Header list of 2bbm.pdb file
Complete list - 9 20 Bytes
HEADER CALCIUM-BINDING PROTEIN 16-JUL-92 2BBM
TITLE SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY
TITLE 2 MULTIDIMENSIONAL NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MYOSIN LIGHT CHAIN KINASE;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 ORGAN: SKELETAL;
SOURCE 6 MOL_ID: 2
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,A.BAX,M.IKURA,A.M.GRONENBORN
REVDAT 4 09-MAR-22 2BBM 1 REMARK LINK
REVDAT 3 24-FEB-09 2BBM 1 VERSN
REVDAT 2 30-SEP-03 2BBM 1 DBREF
REVDAT 1 31-JAN-94 2BBM 0
JRNL AUTH M.IKURA,G.M.CLORE,A.M.GRONENBORN,G.ZHU,C.B.KLEE,A.BAX
JRNL TITL SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY
JRNL TITL 2 MULTIDIMENSIONAL NMR.
JRNL REF SCIENCE V. 256 632 1992
JRNL REFN ISSN 0036-8075
JRNL PMID 1585175
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL
REMARK 3 STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS
REMARK 3 ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS,
REMARK 3 DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES
REMARK 3 AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES
REMARK 3 BETWEEN THE CALCULATED STRUCTURES).
REMARK 3
REMARK 3 THE STRUCTURES ARE BASED ON 1827 INTERPROTON DISTANCE
REMARK 3 RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 148
REMARK 3 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 74 HYDROGEN-BONDS
REMARK 3 IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON
REMARK 3 EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE
REMARK 3 CALCULATIONS; 24 RESTRAINTS FOR THE 4 CALCIUM IONS,
REMARK 3 AND 113 PHI TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING
REMARK 3 DATA, CONSTANTS, NOE AND 13C SECONDARY CHEMICAL SHIFTS.
REMARK 3
REMARK 3 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID
REMARK 3 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED
REMARK 3 ANNEALING METHOD [M.NILGES, G.M.CLORE, AND A.M.GRONENBORN,
REMARK 3 FEBS LETT. 229, 317-324 (1988)].
REMARK 3
REMARK 3 A TOTAL OF 21 STRUCTURES WERE CALCULATED.
REMARK 3 THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE
REMARK 3 PRESENTED IN THIS ENTRY. THIS WAS OBTAINED BY AVERAGING
REMARK 3 THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING
REMARK 3 THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE
REMARK 3 COORDINATES OF THE 21 INDIVIDUAL SA STRUCTURES ARE
REMARK 3 PRESENTED IN PROTEIN DATA BANK ENTRY 2BBN.
REMARK 3
REMARK 3 THE LAST COLUMN IN THIS COORDINATE FILE REPRESENTS THE
REMARK 3 ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE
REMARK 3 MEAN COORDINATE POSITIONS.
REMARK 4
REMARK 4 2BBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177813.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HIS A 107 CG HIS A 107 ND1 -0.114
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 ARG A 74 CG - CD - NE ANGL. DEV. = 17.3 DEGREES
REMARK 500 TRP B 4 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP B 4 CD1 - NE1 - CE2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP B 4 NE1 - CE2 - CZ2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 TRP B 4 NE1 - CE2 - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 LYS B 18 CD - CE - NZ ANGL. DEV. = 19.8 DEGREES
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 THR A 5 -84.52 -88.21
REMARK 500 GLU A 6 13.23 46.70
REMARK 500 LEU A 39 -36.12 -132.70
REMARK 500 GLN A 41 171.09 70.92
REMARK 500 PRO A 43 -100.23 -63.41
REMARK 500 ASP A 56 106.08 -58.85
REMARK 500 ASP A 58 -70.58 -59.78
REMARK 500 ASN A 60 -7.76 -54.50
REMARK 500 ASP A 64 -154.42 -111.83
REMARK 500 LYS A 77 -14.63 -46.28
REMARK 500 ASP A 78 129.09 -27.58
REMARK 500 THR A 79 126.66 -8.74
REMARK 500 SER A 81 58.06 -98.76
REMARK 500 GLU A 82 -19.13 -43.21
REMARK 500 ASP A 95 -87.16 -48.61
REMARK 500 GLU A 104 -71.23 -42.84
REMARK 500 ARG A 106 -35.45 -36.77
REMARK 500 THR A 117 -174.75 -51.97
REMARK 500 GLU A 120 -71.07 -43.02
REMARK 500 ASP A 131 -80.12 -72.92
REMARK 500 ASN A 137 -169.82 -109.59
REMARK 500 SER B 21 91.39 -54.78
