.4 DEGREES
REMARK 500 GLU A 2 C - N - CA ANGL. DEV. = 34.8 DEGREES
REMARK 500 GLU A 2 N - CA - CB ANGL. DEV. = -30.9 DEGREES
REMARK 500 GLU A 2 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 GLU A 2 CG - CD - OE1 ANGL. DEV. = 24.2 DEGREES
REMARK 500 GLU A 2 CG - CD - OE2 ANGL. DEV. = -24.8 DEGREES
REMARK 500 GLU A 2 N - CA - C ANGL. DEV. = 38.0 DEGREES
REMARK 500 GLU A 2 CA - C - O ANGL. DEV. = -71.7 DEGREES
REMARK 500 GLU A 2 CA - C - N ANGL. DEV. = 54.0 DEGREES
REMARK 500 GLU A 2 O - C - N ANGL. DEV. = 17.7 DEGREES
REMARK 500 PHE A 3 C - N - CA ANGL. DEV. = 50.5 DEGREES
REMARK 500 PHE A 3 CB - CA - C ANGL. DEV. = -27.0 DEGREES
REMARK 500 PHE A 3 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 PHE A 3 CA - CB - CG ANGL. DEV. = -25.8 DEGREES
REMARK 500 PHE A 3 CB - CG - CD2 ANGL. DEV. = -18.4 DEGREES
REMARK 500 PHE A 3 CD1 - CG - CD2 ANGL. DEV. = -29.0 DEGREES
REMARK 500 PHE A 3 CB - CG - CD1 ANGL. DEV. = 47.5 DEGREES
REMARK 500 PHE A 3 CG - CD1 - CE1 ANGL. DEV. = 47.6 DEGREES
REMARK 500 PHE A 3 CG - CD2 - CE2 ANGL. DEV. = -18.4 DEGREES
REMARK 500 PHE A 3 CD1 - CE1 - CZ ANGL. DEV. = -17.7 DEGREES
REMARK 500 PHE A 3 CE1 - CZ - CE2 ANGL. DEV. = -30.8 DEGREES
REMARK 500 PHE A 3 CZ - CE2 - CD2 ANGL. DEV. = 48.3 DEGREES
REMARK 500 PHE A 3 N - CA - C ANGL. DEV. = 23.5 DEGREES
REMARK 500 PRO A 4 CA - N - CD ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO A 4 CB - CA - C ANGL. DEV. = 14.4 DEGREES
REMARK 500 PRO A 4 N - CA - CB ANGL. DEV. = -15.3 DEGREES
REMARK 500 PRO A 4 CA - CB - CG ANGL. DEV. = 11.8 DEGREES
REMARK 500 PHE A 5 CB - CG - CD2 ANGL. DEV. = 49.8 DEGREES
REMARK 500 PHE A 5 CD1 - CG - CD2 ANGL. DEV. = 101.3 DEGREES
REMARK 500 PHE A 5 CB - CG - CD1 ANGL. DEV. = 51.6 DEGREES
REMARK 500 PHE A 5 CG - CD1 - CE1 ANGL. DEV. = 51.6 DEGREES
REMARK 500 PHE A 5 CG - CD2 - CE2 ANGL. DEV. = 49.8 DEGREES
REMARK 500 PHE A 5 CD1 - CE1 - CZ ANGL. DEV. = 50.5 DEGREES
REMARK 500 PHE A 5 CE1 - CZ - CE2 ANGL. DEV. = 103.0 DEGREES
REMARK 500 PHE A 5 CZ - CE2 - CD2 ANGL. DEV. = 52.3 DEGREES
REMARK 500 VAL A 9 CG1 - CB - CG2 ANGL. DEV. = -26.2 DEGREES
REMARK 500 VAL A 9 CA - CB - CG1 ANGL. DEV. = 18.8 DEGREES
REMARK 500 VAL A 9 CA - CB - CG2 ANGL. DEV. = 19.7 DEGREES
REMARK 500 GLN A 10 OE1 - CD - NE2 ANGL. DEV. = -44.2 DEGREES
REMARK 500 GLN A 10 CG - CD - OE1 ANGL. DEV. = 15.9 DEGREES
REMARK 500 GLN A 10 CG - CD - NE2 ANGL. DEV. = 28.0 DEGREES
REMARK 500 LEU A 12 CD1 - CG - CD2 ANGL. DEV. = -76.8 DEGREES