REMARK 500 SER B 22 88.72 -55.44
REMARK 500 SER B 23 102.95 25.22
REMARK 500 ALA B 25 -38.60 -35.62
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 ARG A 37 0.18 SIDE CHAIN
REMARK 500 ARG A 74 0.24 SIDE CHAIN
REMARK 500 ARG A 86 0.30 SIDE CHAIN
REMARK 500 ARG A 106 0.30 SIDE CHAIN
REMARK 500 ARG A 126 0.32 SIDE CHAIN
REMARK 500 ARG B 2 0.31 SIDE CHAIN
REMARK 500 ARG B 3 0.31 SIDE CHAIN
REMARK 500 ARG B 16 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 181 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD2 68.0
REMARK 620 3 ASP A 24 OD1 87.0 88.1
REMARK 620 4 THR A 26 O 115.3 150.4 120.9
REMARK 620 5 GLU A 31 OE1 82.9 102.6 161.1 51.4
REMARK 620 6 GLU A 31 OE2 134.3 83.2 128.2 74.5 69.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 182 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 82.3
REMARK 620 3 ASN A 60 OD1 111.9 91.0
REMARK 620 4 THR A 62 O 70.1 150.1 109.4
REMARK 620 5 GLU A 67 OE1 74.8 82.4 170.0 79.6
REMARK 620 6 GLU A 67 OE2 125.6 66.3 111.9 121.3 58.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 183 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 93.9
REMARK 620 3 ASN A 97 OD1 105.1 77.4
REMARK 620 4 PHE A 99 O 62.1 153.7 117.4
REMARK 620 5 GLU A 104 OE1 76.0 72.6 149.9 90.1
REMARK 620 6 GLU A 104 OE2 126.6 101.5 128.1 86.3 61.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 184 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 129 OD2 59.5
REMARK 620 3 ASP A 131 OD1 104.2 72.3
REMARK 620 4 ASP A 133 OD2 147.3 87.8 60.0
REMARK 620 5 GLN A 135 O 68.8 93.0 165.2 118.7
REMARK 620 6 GLU A 140 OE1 89.0 147.6 112.4 123.0 81.1
REMARK 620 7 GLU A 140 OE2 71.1 102.2 66.3 118.8 120.7 56.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 184
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BBN RELATED DB: PDB
DBREF 2BBM A 1 148 UNP P62152 CALM_DROME 1 148
DBREF 2BBM B 1 26 UNP P07313 MYLK2_RABIT 577 602
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY PHE ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL THR
SEQRES 12 A 148 MET MET THR SER LYS
SEQRES 1 B 26 LYS ARG ARG TRP LYS LYS ASN PHE ILE ALA VAL SER ALA
SEQRES 2 B 26 ALA ASN ARG PHE LYS LYS ILE SER SER SER GLY ALA LEU
HET CA A 181 1
HET CA A 182 1
HET CA A 183 1
HET CA A 184 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
HELIX 1 1 GLU A 6 ASP A 20 1 15
HELIX 2 2 THR A 28 GLN A 41 1 14
HELIX 3 3 GLU A 45 GLU A 54 1 10
HELIX 4 4 ASP A 64 ARG A 74 1 11
HELIX 5 5 GLU A 82 ASP A 93 1 12
HELIX 6 6 SER A 101 LEU A 112 1 12
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 ASN A 137 THR A 146 1 10
HELIX 9 9 ARG B 3 ILE B 20 1 18
LINK OD1 ASP A 20 CA CA A 181 1555 1555 1.71
LINK OD2 ASP A 22 CA CA A 181 1555 1555 2.41
LINK OD1 ASP A 24 CA CA A 181 1555 1555 1.73
LINK O THR A 26 CA CA A 181 1555 1555 3.02
LINK OE1 GLU A 31 CA CA A 181 1555 1555 1.86
LINK OE2 GLU A 31 CA CA A 181 1555 1555 1.98
LINK OD1 ASP A 56 CA CA A 182 1555 1555 2.45
LINK OD1 ASP A 58 CA CA A 182 1555 1555 2.20
LINK OD1 ASN A 60 CA CA A 182 1555 1555 2.08
LINK O THR A 62 CA CA A 182 1555 1555 3.04
LINK OE1 GLU A 67 CA CA A 182 1555 1555 2.33
LINK OE2 GLU A 67 CA CA A 182 1555 1555 2.13
LINK OD1 ASP A 93 CA CA A 183 1555 1555 2.30
LINK OD1 ASP A 95 CA CA A 183 1555 1555 2.04
LINK OD1 ASN A 97 CA CA A 183 1555 1555 1.73
LINK O PHE A 99 CA CA A 183 1555 1555 3.17
LINK OE1 GLU A 104 CA CA A 183 1555 1555 1.97
LINK OE2 GLU A 104 CA CA A 183 1555 1555 2.29
LINK OD1 ASP A 129 CA CA A 184 1555 1555 1.83
LINK OD2 ASP A 129 CA CA A 184 1555 1555 2.44
LINK OD1 ASP A 131 CA CA A 184 1555 1555 2.73
LINK OD2 ASP A 133 CA CA A 184 1555 1555 1.88
LINK O GLN A 135 CA CA A 184 1555 1555 3.07
LINK OE1 GLU A 140 CA CA A 184 1555 1555 2.09
LINK OE2 GLU A 140 CA CA A 184 1555 1555 2.48
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 5 GLU A 67
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 PHE A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 5 GLU A 140
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 - 9 20 Bytes