REMARK 500 LEU A 12 CB - CG - CD1 ANGL. DEV. = 53.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 495 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 PHE A 3 109.38 176.82
REMARK 500 PRO A 4 -105.39 -66.28
REMARK 500 GLN A 14 -42.36 67.24
REMARK 500 THR A 15 138.98 175.12
REMARK 500 CYS A 16 79.23 -103.44
REMARK 500 ASP A 17 -5.28 -173.37
REMARK 500 SER A 38 3.83 -57.80
REMARK 500 SER A 40 123.44 32.59
REMARK 500 ASN A 41 68.30 -44.90
REMARK 500 VAL A 50 63.69 -2.80
REMARK 500 SER A 51 62.76 -58.76
REMARK 500 ASN A 67 34.21 175.45
REMARK 500 SER A 70 96.70 48.55
REMARK 500 SER A 75 33.01 -96.01
REMARK 500 SER A 76 -49.61 68.95
REMARK 500 LYS A 85 43.48 172.47
REMARK 500 ASN A 88 22.43 125.47
REMARK 500 ASP A 100 -63.66 -149.47
REMARK 500 ASP A 115 -9.63 -140.54
REMARK 500 TYR A 116 142.81 135.68
REMARK 500 TYR A 117 -164.54 61.82
REMARK 500 GLU A 118 -123.82 -38.35
REMARK 500 ASP A 120 79.74 88.44
REMARK 500 GLU A 121 92.85 -179.45
REMARK 500 CYS A 131 39.81 119.14
REMARK 500 LYS A 133 138.87 -177.36
REMARK 500 ASN A 137 111.60 163.84
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BV8 A 1 138 UNP P01023 A2MG_HUMAN 1337 1474
SEQRES 1 A 138 GLU GLU PHE PRO PHE ALA LEU GLY VAL GLN THR LEU PRO
SEQRES 2 A 138 GLN THR CYS ASP GLU PRO LYS ALA HIS THR SER PHE GLN
SEQRES 3 A 138 ILE SER LEU SER VAL SER TYR THR GLY SER ARG SER ALA
SEQRES 4 A 138 SER ASN MET ALA ILE VAL ASP VAL LYS MET VAL SER GLY
SEQRES 5 A 138 PHE ILE PRO LEU LYS PRO THR VAL LYS MET LEU GLU ARG
SEQRES 6 A 138 SER ASN HIS VAL SER ARG THR GLU VAL SER SER ASN HIS
SEQRES 7 A 138 VAL LEU ILE TYR LEU ASP LYS VAL SER ASN GLN THR LEU
SEQRES 8 A 138 SER LEU PHE PHE THR VAL LEU GLN ASP VAL PRO VAL ARG
SEQRES 9 A 138 ASP LEU LYS PRO ALA ILE VAL LYS VAL TYR ASP TYR TYR
SEQRES 10 A 138 GLU THR ASP GLU PHE ALA ILE ALA GLU TYR ASN ALA PRO
SEQRES 11 A 138 CYS SER LYS ASP LEU GLY ASN ALA
HELIX 1 1 GLU A 18 THR A 23 1 6
HELIX 2 2 LEU A 56 ARG A 65 1 10
SHEET 1 A 4 PHE A 5 THR A 11 0
SHEET 2 A 4 SER A 24 TYR A 33 -1 N SER A 28 O GLN A 10
SHEET 3 A 4 LEU A 91 LEU A 98 -1 O LEU A 91 N VAL A 31
SHEET 4 A 4 ILE A 54 PRO A 55 -1 N ILE A 54 O LEU A 98
SHEET 1 B 5 ARG A 71 VAL A 74 0
SHEET 2 B 5 HIS A 78 LEU A 83 -1 N LEU A 80 O GLU A 73
SHEET 3 B 5 ALA A 43 LYS A 48 -1 N ALA A 43 O LEU A 83
SHEET 4 B 5 ALA A 109 TYR A 114 -1 O ILE A 110 N LYS A 48
SHEET 5 B 5 ALA A 123 TYR A 127 -1 O ALA A 123 N VAL A 113
SSBOND 1 CYS A 16 CYS A 131 1555 1555 1.35
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
Complete list - 16 20 Bytes